FAT3_MOUSE
ID FAT3_MOUSE Reviewed; 4555 AA.
AC Q8BNA6; Q08ED4;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Protocadherin Fat 3;
DE AltName: Full=FAT tumor suppressor homolog 3;
DE Flags: Precursor;
GN Name=Fat3; Synonyms=Gm1132, Gm510;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1464-4555 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP POSSIBLE FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16059920; DOI=10.1002/dvdy.20515;
RA Rock R., Schrauth S., Gessler M.;
RT "Expression of mouse dchs1, fjx1, and fat-j suggests conservation of the
RT planar cell polarity pathway identified in Drosophila.";
RL Dev. Dyn. 234:747-755(2005).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=17131403; DOI=10.1002/dvdy.21030;
RA Nagae S., Tanoue T., Takeichi M.;
RT "Temporal and spatial expression profiles of the Fat3 protein, a giant
RT cadherin molecule, during mouse development.";
RL Dev. Dyn. 236:534-543(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-4508 AND ARG-4518, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: May play a role in the interactions between neurites derived
CC from specific subsets of neurons during development.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BNA6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BNA6-2; Sequence=VSP_032330, VSP_032331;
CC Name=3;
CC IsoId=Q8BNA6-3; Sequence=VSP_032329, VSP_032332, VSP_032333;
CC -!- TISSUE SPECIFICITY: Restricted to the nervous system, mainly in brain.
CC In brain, it is highly expressed in the olfactory bulb and retina. In
CC the developing olfactory bulb, it localizes along the dendrites of
CC these cells as well as in their axons to some extent. In retina, it
CC cocentrates in the inner plexiform layer throughout development (at
CC protein level). {ECO:0000269|PubMed:16059920,
CC ECO:0000269|PubMed:17131403}.
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DR EMBL; AC154406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC162903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117744; AAI17745.1; -; mRNA.
DR EMBL; AK084245; BAC39147.1; -; mRNA.
DR CCDS; CCDS40539.2; -. [Q8BNA6-1]
DR SMR; Q8BNA6; -.
DR IntAct; Q8BNA6; 2.
DR MINT; Q8BNA6; -.
DR STRING; 10090.ENSMUSP00000080808; -.
DR GlyConnect; 2655; 2 N-Linked glycans (3 sites).
DR GlyGen; Q8BNA6; 26 sites, 2 N-linked glycans (3 sites).
DR iPTMnet; Q8BNA6; -.
DR PhosphoSitePlus; Q8BNA6; -.
DR EPD; Q8BNA6; -.
DR MaxQB; Q8BNA6; -.
DR PaxDb; Q8BNA6; -.
DR PRIDE; Q8BNA6; -.
DR ProteomicsDB; 271553; -. [Q8BNA6-1]
DR ProteomicsDB; 271554; -. [Q8BNA6-2]
DR ProteomicsDB; 271555; -. [Q8BNA6-3]
DR Antibodypedia; 8386; 73 antibodies from 13 providers.
DR Ensembl; ENSMUST00000217308; ENSMUSP00000148968; ENSMUSG00000074505. [Q8BNA6-1]
DR UCSC; uc009ogj.1; mouse. [Q8BNA6-1]
DR UCSC; uc009ogk.1; mouse. [Q8BNA6-3]
DR MGI; MGI:2444314; Fat3.
DR VEuPathDB; HostDB:ENSMUSG00000074505; -.
DR eggNOG; KOG1219; Eukaryota.
DR GeneTree; ENSGT00940000154981; -.
DR InParanoid; Q8BNA6; -.
DR OMA; RFHFHVH; -.
DR PhylomeDB; Q8BNA6; -.
DR ChiTaRS; Fat3; mouse.
DR PRO; PR:Q8BNA6; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BNA6; protein.
DR Bgee; ENSMUSG00000074505; Expressed in habenula and 212 other tissues.
DR ExpressionAtlas; Q8BNA6; baseline and differential.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0000904; P:cell morphogenesis involved in differentiation; IMP:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0016358; P:dendrite development; IMP:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:1904936; P:interneuron migration; IMP:MGI.
DR GO; GO:2000171; P:negative regulation of dendrite development; IMP:MGI.
DR GO; GO:0010842; P:retina layer formation; IGI:MGI.
DR CDD; cd00110; LamG; 1.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF00028; Cadherin; 27.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 32.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00282; LamG; 1.
DR SUPFAM; SSF49313; SSF49313; 34.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00232; CADHERIN_1; 19.
DR PROSITE; PS50268; CADHERIN_2; 32.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Developmental protein;
KW Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Methylation;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..4555
FT /note="Protocadherin Fat 3"
FT /id="PRO_0000324635"
FT TOPO_DOM 32..4153
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 4154..4174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 4175..4555
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 43..157
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 158..262
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 263..374
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 376..471
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 472..577
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 578..680
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 726..830
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 831..935
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 936..1042
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1043..1147
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1148..1253
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1254..1358
FT /note="Cadherin 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1362..1459
FT /note="Cadherin 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1460..1565
FT /note="Cadherin 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1566..1768
FT /note="Cadherin 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1769..1882
FT /note="Cadherin 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1883..1985
FT /note="Cadherin 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1982..2083
FT /note="Cadherin 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2084..2185
FT /note="Cadherin 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2186..2286
FT /note="Cadherin 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2287..2393
FT /note="Cadherin 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2394..2495
FT /note="Cadherin 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2496..2599
FT /note="Cadherin 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2600..2707
FT /note="Cadherin 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2708..2813
FT /note="Cadherin 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2814..2923
FT /note="Cadherin 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2924..3028
FT /note="Cadherin 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3029..3130
FT /note="Cadherin 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3131..3235
FT /note="Cadherin 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3236..3340
FT /note="Cadherin 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3341..3445
FT /note="Cadherin 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3446..3550
FT /note="Cadherin 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3551..3660
FT /note="Cadherin 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3794..3832
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3834..4017
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 4020..4057
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4059..4095
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4097..4133
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 4300..4353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4395..4474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4314..4348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4432..4446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4508
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 4518
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 667
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 799
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 879
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 898
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1006
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1751
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1944
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1993
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1996
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2734
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3000
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3926
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 3798..3809
FT /evidence="ECO:0000250"
FT DISULFID 3803..3821
FT /evidence="ECO:0000250"
FT DISULFID 3823..3831
FT /evidence="ECO:0000250"
FT DISULFID 3984..4017
FT /evidence="ECO:0000250"
FT DISULFID 4024..4035
FT /evidence="ECO:0000250"
FT DISULFID 4029..4045
FT /evidence="ECO:0000250"
FT DISULFID 4047..4056
FT /evidence="ECO:0000250"
FT DISULFID 4063..4074
FT /evidence="ECO:0000250"
FT DISULFID 4068..4083
FT /evidence="ECO:0000250"
FT DISULFID 4085..4094
FT /evidence="ECO:0000250"
FT DISULFID 4101..4112
FT /evidence="ECO:0000250"
FT DISULFID 4106..4121
FT /evidence="ECO:0000250"
FT DISULFID 4123..4132
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..3806
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032329"
FT VAR_SEQ 1538..1591
FT /note="RDQEFPYRRNLARVIVNVEDANDHSPYFTNPLYEASVFESAALGSVVLQVTA
FT LD -> GPDLGFCSPGRTVNQPRHIPQEARAFKFYRPSFCTARLHAVLPLYFNEEVTVL
FT R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032330"
FT VAR_SEQ 1592..4555
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032331"
FT VAR_SEQ 4043..4121
FT /note="YQCSCLSQFTGTNCESEITACFPNPCRNGGSCDPIGNTFVCSCKAGLTGVTC
FT EDDVDECEREECENGGSCVNLFGSFFC -> ECTSVQARGGSAPEVCPLHSQPLPPSPG
FT PSQKGWSFGYNFTSAFMGWRSGPAMVGRELRGRGLWSTLEKRGEGTWGNLN (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032332"
FT VAR_SEQ 4122..4555
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032333"
SQ SEQUENCE 4555 AA; 502011 MW; 4E23122CCAC98DDD CRC64;
MSVTMGHCMG TKPPSCIILL LLKLFATVSQ GLPGTGPLGF HFTHSTYNAT VYENSAARTY
VNSQSRMGIT LIDLSWDIKY RIVSGDEEGF FKAEEVIIAD FCFLRIRTKG GNSAILNREI
QDNYLLIIKG SVRGEDLEAW TKVNIQVLDM NDLRPLFSPT TYSVTIAEST PLRTSVAQVT
ATDADIGSNG EFYYYFKNKV DLFSVHPTSG VISLSGRLNY DEKNRYDLEI LAVDRGMKLY
GNNGVSSTAK LYVHIERINE HAPIIHVVSH TPFSLDKEPT YAVVTVDDLD EGANGEIESL
SIVDGDPLEQ FFLAKEGKWL NEYKVKERRQ VDWESFSYGY NLTIQAKDKG SPQKFSELKT
VHIANPRRDN TPVRFEKDVY EVSISEFSPP GVLVAIVKVS PEPLDVEYKL LPGKDSDYFK
INPRSGLIVT AQPLNTVKKE VYKLEVSDKE GDAKAQVTIG IEDANDHTPE FQEALYETFV
NESVRVGTNV LTVSASDKDK GENGYITYSI ASLNLLPFAI NQFTGVISTT EELDFESSPE
TYRFIVRASD WGSPYRHESE VNVTIRVGNV NDNSPLFEKV ACQGVISYDF PVGGHITAIS
AIDIDELELV KYKIISGNEL GFFYLNPDSG VLQLKKSLMN SGIKNGNFAL RITATDGENF
ADPMAINISV LHGKVSSKSF SCRETRVAQK LAEKLLIKAK ANGKLNLEDG FLDFYSINRQ
GPHFDKSFPS DVAVKEDMLV GTNILKIKAY DADSGFNGKV LFTISDGNTD SCFNIDMETG
QLKVLMPMDR EHTDLYVLNI TIYDLGKPQK SSWRLLTVNV EDANDNNPVF LQDSYSVSIL
ESSSIGTEII QVEARDKDLG SNGEVMYSVL TDTHQFIINS STGIVYIADQ LDRESKANYS
LKIEARDKAE SGQQLFSVVT LKIFLDDVND CSPAFIPSSY SVKVLEDLPV GTVIAWLETQ
DPDLGLGGQV RYSLVNDYNG RFEVDKASGA IRLSKELDYE KQQFYNLTVR AKDKGRPVSL
SSVSFVEVEV VDVNENLHTP YFPDFAVVGS VKENSRIGTS VLQVTAHDED SGRDGEIQYS
IRDGSGLGRF NIDDESGVIT AADSLDRETT ASYWLTVYAT DRGVVPLYST IEVYIEVEDV
NDNAPLTSEP IYYPVVMENS PKDVSVIQIQ AEDPDSGSNE KLTYRITSGN PQNFFAINIK
TGLITTTSRK LDREQQAEHF LEVTVTDGGS SPKQSTIWVV VQVLDENDNR PQFPEKVYQI
KLPERDRKKR GEPIYRAFAF DKDEGPNAEI SYSIVDGNDD GKFFIDPKTG MVSSRKQFTA
GSYDILTIKA VDNGRPQKSS TARLHIEWIK KPPPSPIPLT FDEPFYNFTV MESDKVTEIV
GVVSVQPANT PLWFDIVGGN FDSSFDAEKG VGTIVIAKPL DAEQRSVYNM SVEVTDGTNI
AVTQVFIKVL DNNDNGPEFS QPHYDVTISE DVLPDTEILQ IEATDRDEKH KLSYTIHSSI
DAVSMRKFRM DPSTGVLYTA ERLDHEAQDK HILNIMVRDQ EFPYRRNLAR VIVNVEDAND
HSPYFTNPLY EASVFESAAL GSVVLQVTAL DKDKGENAEL IYSIEAGNTG NTFKIEPVLG
IITISKEPDM AAMGQFVLSV KVTDQGSPPM SATAIVRISI SMSDNSHPKF THKDYQAEVN
ENVDIGTSVI LISAISQSTL IYEVKDGNIN GVFTINPYSG VITTRRALDY EHTSSYQLII
QATNMAGMAS NATISVQIVD ENDNPPVFLF SQYSGSLSEA APINSIVRSL DNSPLVIRAT
DADSNQNALL VYQIVESTAK KFFTVDSSTG AIRTIANLDH EAIAHFHFHV HVRDSGNPQL
TAESPVEVNI EVTDVNDNPP VFTQAVFETV LLLPTYIGVE VLKVSATDPD SEVPPELTYS
LMEGSVDNFL MDPNTGVLTI KNNNLSKDHY MLIVRVSDGK FYSTAMVTVM VKEAMDSGLH
FTQSFYSTSI SENSTNITKV AIVNAVGNRL NEPLKYSILN PGNKFKIKST SGVIQTTGVP
FDREEQELYE LVVEASRELD HLRVARVVVR VNIEDVNDNS PVFVGLPYYA AVQVDAEPGT
LIYRVTAIDK DKGANGEVTY VLQDDYGHFE INPNSGNVIL REAFNSDLSN IDYGVTILAK
DGGNPSLSTF VELPITIVNK AMPVFDKPFY TASINEDITM NTPILSINAT SPEGQGIIYL
IIDGDPFQQF NIDFDTGVLK VISPLDYEVT SVYKLTVRAS DALTGARAEV TVDLLVDDIN
DNPPVFDQPT YNTTLSESSL IGTPVLQLVS TDADSGNNKL VRYQIVQDTY NSTDYFHIDS
SSGLILTARM LDHELVQHCT LKVTATDNGF PSLSSEVLVQ IYISDVNDNP PVFNQLIYES
YVSELAPRGH FVTCVQASDA DSSDLDRLEY SILSGNDRAS FLMDSKSGVL TLSSHRKQRM
EPLYSLNVSV SDGLFTSTAQ VHIRVLGANL YSPAFSQSTY VAEVRENAAS GTKVIHVRAT
DGDPGTYGQV SYSIINDFAK DRFLIDSNGQ IITTERLDRE NPLEGDISIY LRALDGGGRT
TFCTVRVIVV DENDNAPQFM TVEYRASVRA DVGRGHLVTQ VQALDPDDGA NSRITYSLYS
EASVSVADLL EIDPDNGWMV TKGNFNQLRN TVLSFFVKAV DGGIPVRHSL IPVYIHVLPP
ETFLPSFTQS QYSFTITEDT SIGSTVDTLR ILPNQSVRFS MVNGERPENN KEGVFIIEQE
TGAIKLDKRL DHEVSPAFHF KVAATIPLDK VDIVFTVDVD VKVLDLNDNK PVFETSTYET
IIMEGMPVGT KLAQVRAIDM DWGANGQVTY SLHSDSHLEK VIEAFNIDSN TGWISTLKDL
DHETDPAFSF FVVASDLGEA FSLSSMALVS VKVTDINDNA PVFAHEVYRG NVKESDPPGE
VVAVLSTLDK DTSNINRQVS YHITGGNPRG QFALGMVQSE WKVYVKRPLD REEQDIYFLN
ITASDGLFVT QAMVEVTVSD VNDNSPVCDQ VAYSASLPED IPSNKIILKV SAKDADIGSN
GDIRYSLYGS GNNEFFLDPE SGELKTLAVL DRERVPVYNL IARATDGGGR FCSSSVLLLL
EDVNDNPPVF SSNHYTACVY ENTATKALLT RVQAMDPDVG INRKVVYSLE DSASGVFSID
SSSGVIVLEQ PLDREQQSSY NISVRATDQS PGQSLSSLAS VTITVLDIND NPPVFERRDY
LVTVPEDTSL GTQVLSVFAT SKDIGTNAEI TYLIRSGNEQ GKFSINPKTG GISVLEALDY
ETCRRFYLVV EAKDGGTPAL STAATVSIDL TDVNDNPPRF SQDVYSAVIS EDALEGDSVI
LLIAEDVDSK PNGQIRFSIV GGDRDNEFAV DPILGLVKVK KKLDRERVSG YSLLIQAVDS
GIPAMSSTTT VNIDISDVND NSPVFTPANY TAVIQENKPV GTSILQLVVT DRDSFHNGPP
FSFSILSGNE DEEFMLDSHG ILRSAVVFRH MESPEYLLCI QAKDSGKPQQ VSHTYIRVRV
IEESTHKPTA IPLEIFIVTM EDDFPGGVIG KIHATDQDMY DVLTFALKSE QKSLFKVNSH
DGKIIALGGL DSGKYVLNVS VSDGRFQVPI DVVVHVEQLV HEMLQNTVTI RFEDVSPEDF
VGLHMHGFRR ILRNAVLTQK QDSLRIISIQ PVVGTNQLDM LFAVEMHSSE FYKPAYLIQK
LSNARRHLEN VMHIAAILEK NCSGLDCQEQ HCEQGLSLDS HALMTYSTAR ISFVCPRFYR
NVRCTCNGGV CPGSNDPCVE KPCPEDMQCV GYEASRRPFL CQCPPGKLGE CSGHTSLSFA
GNSYIKYRLS ENSKEEDFKL ALRLRTLQSN GIIMYTRANP CMILKIVEGK LWFQLDCGSG
PGILGISSRA VNDGSWHSVF LELNRNFTSL ALDDSYVERR RAPLYFQTLS TDSAIFFGAL
VQADNVRSLT DTRVTQVLGG FQGCLDSVVL NHYELPLQNK RSSFAEVVGL TELKLGCVLY
PDACQRSPCL HGGSCSSLPS GGYQCSCLSQ FTGTNCESEI TACFPNPCRN GGSCDPIGNT
FVCSCKAGLT GVTCEDDVDE CEREECENGG SCVNLFGSFF CNCTPGYVGQ YCGLRPVVVP
NIQAGHSYVG KEELIGIAVV LFVIFTLIVL FIVFRKKVFR KNYSRNNITL VQDPATAALL
HKSNGIPFRS LRAGDGRNVY QEVGPPQVPV RPMAYTPCFQ SDSRSNLDKG LDVLGGEPQE
MSTFHPESPR ILTARRGVVV CSVAPNLPAV SPCRSDCDSI RKNGWDTGSE NKGTEDTGEV
TCFTNSNKGS NSEVQSLSSF QSDSGDDNAY HWDTSDWMPG ARLSDIEEMP NYESQDGGAA
HQGSTRELES DYYLGGYDID SEYPPPHEEE FLSRDQLPPP LPEDFPDQYE ALPPSQPTSL
TSTMSPDCRR RPRFHPSQYL PPHPLPGETD LGGPSSSCDF STFAVNMNQG TEVMAPTDSV
SLSLHNSRGT SSSEMSARCG FDDSEVAMSD YESAGELSLT NLHIPFVETQ QQTQV
