ID CAPS2_HUMAN Reviewed; 1296 AA. AC Q86UW7; A4D0X3; B7ZM56; Q658Q2; Q7Z5T7; Q8IZW9; Q8N7M4; Q9H6P4; Q9HCI1; AC Q9NWK8; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 10-JAN-2006, sequence version 2. DT 24-JAN-2024, entry version 170. DE RecName: Full=Calcium-dependent secretion activator 2; DE AltName: Full=Calcium-dependent activator protein for secretion 2; DE Short=CAPS-2; GN Name=CADPS2; Synonyms=CAPS2, KIAA1591; 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 [MRNA] (ISOFORM 1). RX PubMed=14530279; DOI=10.1074/jbc.m304727200; RA Speidel D., Varoqueaux F., Enk C., Nojiri M., Grishanin R.N., RA Martin T.F.J., Hofmann K., Brose N., Reim K.; RT "A family of Ca2+-dependent activator proteins for secretion: comparative RT analysis of structure, expression, localization, and function."; RL J. Biol. Chem. 278:52802-52809(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND VARIANT RP THR-298. RX PubMed=12659812; DOI=10.1016/s0888-7543(02)00040-x; RA Cisternas F.A., Vincent J.B., Scherer S.W., Ray P.N.; RT "Cloning and characterization of human CADPS and CADPS2, new members of the RT Ca2+-dependent activator for secretion protein family."; RL Genomics 81:279-291(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 1-180. RC TISSUE=Brain, 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-506 (ISOFORM 1), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 804-1296 (ISOFORM 2), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 353-1296 (ISOFORM 3). RC TISSUE=Hepatoma, and Trachea; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 238-1296 (ISOFORM 2). RX PubMed=10997877; DOI=10.1093/dnares/7.4.271; RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVIII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:273-281(2000). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 262-1296 (ISOFORM 2). RC TISSUE=Stomach; 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 [9] RP INTERACTION WITH DRD2. RX PubMed=15857609; DOI=10.1016/j.bcp.2005.02.015; RA Binda A.V., Kabbani N., Levenson R.; RT "Regulation of dense core vesicle release from PC12 cells by interaction RT between the D2 dopamine receptor and calcium-dependent activator protein RT for secretion (CAPS)."; RL Biochem. Pharmacol. 69:1451-1461(2005). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-58, AND RP IDENTIFICATION BY 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). CC -!- FUNCTION: Calcium-binding protein involved in exocytosis of vesicles CC filled with neurotransmitters and neuropeptides. Probably acts upstream CC of fusion in the biogenesis or maintenance of mature secretory CC vesicles. Regulates neurotrophin release from granule cells leading to CC regulate cell differentiation and survival during cerebellar CC development. May specifically mediate the Ca(2+)-dependent exocytosis CC of large dense-core vesicles (DCVs) and other dense-core vesicles (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Homodimer (By similarity). Interacts with the dopamine CC receptor DRD2. {ECO:0000250, ECO:0000269|PubMed:15857609}. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000305}; CC Peripheral membrane protein {ECO:0000305}; Cytoplasmic side CC {ECO:0000305}. Synapse. Note=Membrane-associated to vesicles. Strongly CC enriched in synaptic fractions. Probably localizes to different CC vesicles compared to CADPS. Enriched on vesicular structures in the CC parallel fiber terminal of granule cells that are distinct from CC synaptic vesicles. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q86UW7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q86UW7-2; Sequence=VSP_016815, VSP_016816, VSP_016817, CC VSP_016818; CC Name=3; CC IsoId=Q86UW7-3; Sequence=VSP_016815, VSP_016816, VSP_016817; CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in all adult and fetal CC tissues examined, with the strongest expression in kidney and pancreas. CC In brain, it is expressed at high levels in cerebellum, to a lesser CC degree in cerebral cortex, occipital pole, and frontal and temporal CC lobes. Only weakly expressed in medulla, spinal cord and putamen. CC {ECO:0000269|PubMed:12659812}. CC -!- DOMAIN: The PH domain is essential for regulated exocytosis and binds CC phospholipids. {ECO:0000250}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH54339.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=AK098170; Type=Miscellaneous discrepancy; Note=Chimera.; Evidence={ECO:0000305}; CC Sequence=BAA91372.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAB15210.1; 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; AY264289; AAP22132.1; -; mRNA. DR EMBL; AF401638; AAN38707.1; -; mRNA. DR EMBL; AC004594; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC004838; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC004986; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC006009; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC006463; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC015983; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC091438; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH236947; EAL24339.1; -; Genomic_DNA. DR EMBL; BC054339; AAH54339.1; ALT_SEQ; mRNA. DR EMBL; BC136601; AAI36602.1; -; mRNA. DR EMBL; BC144278; AAI44279.1; -; mRNA. DR EMBL; AK000768; BAA91372.1; ALT_INIT; mRNA. DR EMBL; AK025672; BAB15210.1; ALT_INIT; mRNA. DR EMBL; AK098170; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AB046811; BAB13417.1; -; mRNA. DR EMBL; AL833058; CAH56288.1; -; mRNA. DR CCDS; CCDS47691.1; -. [Q86UW7-2] DR CCDS; CCDS55158.1; -. [Q86UW7-1] DR RefSeq; NP_001009571.2; NM_001009571.3. [Q86UW7-2] DR RefSeq; NP_001161412.1; NM_001167940.1. DR RefSeq; NP_060424.9; NM_017954.10. [Q86UW7-1] DR AlphaFoldDB; Q86UW7; -. DR SMR; Q86UW7; -. DR BioGRID; 125051; 18. DR IntAct; Q86UW7; 19. DR MINT; Q86UW7; -. DR STRING; 9606.ENSP00000398481; -. DR DrugBank; DB11093; Calcium citrate. DR DrugBank; DB11348; Calcium Phosphate. DR DrugBank; DB14481; Calcium phosphate dihydrate. DR iPTMnet; Q86UW7; -. DR PhosphoSitePlus; Q86UW7; -. DR BioMuta; CADPS2; -. DR DMDM; 85540964; -. DR EPD; Q86UW7; -. DR jPOST; Q86UW7; -. DR MassIVE; Q86UW7; -. DR MaxQB; Q86UW7; -. DR PaxDb; 9606-ENSP00000398481; -. DR PeptideAtlas; Q86UW7; -. DR ProteomicsDB; 69919; -. [Q86UW7-1] DR ProteomicsDB; 69920; -. [Q86UW7-2] DR ProteomicsDB; 69921; -. [Q86UW7-3] DR Pumba; Q86UW7; -. DR Antibodypedia; 31729; 80 antibodies from 24 providers. DR DNASU; 93664; -. DR Ensembl; ENST00000412584.6; ENSP00000400401.2; ENSG00000081803.17. [Q86UW7-2] DR Ensembl; ENST00000449022.7; ENSP00000398481.2; ENSG00000081803.17. [Q86UW7-1] DR GeneID; 93664; -. DR KEGG; hsa:93664; -. DR MANE-Select; ENST00000449022.7; ENSP00000398481.2; NM_017954.11; NP_060424.9. DR UCSC; uc064hnn.1; human. [Q86UW7-1] DR AGR; HGNC:16018; -. DR CTD; 93664; -. DR DisGeNET; 93664; -. DR GeneCards; CADPS2; -. DR HGNC; HGNC:16018; CADPS2. DR HPA; ENSG00000081803; Tissue enhanced (brain). DR MIM; 609978; gene. DR neXtProt; NX_Q86UW7; -. DR OpenTargets; ENSG00000081803; -. DR PharmGKB; PA26025; -. DR VEuPathDB; HostDB:ENSG00000081803; -. DR eggNOG; KOG3543; Eukaryota. DR GeneTree; ENSGT00590000083094; -. DR InParanoid; Q86UW7; -. DR OMA; LSFTLEX; -. DR OrthoDB; 5399598at2759; -. DR PhylomeDB; Q86UW7; -. DR PathwayCommons; Q86UW7; -. DR SignaLink; Q86UW7; -. DR SIGNOR; Q86UW7; -. DR BioGRID-ORCS; 93664; 12 hits in 1147 CRISPR screens. DR ChiTaRS; CADPS2; human. DR GeneWiki; CADPS2; -. DR GenomeRNAi; 93664; -. DR Pharos; Q86UW7; Tbio. DR PRO; PR:Q86UW7; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q86UW7; Protein. DR Bgee; ENSG00000081803; Expressed in cerebellar vermis and 170 other cell types or tissues. DR ExpressionAtlas; Q86UW7; baseline and differential. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0098793; C:presynapse; IEA:GOC. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:1990504; P:dense core granule exocytosis; IEA:InterPro. DR GO; GO:0006887; P:exocytosis; IBA:GO_Central. DR GO; GO:0045921; P:positive regulation of exocytosis; IBA:GO_Central. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0016079; P:synaptic vesicle exocytosis; IEA:InterPro. DR CDD; cd01234; PH_CADPS; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR033227; CAPS. DR InterPro; IPR010439; MUN_dom. DR InterPro; IPR014770; Munc13_1. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR PANTHER; PTHR12166; CALCIUM-DEPENDENT SECRETION ACTIVATOR; 1. DR PANTHER; PTHR12166:SF7; CALCIUM-DEPENDENT SECRETION ACTIVATOR 2; 1. DR Pfam; PF06292; MUN; 2. DR Pfam; PF00169; PH; 1. DR SMART; SM01145; DUF1041; 1. DR SMART; SM00233; PH; 1. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS50004; C2; 1. DR PROSITE; PS51258; MHD1; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR Genevisible; Q86UW7; HS. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Cytoplasmic vesicle; Exocytosis; KW Lipid-binding; Membrane; Metal-binding; Phosphoprotein; Protein transport; KW Reference proteome; Synapse; Transport. FT CHAIN 1..1296 FT /note="Calcium-dependent secretion activator 2" FT /id="PRO_0000053868" FT DOMAIN 350..464 FT /note="C2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT DOMAIN 487..590 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 885..1056 FT /note="MHD1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00587" FT REGION 1..78 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 755..1074 FT /note="Interaction with DRD2" FT /evidence="ECO:0000269|PubMed:15857609" FT REGION 1274..1296 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..17 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 56 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 58 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1290 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BYR5" FT VAR_SEQ 618..621 FT /note="SGKD -> Y (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:10997877, FT ECO:0000303|PubMed:12659812, ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005" FT /id="VSP_016815" FT VAR_SEQ 860..862 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:10997877, FT ECO:0000303|PubMed:12659812, ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005" FT /id="VSP_016816" FT VAR_SEQ 963..1003 FT /note="KNIANSLPNVALPKVPSLPLNLPQIPNISTASWMPSLYEST -> N (in FT isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:10997877, FT ECO:0000303|PubMed:12659812, ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005" FT /id="VSP_016817" FT VAR_SEQ 1104 FT /note="E -> EFGSQW (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10997877, FT ECO:0000303|PubMed:12659812, ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005" FT /id="VSP_016818" FT VARIANT 298 FT /note="A -> T (in dbSNP:rs17144625)" FT /evidence="ECO:0000269|PubMed:12659812" FT /id="VAR_024786" FT CONFLICT 44..47 FT /note="APGR -> GRG (in Ref. 2; AAN38707)" FT /evidence="ECO:0000305" FT CONFLICT 90 FT /note="F -> L (in Ref. 1; AAP22132)" FT /evidence="ECO:0000305" FT CONFLICT 360 FT /note="D -> G (in Ref. 1; AAP22132)" FT /evidence="ECO:0000305" FT CONFLICT 457 FT /note="S -> T (in Ref. 6; AK098170)" FT /evidence="ECO:0000305" FT CONFLICT 488 FT /note="M -> I (in Ref. 2; AAN38707)" FT /evidence="ECO:0000305" FT CONFLICT 579 FT /note="I -> V (in Ref. 6; BAB15210)" FT /evidence="ECO:0000305" FT CONFLICT 1068 FT /note="S -> G (in Ref. 6; BAB15210)" FT /evidence="ECO:0000305" SQ SEQUENCE 1296 AA; 147735 MW; 7BF3456F3D90410C CRC64; MLDPSSSEEE SDEGLEEESR DVLVAAGSSQ RAPPAPTREG RRDAPGRAGG GGAARSVSPS PSVLSEGRDE PQRQLDDEQE RRIRLQLYVF VVRCIAYPFN AKQPTDMARR QQKLNKQQLQ LLKERFQAFL NGETQIVADE AFCNAVRSYY EVFLKSDRVA RMVQSGGCSA NDFREVFKKN IEKRVRSLPE IDGLSKETVL SSWIAKYDAI YRGEEDLCKQ PNRMALSAVS ELILSKEQLY EMFQQILGIK KLEHQLLYNA CQLDNADEQA AQIRRELDGR LQLADKMAKE RKFPKFIAKD MENMYIEELR SSVNLLMANL ESLPVSKGGP EFKLQKLKRS QNSAFLDIGD ENEIQLSKSD VVLSFTLEIV IMEVQGLKSV APNRIVYCTM EVEGEKLQTD QAEASRPQWG TQGDFTTTHP RPVVKVKLFT ESTGVLALED KELGRVILYP TSNSSKSAEL HRMVVPKNSQ DSDLKIKLAV RMDKPAHMKH SGYLYALGQK VWKRWKKRYF VLVQVSQYTF AMCSYREKKS EPQELMQLEG YTVDYTDPHP GLQGGCMFFN AVKEGDTVIF ASDDEQDRIL WVQAMYRATG QSYKPVPAIQ TQKLNPKGGT LHADAQLSGK DADRFQKHGM DEFISANPCK LDHAFLFRIL QRQTLDHRLN DSYSCLGWFS PGQVFVLDEY CARYGVRGCH RHLCYLAELM EHSENGAVID PTLLHYSFAF CASHVHGNRP DGIGTVSVEE KERFEEIKER LSSLLENQIS HFRYCFPFGR PEGALKATLS LLERVLMKDI ATPIPAEEVK KVVRKCLEKA ALINYTRLTE YAKIEETMNQ ASPARKLEEI LHLAELCIEV LQQNEEHHAE GREAFAWWPD LLAEHAEKFW ALFTVDMDTA LEAQPQDSWD SFPLFQLLNN FLRNDTLLCN GKFHKHLQEI FVPLVVRYVD LMESSIAQSI HRGFEQETWQ PVKNIANSLP NVALPKVPSL PLNLPQIPNI STASWMPSLY ESTNGSATSE DLFWKLDALQ MFVFDLHWPE QEFAHHLEQR LKLMASDMLE ACVKRTRTAF ELKLQKASKT TDLRIPASVC TMFNVLVDAK KQSTKLCALD GGQEQQYHSK IDDLIDNSVK EIISLLVSKF VSVLEGVLSK LSRYDEGTFF SSILSFTVKA AAKYVDVPKP GMDLADTYIM FVRQNQDILR EKVNEEMYIE KLFDQWYSSS MKVICVWLTD RLDLQLHIYQ LKTLIKIVKK TYRDFRLQGV LEGTLNSKTY DTVHRRLTVE EATASVSEGG GLQGITMKDS DEEEEG //