AKNA_MOUSE
ID AKNA_MOUSE Reviewed; 1404 AA.
AC Q80VW7; Q3TC64; Q3TDM3; Q3U3N4; Q6ZPF9; Q8CFV0; Q8R114;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Microtubule organization protein AKNA {ECO:0000305};
DE AltName: Full=AT-hook-containing transcription factor {ECO:0000305};
GN Name=Akna {ECO:0000312|MGI:MGI:2140340};
GN Synonyms=Kiaa1968 {ECO:0000303|PubMed:14621295};
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 MRNA] (ISOFORM 4).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
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. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 175-1404 (ISOFORM 1).
RC STRAIN=NOD;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 756-1404 (ISOFORM 3).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Eye, and Liver;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-617; SER-1144 AND
RP SER-1145, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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 [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=21606955; DOI=10.1038/cr.2011.84;
RA Ma W., Ortiz-Quintero B., Rangel R., McKeller M.R., Herrera-Rodriguez S.,
RA Castillo E.F., Schluns K.S., Hall M., Zhang H., Suh W.K., Okada H.,
RA Mak T.W., Zhou Y., Blackburn M.R., Martinez-Valdez H.;
RT "Coordinate activation of inflammatory gene networks, alveolar destruction
RT and neonatal death in AKNA deficient mice.";
RL Cell Res. 21:1564-1577(2011).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND INTERACTION WITH DCTN1; MAPRE1; ODF2 AND CAMSAP3.
RX PubMed=30787442; DOI=10.1038/s41586-019-0962-4;
RA Camargo Ortega G., Falk S., Johansson P.A., Peyre E., Broix L., Sahu S.K.,
RA Hirst W., Schlichthaerle T., De Juan Romero C., Draganova K., Vinopal S.,
RA Chinnappa K., Gavranovic A., Karakaya T., Steininger T., Merl-Pham J.,
RA Feederle R., Shao W., Shi S.H., Hauck S.M., Jungmann R., Bradke F.,
RA Borrell V., Geerlof A., Reber S., Tiwari V.K., Huttner W.B.,
RA Wilsch-Braeuninger M., Nguyen L., Goetz M.;
RT "The centrosome protein AKNA regulates neurogenesis via microtubule
RT organization.";
RL Nature 567:113-117(2019).
CC -!- FUNCTION: Centrosomal protein that plays a key role in cell
CC delamination by regulating microtubule organization (PubMed:30787442).
CC Required for the delamination and retention of neural stem cells from
CC the subventricular zone during neurogenesis (PubMed:30787442). Also
CC regulates the epithelial-to-mesenchymal transition in other epithelial
CC cells (PubMed:30787442). Acts by increasing centrosomal microtubule
CC nucleation and recruiting nucleation factors and minus-end stabilizers,
CC thereby destabilizing microtubules at the adherens junctions and
CC mediating constriction of the apical endfoot (PubMed:30787442). In
CC addition, may also act as a transcription factor that specifically
CC activates the expression of the CD40 receptor and its ligand
CC CD40L/CD154, two cell surface molecules on lymphocytes that are
CC critical for antigen-dependent-B-cell development (By similarity).
CC Binds to A/T-rich promoters (By similarity). It is unclear how it can
CC both act as a microtubule organizer and as a transcription factor;
CC additional evidences are required to reconcile these two apparently
CC contradictory functions (Probable). {ECO:0000250|UniProtKB:Q7Z591,
CC ECO:0000269|PubMed:30787442, ECO:0000305}.
CC -!- SUBUNIT: Interacts with DCTN1 (PubMed:30787442). Interacts with
CC MAPRE1/EB1 (PubMed:30787442). Interacts with ODF2 (PubMed:30787442).
CC Interacts with CAMSAP3 (PubMed:30787442).
CC {ECO:0000269|PubMed:30787442}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:30787442}. Nucleus
CC {ECO:0000250|UniProtKB:Q7Z591}. Note=Localizes to the distal part of
CC the subdistal appendages of the mother centriole in interphase
CC (PubMed:30787442). Also found at the proximal ends of centrioles and
CC along microtubules (PubMed:30787442). The centrosomal localization is
CC dependent on centrioles (PubMed:30787442). Dissociates from centrosomes
CC during M-phase without proteolytic degradation and reassembles at the
CC centrosomes during late telophase and early G1 phase (PubMed:30787442).
CC Dissociation and reassembly is regulated by phosphorylation
CC (PubMed:30787442). {ECO:0000269|PubMed:30787442}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q80VW7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80VW7-2; Sequence=VSP_025942, VSP_025943;
CC Name=3;
CC IsoId=Q80VW7-3; Sequence=VSP_025944, VSP_025945;
CC Name=4;
CC IsoId=Q80VW7-4; Sequence=VSP_025941, VSP_025944, VSP_025945;
CC -!- TISSUE SPECIFICITY: Expressed in neural stem cells isolated at the peak
CC of subventricular zone (SVZ): localizes at the subdistal appendages of
CC the mother centriole in specific subtypes of neural stem cells and in
CC almost all basal progenitors. {ECO:0000269|PubMed:30787442}.
CC -!- DEVELOPMENTAL STAGE: During development, expressed when the
CC subventricular zone (SVZ) is generated (low at 11 dpc, high at 14 dpc
CC and low at 18 dpc). {ECO:0000269|PubMed:30787442}.
CC -!- PTM: Phosphorylated; phosphorylation regulates dissociation from and
CC reassembly at the centrosome. {ECO:0000269|PubMed:30787442}.
CC -!- DISRUPTION PHENOTYPE: Neonatal lethality: mice fail to thrive and most
CC of them die by postnatal day 10 (PubMed:21606955). Mice display
CC systemic inflammation, predominantly in the lungs, accompanied by
CC enhanced leukocyte infiltration and alveolar destruction
CC (PubMed:21606955). {ECO:0000269|PubMed:21606955}.
CC -!- SIMILARITY: Belongs to the AKNA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98278.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129468; BAC98278.1; ALT_INIT; mRNA.
DR EMBL; AK154663; BAE32751.1; -; mRNA.
DR EMBL; AK170121; BAE41578.1; -; mRNA.
DR EMBL; AK170885; BAE42093.1; -; mRNA.
DR EMBL; AL683828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025835; AAH25835.1; -; mRNA.
DR EMBL; BC036324; AAH36324.1; -; mRNA.
DR EMBL; BC092227; AAH92227.1; -; mRNA.
DR CCDS; CCDS38777.1; -. [Q80VW7-1]
DR RefSeq; NP_001038979.1; NM_001045514.3. [Q80VW7-1]
DR RefSeq; NP_001292361.1; NM_001305432.1. [Q80VW7-1]
DR RefSeq; XP_006537583.1; XM_006537520.3. [Q80VW7-1]
DR RefSeq; XP_006537584.1; XM_006537521.2. [Q80VW7-1]
DR RefSeq; XP_006537585.1; XM_006537522.3. [Q80VW7-1]
DR AlphaFoldDB; Q80VW7; -.
DR SMR; Q80VW7; -.
DR STRING; 10090.ENSMUSP00000041614; -.
DR iPTMnet; Q80VW7; -.
DR PhosphoSitePlus; Q80VW7; -.
DR EPD; Q80VW7; -.
DR jPOST; Q80VW7; -.
DR MaxQB; Q80VW7; -.
DR PaxDb; Q80VW7; -.
DR PeptideAtlas; Q80VW7; -.
DR PRIDE; Q80VW7; -.
DR ProteomicsDB; 296154; -. [Q80VW7-1]
DR ProteomicsDB; 296155; -. [Q80VW7-2]
DR ProteomicsDB; 296156; -. [Q80VW7-3]
DR ProteomicsDB; 296157; -. [Q80VW7-4]
DR Antibodypedia; 54667; 42 antibodies from 14 providers.
DR Ensembl; ENSMUST00000035724; ENSMUSP00000041614; ENSMUSG00000039158. [Q80VW7-1]
DR GeneID; 100182; -.
DR KEGG; mmu:100182; -.
DR UCSC; uc008tgb.3; mouse. [Q80VW7-1]
DR UCSC; uc008tge.2; mouse. [Q80VW7-2]
DR CTD; 80709; -.
DR MGI; MGI:2140340; Akna.
DR VEuPathDB; HostDB:ENSMUSG00000039158; -.
DR eggNOG; ENOG502QRSN; Eukaryota.
DR GeneTree; ENSGT00940000154254; -.
DR HOGENOM; CLU_005641_0_0_1; -.
DR InParanoid; Q80VW7; -.
DR OMA; GTEVHWA; -.
DR OrthoDB; 112521at2759; -.
DR PhylomeDB; Q80VW7; -.
DR TreeFam; TF336885; -.
DR BioGRID-ORCS; 100182; 2 hits in 57 CRISPR screens.
DR PRO; PR:Q80VW7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q80VW7; protein.
DR Bgee; ENSMUSG00000039158; Expressed in granulocyte and 207 other tissues.
DR Genevisible; Q80VW7; MM.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0060232; P:delamination; IDA:UniProtKB.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IDA:UniProtKB.
DR GO; GO:0060234; P:neuroblast delamination; IDA:UniProtKB.
DR GO; GO:0021849; P:neuroblast division in subventricular zone; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:UniProtKB.
DR InterPro; IPR022150; AKNA_dom.
DR Pfam; PF12443; AKNA; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytoplasm; Cytoskeleton; DNA-binding;
KW Microtubule; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..1404
FT /note="Microtubule organization protein AKNA"
FT /id="PRO_0000289160"
FT DNA_BIND 1088..1096
FT /note="A.T hook"
FT REGION 1..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..787
FT /note="PEST"
FT REGION 755..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..906
FT /note="PEST"
FT REGION 1085..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1208..1235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..90
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..776
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..937
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z591"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z591"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z591"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 750
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z591"
FT MOD_RES 753
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z591"
FT MOD_RES 831
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z591"
FT MOD_RES 860
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z591"
FT MOD_RES 971
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z591"
FT MOD_RES 1144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z591"
FT MOD_RES 1339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z591"
FT MOD_RES 1352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z591"
FT MOD_RES 1389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z591"
FT VAR_SEQ 205..353
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_025941"
FT VAR_SEQ 512..530
FT /note="WPFPRTDLSPSSSPGVATP -> ELGKEPGLLSTPLLMEGEP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025942"
FT VAR_SEQ 531..1404
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025943"
FT VAR_SEQ 1226..1244
FT /note="SAVSRDTTRGSSAADTLRC -> KRQHFVQWRLKPLPTEKFY (in
FT isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_025944"
FT VAR_SEQ 1245..1404
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_025945"
FT CONFLICT 396
FT /note="S -> R (in Ref. 2; BAE32751)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="V -> M (in Ref. 1; BAC98278)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="P -> S (in Ref. 1; BAC98278)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="R -> Q (in Ref. 1; BAC98278)"
FT /evidence="ECO:0000305"
FT CONFLICT 712
FT /note="K -> E (in Ref. 1; BAC98278)"
FT /evidence="ECO:0000305"
FT CONFLICT 928..929
FT /note="Missing (in Ref. 1; BAC98278 and 4; AAH25835)"
FT /evidence="ECO:0000305"
FT CONFLICT 944
FT /note="P -> S (in Ref. 1; BAC98278 and 4; AAH25835)"
FT /evidence="ECO:0000305"
FT CONFLICT 956..958
FT /note="TET -> IEA (in Ref. 1; BAC98278 and 4; AAH25835)"
FT /evidence="ECO:0000305"
FT CONFLICT 963
FT /note="S -> T (in Ref. 1; BAC98278 and 4; AAH25835)"
FT /evidence="ECO:0000305"
FT CONFLICT 967..969
FT /note="QHF -> RHL (in Ref. 1; BAC98278 and 4; AAH25835)"
FT /evidence="ECO:0000305"
FT CONFLICT 1113
FT /note="R -> G (in Ref. 1; BAC98278 and 4; AAH25835)"
FT /evidence="ECO:0000305"
FT CONFLICT 1166
FT /note="P -> S (in Ref. 1; BAC98278 and 4; AAH25835)"
FT /evidence="ECO:0000305"
FT CONFLICT 1211
FT /note="P -> L (in Ref. 1; BAC98278 and 4; AAH25835)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1404 AA; 153123 MW; D24B6545BFA01372 CRC64;
MASSGAKAQW VGPSLGQGPR RRRWAWAEEQ DTDGRRDQGW GNSQSLPEAP SPELLEDFRR
AQEHLPPLEW DPDMQDSEES SGEETEADDA SSPEGSTVPL PWLSRSNQQL DMSEEELDEA
SGRPEVDLAG ESCTELECED QGDSSPPPPG QGPAKGWVTF IKQGSNYRPS EHLEAQPSVE
HSRTKSWSSG TVSLRQPSDS LGSTWEGDTE VPQPSILPKA LPQSPCHNFP HPGDRNGGDV
APATPTEFRD SLAAPAQNAE CSAGTWGEET TSLPSSRPED QTWKRTKTSP KPLPSRFTGS
VSPLSTRLGA IKKVVPQHKQ GATLAGHSSS QAPKYGRGRR LNYPLPDFSK VGPRVRFPKD
ENYRPPKSRG HNRQQGSTRP LIFKSPAEIV RDVLLSSGEA SLAKESSLAH TITRVPQEFQ
TPEQATELVH QLQEDYHKLL TKYAEAENTI DQLRLGAKVH LYSDPPQPSQ SFCSGSMPQG
SKVLSFSIPQ PRVAEWWPDP AQDPQASEAT GWPFPRTDLS PSSSPGVATP GRLPQSQGIA
TDQPSTGQTQ ALTSQASRLL AKVQSFEELV LAGHLPPQDQ IKSLEQLRAA HMALEAEYLQ
ACREELLDPQ LDASQGSPRT LNLCRELEAE IYHLGQRLEE LQDHMDQTQR ETEPCRPDLQ
DSTPTMSFLP QSAHLSMPSG PVSLPDGQTY QEPATTTTTS PGSSCTLPIN KKLSLSIKTE
ESPRGLPVPL RDRTLQVEQD FHGLLERYLS VKSLPEALRD EDEDDLEEEE EEQDHQGPLE
VDSPATAPGK TEAVRVPPGE RPTQAEESHR DATQEDEEQM GPMKSPDFRP SMARDTYTPV
LDTAEVAQRG TKAMVSHQSS LTSLEESRPS ELLPRKALLR AGGPHTEEPW MVSPETDSGF
VGSETSIVSP FTQTPEHRLS HVSTSGPSAQ HLTASVPGDR TSHPKARGLM VPRRATETGI
PRSRTQQHFS SLSSPGRGAQ SCHLEETSVA KIAVPRSEFK RQKQISKQLL PSGRTSPDSA
PAPTAASTPH GSAESTANLL LNRTERDQAI KDLQAEVSRL RLQLEDSLHR PHPDGPACVA
SAFNHSTQTQ EKLGSSPSWG PHYGSKSTER LSREPNGVEP AEPMGRRRAR SSSVPRDVPR
LYLSSESESP APRLSSEKSR TFEEHPEAAQ WGTRPQSSSK RRERVSFRGQ YTGQEYHILS
PKAILKDSGT PSCPHCHPIR TQDTGSAVSR DTTRGSSAAD TLRCALCGEV KSSAEADGSS
SGPSEKNTPK KPSTPILKRK NRQTGSPVRM APGLWYLAAA PPAPAPPALA YISSAPIMPY
LPPTVYYAAP APTSAQTASP QPARGPRRTR HSVQLGLNDL EELQAALREA AQAAENVRST
TRQLSRSLSA DLRHARSLRG SCLF
