SH319_HUMAN
ID SH319_HUMAN Reviewed; 790 AA.
AC Q5HYK7; B7Z296; Q08EK1; Q32N10; Q5U3B8; Q86XB3; Q8N5E7; Q9UFC8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=SH3 domain-containing protein 19;
DE AltName: Full=ADAM-binding protein Eve-1;
DE AltName: Full=EEN-binding protein;
DE Short=EBP;
GN Name=SH3D19;
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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 275-790 (ISOFORM 1).
RC TISSUE=Amygdala;
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).
RC TISSUE=Colon endothelium, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 312-790 (ISOFORM 1).
RC TISSUE=Brain, Chondrosarcoma, and Lung;
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SH3GL1 AND SOS2.
RX PubMed=14551139; DOI=10.1182/blood-2003-07-2452;
RA Yam J.W., Jin D.Y., So C.W., Chan L.C.;
RT "Identification and characterization of EBP, a novel EEN binding protein
RT that inhibits Ras signaling and is recruited into the nucleus by the MLL-
RT EEN fusion protein.";
RL Blood 103:1445-1453(2004).
RN [7]
RP FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1; 2; 4 AND 5), TISSUE
RP SPECIFICITY, AND INTERACTION WITH ADAM9; ADAM10; ADAM12; ADAM15 AND ADAM17.
RX PubMed=15280379; DOI=10.1074/jbc.m400086200;
RA Tanaka M., Nanba D., Mori S., Shiba F., Ishiguro H., Yoshino K.,
RA Matsuura N., Higashiyama S.;
RT "ADAM binding protein Eve-1 is required for ectodomain shedding of
RT epidermal growth factor receptor ligands.";
RL J. Biol. Chem. 279:41950-41959(2004).
RN [8]
RP IDENTIFICATION BY 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 [9]
RP FUNCTION.
RX PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT "Identification and characterization of a set of conserved and new
RT regulators of cytoskeletal organisation, cell morphology and migration.";
RL BMC Biol. 9:54-54(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-762, 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: May play a role in regulating A disintegrin and
CC metalloproteases (ADAMs) in the signaling of EGFR-ligand shedding. May
CC be involved in suppression of Ras-induced cellular transformation and
CC Ras-mediated activation of ELK1. Plays a role in the regulation of cell
CC morphology and cytoskeletal organization. {ECO:0000269|PubMed:14551139,
CC ECO:0000269|PubMed:15280379, ECO:0000269|PubMed:21834987}.
CC -!- SUBUNIT: Interacts with ADAM12. Isoform 4 and isoform 5 (but not
CC isoform 1 and isoform 2) interact with ADAM9, ADAM10, ADAM15 and
CC ADAM17. Interacts with SH3GL1 SH3 domain. Interacts via SH3 3 and SH3 4
CC or SH3 4 and SH3 5 domains with SOS2. Probably forms a trimeric complex
CC with SH3GL1 and SOS2. Interacts with SH3YL1 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q5HYK7; Q96HL8: SH3YL1; NbExp=3; IntAct=EBI-2563437, EBI-722667;
CC Q5HYK7-2; Q96HL8: SH3YL1; NbExp=7; IntAct=EBI-14699032, EBI-722667;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14551139}. Nucleus
CC {ECO:0000269|PubMed:14551139}. Note=Is recruited to the nucleus by the
CC KMT2A/MLL1-EEN fusion protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Eve-1a;
CC IsoId=Q5HYK7-1; Sequence=Displayed;
CC Name=2; Synonyms=Eve-1b;
CC IsoId=Q5HYK7-2; Sequence=VSP_031184;
CC Name=3;
CC IsoId=Q5HYK7-3; Sequence=VSP_031183, VSP_031184;
CC Name=4; Synonyms=Eve-1c;
CC IsoId=Q5HYK7-4; Sequence=VSP_031182;
CC Name=5; Synonyms=Eve-1d;
CC IsoId=Q5HYK7-5; Sequence=VSP_031182, VSP_031184;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in heart,
CC skeletal muscle, kidney, liver, placenta, small intestine and lung.
CC Expressed at low levels in colon, thymus, spleen and leukocytes.
CC {ECO:0000269|PubMed:15280379}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI08891.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI08892.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI08893.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI08894.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAF83714.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAI46052.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK291025; BAF83714.1; ALT_INIT; mRNA.
DR EMBL; AK294476; BAH11782.1; -; mRNA.
DR EMBL; AL133047; CAB61374.1; -; mRNA.
DR EMBL; BX647422; CAI46052.1; ALT_INIT; mRNA.
DR EMBL; AC095055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471056; EAX04986.1; -; Genomic_DNA.
DR EMBL; BC032468; AAH32468.1; -; mRNA.
DR EMBL; BC045742; AAH45742.1; -; mRNA.
DR EMBL; BC085613; AAH85613.2; -; mRNA.
DR EMBL; BC108890; AAI08891.1; ALT_INIT; mRNA.
DR EMBL; BC108891; AAI08892.1; ALT_INIT; mRNA.
DR EMBL; BC108892; AAI08893.1; ALT_INIT; mRNA.
DR EMBL; BC108893; AAI08894.1; ALT_INIT; mRNA.
DR CCDS; CCDS34077.2; -. [Q5HYK7-1]
DR CCDS; CCDS47143.1; -. [Q5HYK7-3]
DR CCDS; CCDS47144.1; -. [Q5HYK7-2]
DR RefSeq; NP_001009555.3; NM_001009555.3. [Q5HYK7-1]
DR RefSeq; NP_001122395.1; NM_001128923.1. [Q5HYK7-2]
DR RefSeq; NP_001122396.1; NM_001128924.1. [Q5HYK7-3]
DR RefSeq; NP_001230278.1; NM_001243349.1. [Q5HYK7-2]
DR RefSeq; XP_005262824.1; XM_005262767.2. [Q5HYK7-1]
DR RefSeq; XP_011529948.1; XM_011531646.1. [Q5HYK7-1]
DR RefSeq; XP_011529951.1; XM_011531649.1.
DR RefSeq; XP_016863268.1; XM_017007779.1. [Q5HYK7-3]
DR RefSeq; XP_016863270.1; XM_017007781.1.
DR RefSeq; XP_016863271.1; XM_017007782.1.
DR RefSeq; XP_016863272.1; XM_017007783.1.
DR AlphaFoldDB; Q5HYK7; -.
DR SMR; Q5HYK7; -.
DR BioGRID; 127448; 41.
DR IntAct; Q5HYK7; 14.
DR MINT; Q5HYK7; -.
DR STRING; 9606.ENSP00000302913; -.
DR GlyGen; Q5HYK7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5HYK7; -.
DR PhosphoSitePlus; Q5HYK7; -.
DR BioMuta; SH3D19; -.
DR DMDM; 166977688; -.
DR EPD; Q5HYK7; -.
DR jPOST; Q5HYK7; -.
DR MassIVE; Q5HYK7; -.
DR MaxQB; Q5HYK7; -.
DR PaxDb; Q5HYK7; -.
DR PeptideAtlas; Q5HYK7; -.
DR PRIDE; Q5HYK7; -.
DR ProteomicsDB; 62944; -. [Q5HYK7-1]
DR ProteomicsDB; 62945; -. [Q5HYK7-2]
DR ProteomicsDB; 62946; -. [Q5HYK7-3]
DR ProteomicsDB; 62947; -. [Q5HYK7-4]
DR ProteomicsDB; 62948; -. [Q5HYK7-5]
DR ABCD; Q5HYK7; 7 sequenced antibodies.
DR Antibodypedia; 2969; 105 antibodies from 20 providers.
DR DNASU; 152503; -.
DR Ensembl; ENST00000304527.8; ENSP00000302913.4; ENSG00000109686.19. [Q5HYK7-1]
DR Ensembl; ENST00000409252.6; ENSP00000386848.2; ENSG00000109686.19. [Q5HYK7-1]
DR Ensembl; ENST00000409598.8; ENSP00000387030.4; ENSG00000109686.19. [Q5HYK7-2]
DR Ensembl; ENST00000427414.2; ENSP00000415694.1; ENSG00000109686.19. [Q5HYK7-3]
DR Ensembl; ENST00000514152.5; ENSP00000423449.1; ENSG00000109686.19. [Q5HYK7-2]
DR GeneID; 152503; -.
DR KEGG; hsa:152503; -.
DR UCSC; uc003imc.3; human. [Q5HYK7-1]
DR CTD; 152503; -.
DR GeneCards; SH3D19; -.
DR HGNC; HGNC:30418; SH3D19.
DR HPA; ENSG00000109686; Low tissue specificity.
DR MIM; 608674; gene.
DR neXtProt; NX_Q5HYK7; -.
DR OpenTargets; ENSG00000109686; -.
DR PharmGKB; PA162403244; -.
DR VEuPathDB; HostDB:ENSG00000109686; -.
DR eggNOG; KOG4225; Eukaryota.
DR GeneTree; ENSGT00940000155694; -.
DR HOGENOM; CLU_015305_2_0_1; -.
DR InParanoid; Q5HYK7; -.
DR OMA; VHKSCMK; -.
DR OrthoDB; 288421at2759; -.
DR PhylomeDB; Q5HYK7; -.
DR TreeFam; TF330850; -.
DR PathwayCommons; Q5HYK7; -.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR SignaLink; Q5HYK7; -.
DR BioGRID-ORCS; 152503; 9 hits in 1078 CRISPR screens.
DR ChiTaRS; SH3D19; human.
DR GenomeRNAi; 152503; -.
DR Pharos; Q5HYK7; Tbio.
DR PRO; PR:Q5HYK7; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q5HYK7; protein.
DR Bgee; ENSG00000109686; Expressed in tendon of biceps brachii and 176 other tissues.
DR ExpressionAtlas; Q5HYK7; baseline and differential.
DR Genevisible; Q5HYK7; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0070064; F:proline-rich region binding; IPI:BHF-UCL.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IMP:BHF-UCL.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB.
DR CDD; cd11814; SH3_Eve1_1; 1.
DR CDD; cd11816; SH3_Eve1_3; 1.
DR InterPro; IPR035834; Eve1_SH3_1.
DR InterPro; IPR035835; Eve1_SH3_3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00018; SH3_1; 4.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 5.
DR SUPFAM; SSF50044; SSF50044; 5.
DR PROSITE; PS50002; SH3; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..790
FT /note="SH3 domain-containing protein 19"
FT /id="PRO_0000318197"
FT DOMAIN 415..477
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 495..554
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 571..630
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 661..720
FT /note="SH3 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 730..789
FT /note="SH3 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 21..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..358
FT /note="Interaction with SH3GL1"
FT /evidence="ECO:0000269|PubMed:14551139"
FT COMPBIAS 286..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..351
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91X43"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91X43"
FT MOD_RES 762
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..370
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_031182"
FT VAR_SEQ 232..268
FT /note="DPFQLPAKTEPIKERAVQPAPTRKPTVIRIPAKPGKC -> G (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031183"
FT VAR_SEQ 415..437
FT /note="Missing (in isoform 2, isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_031184"
FT CONFLICT 1
FT /note="M -> V (in Ref. 2; CAI46052)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="K -> R (in Ref. 2; CAI46052)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="K -> E (in Ref. 2; CAI46052)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 790 AA; 86525 MW; FA860FB41FE8CDD5 CRC64;
MNIMNTEQSQ NSIVSRIKVF EGQTNIETSG LPKKPEITPR SLPPKPTVSS GKPSVAPKPA
ANRASGEWDS GTENRLKVTS KEGLTPYPPL QEAGSIPVTK PELPKKPNPG LIRSVNPEIP
GRGPLAESSD SGKKVPTPAP RPLLLKKSVS SENPTYPSAP LKPVTVPPRL AGASQAKAYK
SLGEGPPANP PVPVLQSKPL VDIDLISFDD DVLPTPSGNL AEESVGSEMV LDPFQLPAKT
EPIKERAVQP APTRKPTVIR IPAKPGKCLH EDPQSPPPLP AEKPIGNTFS TVSGKLSNVE
RTRNLESNHP GQTGGFVRVP PRLPPRPVNG KTIPTQQPPT KVPPERPPPP KLSATRRSNK
KLPFNRSSSD MDLQKKQSNL ATGLSKAKSQ VFKNQDPVLP PRPKPGHPLY SKYMLSVPHG
IANEDIVSQN PGELSCKRGD VLVMLKQTEN NYLECQKGED TGRVHLSQMK IITPLDEHLR
SRPNDPSHAQ KPVDSGAPHA VVLHDFPAEQ VDDLNLTSGE IVYLLEKIDT DWYRGNCRNQ
IGIFPANYVK VIIDIPEGGN GKRECVSSHC VKGSRCVARF EYIGEQKDEL SFSEGEIIIL
KEYVNEEWAR GEVRGRTGIF PLNFVEPVED YPTSGANVLS TKVPLKTKKE DSGSNSQVNS
LPAEWCEALH SFTAETSDDL SFKRGDRIQI LERLDSDWCR GRLQDREGIF PAVFVRPCPA
EAKSMLAIVP KGRKAKALYD FRGENEDELS FKAGDIITEL ESVDDDWMSG ELMGKSGIFP
KNYIQFLQIS
