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 27-MAR-2024, entry version 151. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. DR RefSeq; XP_011529948.1; XM_011531646.1. DR RefSeq; XP_011529951.1; XM_011531649.1. DR RefSeq; XP_016863268.1; XM_017007779.1. 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; 55. DR IntAct; Q5HYK7; 22. 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; 9606-ENSP00000302913; -. DR PeptideAtlas; 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 Pumba; Q5HYK7; -. DR ABCD; Q5HYK7; 7 sequenced antibodies. DR Antibodypedia; 2969; 122 antibodies from 20 providers. DR DNASU; 152503; -. DR Ensembl; ENST00000409252.6; ENSP00000386848.2; ENSG00000109686.20. [Q5HYK7-1] DR Ensembl; ENST00000409598.8; ENSP00000387030.4; ENSG00000109686.20. [Q5HYK7-2] DR Ensembl; ENST00000427414.2; ENSP00000415694.1; ENSG00000109686.20. [Q5HYK7-3] DR Ensembl; ENST00000514152.5; ENSP00000423449.1; ENSG00000109686.20. [Q5HYK7-2] DR Ensembl; ENST00000709914.1; ENSP00000517934.1; ENSG00000292165.1. [Q5HYK7-2] DR Ensembl; ENST00000709915.1; ENSP00000517935.1; ENSG00000292165.1. [Q5HYK7-1] DR Ensembl; ENST00000709917.1; ENSP00000517936.1; ENSG00000292165.1. [Q5HYK7-2] DR Ensembl; ENST00000709920.1; ENSP00000517939.1; ENSG00000292165.1. [Q5HYK7-3] DR Ensembl; ENST00000709926.1; ENSP00000517941.1; ENSG00000292165.1. [Q5HYK7-1] DR GeneID; 152503; -. DR KEGG; hsa:152503; -. DR UCSC; uc003imc.3; human. [Q5HYK7-1] DR AGR; HGNC:30418; -. 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; 2920126at2759; -. 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 1156 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 178 other cell types or tissues. DR ExpressionAtlas; Q5HYK7; baseline and differential. 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; cd11815; SH3_Eve1_2; 1. DR CDD; cd11816; SH3_Eve1_3; 1. DR CDD; cd11817; SH3_Eve1_4; 1. DR CDD; cd11818; SH3_Eve1_5; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 4. 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 PANTHER; PTHR45929; JAK PATHWAY SIGNAL TRANSDUCTION ADAPTOR MOLECULE; 1. DR Pfam; PF00018; SH3_1; 3. DR Pfam; PF07653; SH3_2; 1. DR Pfam; PF14604; SH3_9; 1. DR PRINTS; PR00499; P67PHOX. DR PRINTS; PR00452; SH3DOMAIN. DR SMART; SM00326; SH3; 5. DR SUPFAM; SSF50044; SH3-domain; 5. DR PROSITE; PS50002; SH3; 5. DR Genevisible; Q5HYK7; HS. 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 //