EXOC1_HUMAN
ID EXOC1_HUMAN Reviewed; 894 AA.
AC Q9NV70; Q504V4; Q8WUE7; Q96T15; Q9NZE4;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Exocyst complex component 1;
DE AltName: Full=Exocyst complex component Sec3;
GN Name=EXOC1; Synonyms=SEC3, SEC3L1; ORFNames=BM-012;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 392-894 (ISOFORM 2).
RC TISSUE=Skin, and Testis;
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 PROTEIN SEQUENCE OF 2-10.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 392-894 (ISOFORM 2).
RC TISSUE=Bone marrow;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [5]
RP IDENTIFICATION AS SEC3.
RX PubMed=11406615; DOI=10.1074/jbc.c100320200;
RA Brymora A., Valova V.A., Larsen M.R., Roufogalis B.D., Robinson P.J.;
RT "The brain exocyst complex interacts with RalA in a GTP-dependent manner:
RT identification of a novel mammalian Sec3 gene and a second Sec15 gene.";
RL J. Biol. Chem. 276:29792-29797(2001).
RN [6]
RP INTERACTION WITH SLC6A9, AND SUBCELLULAR LOCATION.
RX PubMed=16181645; DOI=10.1016/j.neuropharm.2005.07.021;
RA Cubelos B., Gimenez C., Zafra F.;
RT "The glycine transporter GLYT1 interacts with Sec3, a component of the
RT exocyst complex.";
RL Neuropharmacology 49:935-944(2005).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=16213214; DOI=10.1016/j.cell.2005.07.027;
RA Gromley A., Yeaman C., Rosa J., Redick S., Chen C.-T., Mirabelle S.,
RA Guha M., Sillibourne J., Doxsey S.J.;
RT "Centriolin anchoring of exocyst and SNARE complexes at the midbody is
RT required for secretory-vesicle-mediated abscission.";
RL Cell 123:75-87(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487 AND SER-501, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP INTERACTION WITH WEST NILE VIRUS AND DENGUE VIRUS CAPSID PROTEIN C,
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH EEF1A1.
RX PubMed=19889084; DOI=10.1111/j.1462-5822.2009.01407.x;
RA Bhuvanakantham R., Li J., Tan T.T., Ng M.L.;
RT "Human Sec3 protein is a novel transcriptional and translational repressor
RT of flavivirus.";
RL Cell. Microbiol. 12:453-472(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-471, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473 AND SER-501, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Component of the exocyst complex involved in the docking of
CC exocytic vesicles with fusion sites on the plasma membrane.
CC -!- FUNCTION: (Microbial infection) Has an antiviral effect against
CC flaviviruses by affecting viral RNA transcription and translation
CC through the sequestration of elongation factor 1-alpha (EEF1A1). This
CC results in decreased viral RNA synthesis and decreased viral protein
CC translation. {ECO:0000269|PubMed:19889084}.
CC -!- SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4,
CC EXOC5, EXOC6, EXOC7 and EXOC8. Interacts with EEF1A1 (PubMed:19889084).
CC Interacts with SLC6A9; interaction increases the transporter capacity
CC of SLC6A9 probably by promoting its insertion into the cell membrane
CC (PubMed:16181645). {ECO:0000269|PubMed:16181645,
CC ECO:0000269|PubMed:19889084}.
CC -!- SUBUNIT: (Microbial infection) Interacts with West Nile virus and
CC Dengue virus capsid protein C; this interaction results in EXOC1
CC degradation through the proteasome degradation pathway.
CC {ECO:0000269|PubMed:19889084}.
CC -!- INTERACTION:
CC Q9NV70; P18848: ATF4; NbExp=3; IntAct=EBI-1045313, EBI-492498;
CC Q9NV70; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-1045313, EBI-10175300;
CC Q9NV70; Q96KP1: EXOC2; NbExp=6; IntAct=EBI-1045313, EBI-465715;
CC Q9NV70; Q96A65: EXOC4; NbExp=5; IntAct=EBI-1045313, EBI-355383;
CC Q9NV70; Q7Z3B4: NUP54; NbExp=4; IntAct=EBI-1045313, EBI-741048;
CC Q9NV70; A8K0Z3: WASHC1; NbExp=2; IntAct=EBI-1045313, EBI-6160405;
CC -!- SUBCELLULAR LOCATION: Midbody, Midbody ring
CC {ECO:0000269|PubMed:16213214}. Cytoplasm {ECO:0000269|PubMed:16181645,
CC ECO:0000269|PubMed:19889084}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:19889084}. Cell membrane
CC {ECO:0000269|PubMed:16181645}. Note=Colocalizes with CNTRL/centriolin
CC at the midbody ring (PubMed:16213214). Localizes in cell membrane in
CC the presence of SLC6A9 (PubMed:16181645). {ECO:0000269|PubMed:16181645,
CC ECO:0000269|PubMed:16213214}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NV70-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NV70-2; Sequence=VSP_001481;
CC -!- SIMILARITY: Belongs to the SEC3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF64268.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK001755; BAA91886.1; -; mRNA.
DR EMBL; AK027413; BAB55095.1; -; mRNA.
DR EMBL; BC020650; AAH20650.1; -; mRNA.
DR EMBL; BC094751; AAH94751.1; -; mRNA.
DR EMBL; AF208854; AAF64268.1; ALT_INIT; mRNA.
DR CCDS; CCDS3502.1; -. [Q9NV70-1]
DR CCDS; CCDS3503.1; -. [Q9NV70-2]
DR RefSeq; NP_001020095.1; NM_001024924.1. [Q9NV70-1]
DR RefSeq; NP_060731.2; NM_018261.3. [Q9NV70-1]
DR RefSeq; NP_839955.1; NM_178237.2. [Q9NV70-2]
DR RefSeq; XP_016863898.1; XM_017008409.1.
DR AlphaFoldDB; Q9NV70; -.
DR SMR; Q9NV70; -.
DR BioGRID; 120881; 135.
DR ComplexPortal; CPX-4943; Exocyst, EXOC6 variant.
DR ComplexPortal; CPX-4944; Exocyst, EXOC6B variant.
DR CORUM; Q9NV70; -.
DR DIP; DIP-37579N; -.
DR IntAct; Q9NV70; 139.
DR MINT; Q9NV70; -.
DR STRING; 9606.ENSP00000370695; -.
DR TCDB; 1.F.2.1.2; the octameric exocyst (exocyst) family.
DR iPTMnet; Q9NV70; -.
DR PhosphoSitePlus; Q9NV70; -.
DR BioMuta; EXOC1; -.
DR DMDM; 24418677; -.
DR EPD; Q9NV70; -.
DR jPOST; Q9NV70; -.
DR MassIVE; Q9NV70; -.
DR MaxQB; Q9NV70; -.
DR PaxDb; Q9NV70; -.
DR PeptideAtlas; Q9NV70; -.
DR PRIDE; Q9NV70; -.
DR ProteomicsDB; 82754; -. [Q9NV70-1]
DR ProteomicsDB; 82755; -. [Q9NV70-2]
DR Antibodypedia; 23967; 102 antibodies from 23 providers.
DR DNASU; 55763; -.
DR Ensembl; ENST00000346134.11; ENSP00000326514.7; ENSG00000090989.18. [Q9NV70-1]
DR Ensembl; ENST00000349598.6; ENSP00000334431.6; ENSG00000090989.18. [Q9NV70-2]
DR Ensembl; ENST00000381295.7; ENSP00000370695.2; ENSG00000090989.18. [Q9NV70-1]
DR GeneID; 55763; -.
DR KEGG; hsa:55763; -.
DR MANE-Select; ENST00000381295.7; ENSP00000370695.2; NM_001024924.2; NP_001020095.1.
DR UCSC; uc003hbe.2; human. [Q9NV70-1]
DR CTD; 55763; -.
DR DisGeNET; 55763; -.
DR GeneCards; EXOC1; -.
DR HGNC; HGNC:30380; EXOC1.
DR HPA; ENSG00000090989; Low tissue specificity.
DR MIM; 607879; gene.
DR neXtProt; NX_Q9NV70; -.
DR OpenTargets; ENSG00000090989; -.
DR PharmGKB; PA134891660; -.
DR VEuPathDB; HostDB:ENSG00000090989; -.
DR eggNOG; KOG2148; Eukaryota.
DR GeneTree; ENSGT00940000158640; -.
DR HOGENOM; CLU_015381_1_0_1; -.
DR InParanoid; Q9NV70; -.
DR OMA; KEAKKCY; -.
DR OrthoDB; 201698at2759; -.
DR PhylomeDB; Q9NV70; -.
DR TreeFam; TF314195; -.
DR PathwayCommons; Q9NV70; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-264876; Insulin processing.
DR Reactome; R-HSA-5620916; VxPx cargo-targeting to cilium.
DR SignaLink; Q9NV70; -.
DR BioGRID-ORCS; 55763; 367 hits in 1093 CRISPR screens.
DR ChiTaRS; EXOC1; human.
DR GeneWiki; EXOC1; -.
DR GenomeRNAi; 55763; -.
DR Pharos; Q9NV70; Tbio.
DR PRO; PR:Q9NV70; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9NV70; protein.
DR Bgee; ENSG00000090989; Expressed in gingival epithelium and 199 other tissues.
DR ExpressionAtlas; Q9NV70; baseline and differential.
DR Genevisible; Q9NV70; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0098592; C:cytoplasmic side of apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IBA:GO_Central.
DR GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0000281; P:mitotic cytokinesis; IC:ComplexPortal.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IDA:UniProtKB.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016241; P:regulation of macroautophagy; TAS:ParkinsonsUK-UCL.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IC:ComplexPortal.
DR GO; GO:0090522; P:vesicle tethering involved in exocytosis; IC:ComplexPortal.
DR InterPro; IPR028258; Sec3-PIP2_bind.
DR InterPro; IPR019160; Sec3_C.
DR Pfam; PF15277; Sec3-PIP2_bind; 1.
DR Pfam; PF09763; Sec3_C; 1.
DR SMART; SM01313; Sec3-PIP2_bind; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiviral defense; Cell membrane; Coiled coil;
KW Cytoplasm; Direct protein sequencing; Exocytosis; Host-virus interaction;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801"
FT CHAIN 2..894
FT /note="Exocyst complex component 1"
FT /id="PRO_0000118913"
FT REGION 439..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 152..174
FT /evidence="ECO:0000255"
FT COILED 205..259
FT /evidence="ECO:0000255"
FT COMPBIAS 439..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 471
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 444..459
FT /note="ATLPRKESAVKQETES -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11042152,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_001481"
FT CONFLICT 74
FT /note="D -> G (in Ref. 1; BAB55095)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="F -> L (in Ref. 1; BAA91886)"
FT /evidence="ECO:0000305"
FT CONFLICT 801
FT /note="Q -> R (in Ref. 1; BAA91886)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 894 AA; 101982 MW; F63C88E3A7F611BD CRC64;
MTAIKHALQR DIFTPNDERL LSIVNVCKAG KKKKNCFLCA TVTTERPVQV KVVKVKKSDK
GDFYKRQIAW ALRDLAVVDA KDAIKENPEF DLHFEKIYKW VASSTAEKNA FISCIWKLNQ
RYLRKKIDFV NVSSQLLEES VPSGENQSVT GGDEEVVDEY QELNAREEQD IEIMMEGCEY
AISNAEAFAE KLSRELQVLD GANIQSIMAS EKQVNILMKL LDEALKEVDQ IELKLSSYEE
MLQSVKEQMD QISESNHLIH LSNTNNVKLL SEIEFLVNHM DLAKGHIKAL QEGDLASSRG
IEACTNAADA LLQCMNVALR PGHDLLLAVK QQQQRFSDLR ELFARRLASH LNNVFVQQGH
DQSSTLAQHS VELTLPNHHP FHRDLLRYAK LMEWLKSTDY GKYEGLTKNY MDYLSRLYER
EIKDFFEVAK IKMTGTTKES KKFATLPRKE SAVKQETESL HGSSGKLTGS TSSLNKLSVQ
SSGNRRSQSS SLLDMGNMSA SDLDVADRTK FDKIFEQVLS ELEPLCLAEQ DFISKFFKLQ
QHQSMPGTMA EAEDLDGGTL SRQHNCGTPL PVSSEKDMIR QMMIKIFRCI EPELNNLIAL
GDKIDSFNSL YMLVKMSHHV WTAQNVDPAS FLSTTLGNVL VTVKRNFDKC ISNQIRQMEE
VKISKKSKVG ILPFVAEFEE FAGLAESIFK NAERRGDLDK AYTKLIRGVF VNVEKVANES
QKTPRDVVMM ENFHHIFATL SRLKISCLEA EKKEAKQKYT DHLQSYVIYS LGQPLEKLNH
FFEGVEARVA QGIREEEVSY QLAFNKQELR KVIKEYPGKE VKKGLDNLYK KVDKHLCEEE
NLLQVVWHSM QDEFIRQYKH FEGLIARCYP GSGVTMEFTI QDILDYCSSI AQSH
