FAT2_MOUSE
ID FAT2_MOUSE Reviewed; 4351 AA.
AC Q5F226; Q3V1D4; Q69ZY7;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Protocadherin Fat 2;
DE AltName: Full=FAT tumor suppressor homolog 2;
DE Flags: Precursor;
GN Name=Fat2; Synonyms=Fath2, Kiaa0811;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2698-4351.
RC TISSUE=Brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3590-4351.
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Involved in the regulation of cell migration (By similarity).
CC May be involved in mediating the organization of the parallel fibers of
CC granule cells during cerebellar development (By similarity).
CC {ECO:0000250|UniProtKB:O88277, ECO:0000250|UniProtKB:Q9NYQ8}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Cell junction {ECO:0000250|UniProtKB:Q9NYQ8}.
CC Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:O88277}.
CC Note=Localized at adhesion zippers (early state of adherens junctions)
CC of keratinocytes. {ECO:0000250|UniProtKB:Q9NYQ8}.
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DR EMBL; AL713870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466575; EDL33495.1; -; Genomic_DNA.
DR EMBL; AK173031; BAD32309.1; -; mRNA.
DR EMBL; AK132523; BAE21217.1; -; mRNA.
DR CCDS; CCDS36157.1; -.
DR RefSeq; NP_001025159.1; NM_001029988.2.
DR RefSeq; XP_006533385.1; XM_006533322.3.
DR RefSeq; XP_006533386.1; XM_006533323.3.
DR SMR; Q5F226; -.
DR BioGRID; 232833; 1.
DR IntAct; Q5F226; 1.
DR STRING; 10090.ENSMUSP00000067556; -.
DR GlyConnect; 2654; 3 N-Linked glycans (3 sites).
DR GlyGen; Q5F226; 37 sites, 3 N-linked glycans (3 sites).
DR iPTMnet; Q5F226; -.
DR PhosphoSitePlus; Q5F226; -.
DR MaxQB; Q5F226; -.
DR PaxDb; Q5F226; -.
DR PeptideAtlas; Q5F226; -.
DR PRIDE; Q5F226; -.
DR ProteomicsDB; 267341; -.
DR Antibodypedia; 77918; 108 antibodies from 11 providers.
DR DNASU; 245827; -.
DR Ensembl; ENSMUST00000068853; ENSMUSP00000067556; ENSMUSG00000055333.
DR Ensembl; ENSMUST00000108864; ENSMUSP00000104492; ENSMUSG00000055333.
DR GeneID; 245827; -.
DR KEGG; mmu:245827; -.
DR UCSC; uc007izf.1; mouse.
DR CTD; 2196; -.
DR MGI; MGI:2685369; Fat2.
DR VEuPathDB; HostDB:ENSMUSG00000055333; -.
DR eggNOG; KOG1219; Eukaryota.
DR GeneTree; ENSGT00940000158507; -.
DR HOGENOM; CLU_000042_2_0_1; -.
DR InParanoid; Q5F226; -.
DR OMA; CFLNEPL; -.
DR OrthoDB; 12779at2759; -.
DR PhylomeDB; Q5F226; -.
DR TreeFam; TF316403; -.
DR BioGRID-ORCS; 245827; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q5F226; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5F226; protein.
DR Bgee; ENSMUSG00000055333; Expressed in cerebellum and 72 other tissues.
DR Genevisible; Q5F226; MM.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0031589; P:cell-substrate adhesion; ISS:UniProtKB.
DR GO; GO:0010631; P:epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
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; IPR001791; Laminin_G.
DR Pfam; PF00028; Cadherin; 28.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 33.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00282; LamG; 1.
DR SUPFAM; SSF49313; SSF49313; 33.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS00232; CADHERIN_1; 13.
DR PROSITE; PS50268; CADHERIN_2; 32.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell junction; Cell membrane; Disulfide bond;
KW EGF-like domain; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..4351
FT /note="Protocadherin Fat 2"
FT /id="PRO_0000406601"
FT TOPO_DOM 19..4050
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 4051..4071
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 4072..4351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..148
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 149..256
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 363..458
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 459..564
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 565..669
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 716..820
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 821..925
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 926..1032
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1033..1142
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1138..1242
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1243..1346
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1350..1448
FT /note="Cadherin 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1449..1555
FT /note="Cadherin 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1556..1660
FT /note="Cadherin 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1661..1758
FT /note="Cadherin 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1759..1872
FT /note="Cadherin 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1873..1968
FT /note="Cadherin 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1969..2070
FT /note="Cadherin 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2071..2171
FT /note="Cadherin 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2172..2272
FT /note="Cadherin 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2273..2379
FT /note="Cadherin 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2380..2481
FT /note="Cadherin 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2482..2585
FT /note="Cadherin 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2586..2692
FT /note="Cadherin 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2693..2799
FT /note="Cadherin 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2800..2908
FT /note="Cadherin 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2909..3013
FT /note="Cadherin 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3014..3115
FT /note="Cadherin 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3116..3220
FT /note="Cadherin 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3221..3323
FT /note="Cadherin 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3324..3428
FT /note="Cadherin 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3429..3533
FT /note="Cadherin 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3534..3631
FT /note="Cadherin 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3775..3946
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 3949..3986
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3988..4024
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 4313..4340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 789
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 996
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1899
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1998
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2007
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2597
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3770
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3774
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3815
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3842
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3875
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3906
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3991
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 3914..3946
FT /evidence="ECO:0000250"
FT DISULFID 3953..3964
FT /evidence="ECO:0000250"
FT DISULFID 3958..3974
FT /evidence="ECO:0000250"
FT DISULFID 3976..3985
FT /evidence="ECO:0000250"
FT DISULFID 3992..4003
FT /evidence="ECO:0000250"
FT DISULFID 3997..4012
FT /evidence="ECO:0000250"
FT DISULFID 4014..4023
FT /evidence="ECO:0000250"
FT CONFLICT 4010
FT /note="T -> N (in Ref. 4; BAE21217)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4351 AA; 480109 MW; 72F9DADAAA5467D5 CRC64;
MTLVLLGVAM VLLHRAACEK PLEETITPLT WRFTHSLYNA TIYENSAPKT YVESPVKMGM
YLAEPHWVVK YRIISGDAAG VFKTEEHVVG NFCFLRIRTK SSNTALLNRE VRDSYTLVVQ
ASDKSLEFEA LTQVVVHILD QNDLKPLFSP PSYRFTISED RPLKSPICKV TATDADLGQN
AEFYYAFNAR SEVFAIHPTS GVVTVAGKLN VTWRGKYELQ VLAVDRMRKI SEGNGFGNLA
PLVIYVEPVH RKPPVITLVV LNPPEGDEGD IYATVTVDTN GSGAEVDSLE VVGGDPGKYF
KVLKSYAQGN EFNLVAVRDI NWAEHLHGFN ISLQTHSRSR FPSRSIIRAF HLPPYTLANL
RFEKAVYRVK LSEFSPPGSR VALVRVTTAL PTLRYALKPS SGSTVFKLNA RTGLITTTKP
VDFHEQNQYQ LHVKTSLGQA TTTVIIDIVD CNNHAPVFNR SSYEGTLDEN IPPGTSVLTV
TATDQDHGDN GHITYSIAGP KAVPFSIDPY LGVISTTKSM DYELMKRIYT FRVRASDWGS
PFRQEKEVSV SLRLKNLNDN QPMFEEVNCT VSLRQDAPVG KSIMAVSAID MDELQNLKYE
IVSGNEQDYF HLNHFSGVIS LKRSFMNLTA VRPTVYSLKI TASDGKNYAS PTTLKVTVVK
DPRSEVPVQC DKTGVLTHIT KTILQSAGLQ GQEMGEEDFT SLGNYQINHH APQFEDHFPQ
SIDILEQVPV NTPLAHLAAT DPDPGFHGRL VYVIADGNEE GCFDIELETG LLTVAAALDY
ETTSFYVLNV TVYDLGTPPK SSWKLLTVTV KDWNDKPPRF PPGGYQLTIS EDTEVGTTVA
ELKTRDTDSE DNGRVRYTLL TPTEKFSLHP LTGELVVTGQ LDRESEPQYI LKAEARDQPT
KGHQLFSVTD VIVTLEDIND NPPQCITEHS SLKVPEDMPL GTVLTFLDAS DPDLGPAGEV
KYILVDDVHG TFRVDPMTGA LSLEKELDFE RRAGYNLSFW ASDSGRPLAR RTLCHVEVLV
MDVNENLHSP HFSSFVYQGQ VQENSPAGTQ VMVVTAQDDD SGLDGELQYF LRAGTGLEAF
SINQDTGMLE TLAPLDREFT PYYWLTVLAV DRGSVPLSAV TEVYIEVTDI NDNIPSMSRP
VFYPSVKEDA PLGTSVLQLE AWDPDFSSQG KLTFNLTSGN HMGHFIVHPF TGLLSTAKQL
DRENKDEYVL EVTVQDNGDP PLRSTSRVVV CVLDVNDNSP MFSHKLFNVR LSERLSPLSP
EPVYRLVASD PDEGLNGSIT YSIEESDEES FRIDPVTGVV SSSSTFAAGE YNILTIKATD
SGQPALSTSV RLHIEWIPQP RPSSIPLSFD ESHYSFAVME TDPVNHMLGV ISVEGRPGLF
WFHISDGDKD MDFDIEKTTG SIVIARPLDT RRKSSYNLTV EVTDGFHTIA TQVHILMIAN
INHHRPQFLQ DHYDIRVPQD TLPGVELLRV QATDQDHGKG LIYTIHSSRD PGSANLFQLD
PSSGVLVTVG TLDLHSGPSQ HILTVMVRDQ EMPIKRNFVW VTIHVEDGNL HSPHFTQPRY
EANVPDTTTP GTELLQVRAV DADRGANAEV HYSFLKGNSE GFFNIDSLLG IITVAQRLDH
VHLNRHALTV KAEDQGSPQR HDLAMVVVHV HPSDSSAPIF SKDEYFIEIP ESVPIGSPIL
LISAASSSDV TYELREGNKN SVFSMNSYSG LISTQKRLDH EKVSSYQLKI RGSNMAGVFT
EVVALVYIID ENDNAPAFLK STFVGHISEA APLHSLILGE DNSPLVIRAS DSDQEANSLL
VYKILEPEAL KFFKIDPSMG TLTITSELDY ETTPLFQFSI YVHDQGTPIL FAPRSARVII
HVRDVNDSPP RFSEQIYEVA VVEPIHPGME LLTVQAEDND SKVTYSIKTS NTDEAVTIHP
ITGQISVVNP AALRLFPKLN IRAFDGLYQD TAVVKISLTQ ALDKSLQFDQ DIYRARVTEN
TPHSNVLVIL GVHGNHLNDT LSYFLLNGTD LFHMVKSAGV LQTRGVTFDR EQQDTHEVAV
EVRDNRVPRR VAQALVRVSV EDVNDNIPEF QHLPYYTVIQ DGTEPGDVLF QVSATDKDLG
ANGTVTYGFA EDYAYFRIDP YVGDISLKKP FDYQALNKYH LRVTARDAGT PPLQTEVEVH
VTVRNKSNPL FQSPYYKVKV PENITLYTPI LHTQARSPEG LRLIYNIVEE EPLMLFTTDF
KTGVLTVTGP LDYESKNKHV FTVRATDTAL GSFSEATVEV LVEDINDNPP TFSQLVYSTS
VSEGSPAQTP VIQLLASDQD SGQNQDVSYQ IVEDGSDVSK FFRINGSTGE MFTIQELDYE
AHQHFRVKVR ATDRGDPPLT GETLVVVNVS DINDNPPEFR EPQYEANVSE LATCGHLVLK
VQALDPDIGD TSRLEYLILS GNQDRHFSIN STSGIISMFN LCKKQLDSSY NLRVGASDGV
FQATVPVYIN TTNANKYSPE FQQNVYEAEL AENAKVGTKV IELLAIDKDS GPYGTVDYTI
INKLAGERFF INPSGQITTL QKLDRENSTE RVIAIKIMAR DGGGKVAFCT VKIILTDEND
NAPQFKASGY TVSIPSNVSR DSPIIQVLAY DADEGRNADV TYSVDSTEDL AEEIIEVNPT
TGVVKVKESL VGLENKAVDF NIKAQDGGPP HWDSLVPVRL QVVPNEIPLP KFSEPLYTFS
ASEDLPEGSE IGSVKAVAAQ DPIIYSLVQG TTPESNSDDV FSLDQDTGVL KVKKAMDHES
TKWYQIDLMA HCPHEDTDLV SLVSVNIQVE DVNDNRPVFE ADPYKAFLTE NMPGGTTVIQ
VTANDQDTGS DGQVSYRLSV EPGSNIHQLF AVDSESGWIT TLQELDCETQ QTYRFYVVAF
DHGQTIQLSS QALVEVSITD ENDNPPRFAS EDYRGSVVEN NEPGELVATL KTLDADISEQ
NRQVTCYITE GDPLGQFSIS QVGDEWRITS RKTLDREHIA KYLLRITASD GKFQASVPVE
VFVLDINDNS PQCSQLLYTG KVREDVTPGH FILKVSAIDV DMDTNAQITY SLHGPGAQEF
KLDPHTGELT TLSVLDRERK DVYNLVAKAT DGGGQSCQAE VTLHIEDVND NAPRFFPSHC
AVAVFDNTTV KTPVAVVFAR DPDQGVNAQV VYSLTDSADG QFSIDATSGV IRLEKPLQVR
SSSAVELTVR ASDLGTPIPL STLGTVTVSI VGLEDYLPIF LNSEHSTQVP EDALIDMEVL
YLATLTRPGS EKTGYHITGG NEQGKFRLDA HTGILYVNGS LDFETNPKYF LSIECSRKSS
SSLSDVTTIV INVTDVNEHH PRFTHDLYTV RVLENAIVGD VILTVSASDD DGPVNSVITY
SLVGGNQLGH FTIDPKKGKL QVAKALDWEQ TPSYSLRIRA TDSGQPPLHE DTEVAVEVVD
VNDNPPRFFQ LNYSTAVQEN SPIGIKVLQL ILDDPDSPQN GPPYFFRITE GNTGSVFRVT
PDGWLVTAGS LSRRAQEWYQ LHIEVSDSGL PPLSSSTLVR VHITEQSRYP PSTLPLEIFI
TKGEEEFQGG MVGKIHATDR DPQDTLTYSL DREGSLGKYF TVGASDGKII ASQGLPRGRY
LFNVTVSDGT FTTTTGVHVH VWHMGQEAPQ QAVWLGFHQL TPEELVSDHW RNLQRFLSNI
LDIKRANIHL ASLQPAEVTA GVDVLLAFEG HSGTSYDLQE LASAIAHSAK EMEHSVGIQM
RSALPVVPCQ GPSCQDQTCQ ETVSLEPRVG PSYSTARLSI LTPRHHLGKN CSCNGTTWRF
SGQSYMRYRP LEAQNWQIHF YLKTLQPWAL LMFTNETASI SLKLANGFLH LEYRCPGGFY
GNLSSHRPVN DGQWHSMLLE ERDTSVHLLV DITDNTSLVI PEECQGLRTE RHLLLGGLVP
SNPSSNVSLG FEGCLDAVVV NSERLELLGH RKKMAGYLET WALSQCCWPG TTCSQNPCLN
GGSCSPALGS GYLCRCPPLF SGRNCELGRE NCTSAPCQEG GTCVSSPEGT SCSCPHPYTG
DRCEMEARGC SGGHCLITPE IKRGDWGQQE FLVIIVALPL LIIATVGLLL YCRRCKSHKP
VAMEDPDLLA RSIGVDTQAS PAIELDPLNA GSCNDLNQLE PSKTSVPNEL VTFGPSSKQR
PMVCSVPPRL PPAVVSSHPG HEPIIKRTWS GEELVYPSGA AVWPPTYSRK EHWEYPHPEA
MQGPLPPSPR RHVSPAVMPD PAGLYGGFPF PLELENKRAP LPPRYSNQNL EDLIPPRPPS
PREHLLAPCL NEYTAISYYH SQFRQGGGGP CLAEGGYKGV SMRLSRAGPS YADCEVNGGP
APGRSQPRAP PNYEGSDMVE SDYGSCEEVM F
