CAPS2_HUMAN
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 03-AUG-2022, entry version 162.
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};
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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; 16.
DR IntAct; Q86UW7; 17.
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; Q86UW7; -.
DR PeptideAtlas; Q86UW7; -.
DR PRIDE; Q86UW7; -.
DR ProteomicsDB; 69919; -. [Q86UW7-1]
DR ProteomicsDB; 69920; -. [Q86UW7-2]
DR ProteomicsDB; 69921; -. [Q86UW7-3]
DR Antibodypedia; 31729; 63 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 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; XLLCNGK; -.
DR OrthoDB; 138870at2759; -.
DR PhylomeDB; Q86UW7; -.
DR PathwayCommons; Q86UW7; -.
DR SignaLink; Q86UW7; -.
DR SIGNOR; Q86UW7; -.
DR BioGRID-ORCS; 93664; 11 hits in 1069 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 168 other tissues.
DR ExpressionAtlas; Q86UW7; baseline and differential.
DR Genevisible; Q86UW7; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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 Gene3D; 2.30.29.30; -; 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; PTHR12166; 1.
DR Pfam; PF06292; MUN; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM01145; DUF1041; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51258; MHD1; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
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
