MCTP2_HUMAN
ID MCTP2_HUMAN Reviewed; 878 AA.
AC Q6DN12; A2RRC2; C6G483; C6G484; Q49AB0; Q8TAX2; Q9NUS2; Q9NUW7;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Multiple C2 and transmembrane domain-containing protein 2;
GN Name=MCTP2;
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), AND COFACTOR.
RX PubMed=15528213; DOI=10.1074/jbc.m407305200;
RA Shin O.H., Han W., Wang Y., Sudhof T.C.;
RT "Evolutionarily conserved multiple C2 domain proteins with two
RT transmembrane regions (MCTPs) and unusual Ca2+ binding properties.";
RL J. Biol. Chem. 280:1641-1651(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5).
RC TISSUE=Brain, Lung, and Pancreas;
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 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 [7]
RP POTENTIAL INVOLVEMENT IN CONGENITAL LEFT HEART OBSTRUCTIVE DEFECTS,
RP VARIANTS HIS-46; HIS-47; THR-60; ASP-203; CYS-235; ILE-475 AND VAL-695,
RP CHARACTERIZATION OF VARIANTS ASP-203 AND CYS-235, AND FUNCTION.
RX PubMed=23773997; DOI=10.1093/hmg/ddt283;
RA Lalani S.R., Ware S.M., Wang X., Zapata G., Tian Q., Franco L.M., Jiang Z.,
RA Bucasas K., Scott D.A., Campeau P.M., Hanchard N., Umana L., Cast A.,
RA Patel A., Cheung S.W., McBride K.L., Bray M., Craig Chinault A.,
RA Boggs B.A., Huang M., Baker M.R., Hamilton S., Towbin J., Jefferies J.L.,
RA Fernbach S.D., Potocki L., Belmont J.W.;
RT "MCTP2 is a dosage-sensitive gene required for cardiac outflow tract
RT development.";
RL Hum. Mol. Genet. 22:4339-4348(2013).
RN [8]
RP STRUCTURE BY NMR OF 504-629.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the second C2 domain from human MCTP2 protein.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: Might play a role in the development of cardiac outflow
CC tract. {ECO:0000269|PubMed:23773997}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041,
CC ECO:0000269|PubMed:15528213};
CC Note=Binds Ca(2+) via the C2 domains in absence of phospholipids.
CC {ECO:0000269|PubMed:15528213};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q6DN12-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6DN12-2; Sequence=VSP_026664;
CC Name=3;
CC IsoId=Q6DN12-3; Sequence=VSP_026662;
CC Name=4;
CC IsoId=Q6DN12-4; Sequence=VSP_026662, VSP_026665, VSP_026666;
CC Name=5;
CC IsoId=Q6DN12-6; Sequence=VSP_038981, VSP_038982;
CC -!- DISEASE: Note=Heterozygosity for a 2.2-Mb deletion at chromosome
CC 15q26.2, encompassing MCTP2, has been identified in a 10-year-old girl
CC and her 3-year-old half brother, who had both coarctation of the aorta
CC associated with dysmorphic features and ventricular septal defects. An
CC intragenic MCTP2 duplication, leading to premature truncation (F697X)
CC within the first transmembrane region of the protein, has also been
CC observed in a male patient with a non-syndromic complex cardiac
CC malformation involving coarctation, hypoplastic left heart, mitral
CC atresia, bicuspid aortic valve and muscular ventricular septal defect.
CC Although the link between left ventricular outflow tract malformations
CC and MCTP2 could not be established, it has been proposed that defects
CC in the MCTP2 gene may contribute to phenotype. This hypothesis is
CC supported by the observation that Xenopus laevis embryos treated with
CC MCTP2 morpholinos show no evidence of endocardial cushion formation at
CC any level of the developing outflow tract (PubMed:23773997).
CC {ECO:0000269|PubMed:23773997}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MCTP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH41387.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=BAA91998.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY656717; AAT73060.1; -; mRNA.
DR EMBL; AK001953; BAA91998.1; ALT_INIT; mRNA.
DR EMBL; AK002037; BAA92048.1; -; mRNA.
DR EMBL; FJ515839; ACS13731.1; -; Genomic_DNA.
DR EMBL; FJ515839; ACS13732.1; -; Genomic_DNA.
DR EMBL; AC103749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC135626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025708; AAH25708.1; -; mRNA.
DR EMBL; BC041387; AAH41387.1; ALT_SEQ; mRNA.
DR EMBL; BC111024; AAI11025.1; -; mRNA.
DR EMBL; BC131527; AAI31528.1; -; mRNA.
DR CCDS; CCDS32338.1; -. [Q6DN12-1]
DR CCDS; CCDS53975.1; -. [Q6DN12-2]
DR CCDS; CCDS53976.1; -. [Q6DN12-4]
DR RefSeq; NP_001153115.1; NM_001159643.1. [Q6DN12-2]
DR RefSeq; NP_001153116.1; NM_001159644.1. [Q6DN12-4]
DR RefSeq; NP_060819.3; NM_018349.3. [Q6DN12-1]
DR RefSeq; XP_005255012.1; XM_005254955.3.
DR RefSeq; XP_005255017.1; XM_005254960.2. [Q6DN12-3]
DR RefSeq; XP_006720666.1; XM_006720603.2.
DR RefSeq; XP_011520073.1; XM_011521771.2.
DR RefSeq; XP_011520074.1; XM_011521772.2.
DR RefSeq; XP_016877893.1; XM_017022404.1. [Q6DN12-2]
DR RefSeq; XP_016877894.1; XM_017022405.1. [Q6DN12-2]
DR PDB; 2EP6; NMR; -; A=504-629.
DR PDBsum; 2EP6; -.
DR AlphaFoldDB; Q6DN12; -.
DR SMR; Q6DN12; -.
DR BioGRID; 120898; 7.
DR IntAct; Q6DN12; 1.
DR STRING; 9606.ENSP00000350377; -.
DR TCDB; 9.A.57.1.6; the extended-synaptotagmin (e-syt) family.
DR iPTMnet; Q6DN12; -.
DR PhosphoSitePlus; Q6DN12; -.
DR BioMuta; MCTP2; -.
DR DMDM; 294862501; -.
DR EPD; Q6DN12; -.
DR jPOST; Q6DN12; -.
DR MassIVE; Q6DN12; -.
DR MaxQB; Q6DN12; -.
DR PaxDb; Q6DN12; -.
DR PeptideAtlas; Q6DN12; -.
DR PRIDE; Q6DN12; -.
DR ProteomicsDB; 66238; -. [Q6DN12-1]
DR ProteomicsDB; 66239; -. [Q6DN12-2]
DR ProteomicsDB; 66240; -. [Q6DN12-3]
DR ProteomicsDB; 66241; -. [Q6DN12-4]
DR ProteomicsDB; 66242; -. [Q6DN12-6]
DR Antibodypedia; 29077; 166 antibodies from 23 providers.
DR DNASU; 55784; -.
DR Ensembl; ENST00000357742.10; ENSP00000350377.4; ENSG00000140563.16. [Q6DN12-1]
DR Ensembl; ENST00000451018.7; ENSP00000395109.3; ENSG00000140563.16. [Q6DN12-2]
DR Ensembl; ENST00000456504.5; ENSP00000388887.1; ENSG00000140563.16. [Q6DN12-6]
DR Ensembl; ENST00000557742.1; ENSP00000454847.1; ENSG00000140563.16. [Q6DN12-4]
DR GeneID; 55784; -.
DR KEGG; hsa:55784; -.
DR MANE-Select; ENST00000357742.10; ENSP00000350377.4; NM_001385001.1; NP_001371930.1.
DR UCSC; uc002btj.4; human. [Q6DN12-1]
DR CTD; 55784; -.
DR DisGeNET; 55784; -.
DR GeneCards; MCTP2; -.
DR HGNC; HGNC:25636; MCTP2.
DR HPA; ENSG00000140563; Low tissue specificity.
DR MalaCards; MCTP2; -.
DR MIM; 616297; gene.
DR neXtProt; NX_Q6DN12; -.
DR OpenTargets; ENSG00000140563; -.
DR Orphanet; 1596; Distal monosomy 15q.
DR PharmGKB; PA142671473; -.
DR VEuPathDB; HostDB:ENSG00000140563; -.
DR eggNOG; KOG1030; Eukaryota.
DR GeneTree; ENSGT00940000156291; -.
DR HOGENOM; CLU_1371782_0_0_1; -.
DR InParanoid; Q6DN12; -.
DR OMA; HFEEQSA; -.
DR OrthoDB; 234298at2759; -.
DR PhylomeDB; Q6DN12; -.
DR TreeFam; TF323373; -.
DR PathwayCommons; Q6DN12; -.
DR SignaLink; Q6DN12; -.
DR BioGRID-ORCS; 55784; 9 hits in 1061 CRISPR screens.
DR ChiTaRS; MCTP2; human.
DR EvolutionaryTrace; Q6DN12; -.
DR GenomeRNAi; 55784; -.
DR Pharos; Q6DN12; Tbio.
DR PRO; PR:Q6DN12; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q6DN12; protein.
DR Bgee; ENSG00000140563; Expressed in germinal epithelium of ovary and 161 other tissues.
DR ExpressionAtlas; Q6DN12; baseline and differential.
DR Genevisible; Q6DN12; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IDA:HGNC-UCL.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IDA:HGNC-UCL.
DR GO; GO:0019722; P:calcium-mediated signaling; NAS:HGNC-UCL.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IBA:GO_Central.
DR Gene3D; 2.60.40.150; -; 3.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR013583; PRibTrfase_C.
DR Pfam; PF00168; C2; 3.
DR Pfam; PF08372; PRT_C; 1.
DR SMART; SM00239; C2; 3.
DR SUPFAM; SSF49562; SSF49562; 3.
DR PROSITE; PS50004; C2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Developmental protein;
KW Membrane; Metal-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..878
FT /note="Multiple C2 and transmembrane domain-containing
FT protein 2"
FT /id="PRO_0000294472"
FT TRANSMEM 697..717
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 802..822
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 177..292
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 334..452
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 494..607
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 20..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 265
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 265
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 270
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 525
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 525
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 531
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 577
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 577
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 579
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 579
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 585
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT VAR_SEQ 1..412
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_026662"
FT VAR_SEQ 177..199
FT /note="VPGEASDGLSNLPSPFAYLLTIH -> DSQKFEMTQKFNWAHVIHIQKQT
FT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038981"
FT VAR_SEQ 200..878
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038982"
FT VAR_SEQ 696..750
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026664"
FT VAR_SEQ 696..718
FT /note="VFLITVWNFELYMIPLALLLIFV -> HRKEEPPLSMKCTLFSGDIGPSL
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026665"
FT VAR_SEQ 719..878
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026666"
FT VARIANT 46
FT /note="R -> H (found in a patient with left-sided
FT obstructive cardiac lesions; unknown pathological
FT significance; dbSNP:rs61735139)"
FT /evidence="ECO:0000269|PubMed:23773997"
FT /id="VAR_073421"
FT VARIANT 47
FT /note="R -> H (found in a patient with left-sided
FT obstructive cardiac lesions; unknown pathological
FT significance; dbSNP:rs149133063)"
FT /evidence="ECO:0000269|PubMed:23773997"
FT /id="VAR_073422"
FT VARIANT 60
FT /note="A -> T (found in a patient with left-sided
FT obstructive cardiac lesions; unknown pathological
FT significance; dbSNP:rs143256791)"
FT /evidence="ECO:0000269|PubMed:23773997"
FT /id="VAR_073423"
FT VARIANT 203
FT /note="G -> D (found in a patient with left-sided
FT obstructive cardiac lesions; unknown pathological
FT significance; alters Ca(2+)-binding affinity;
FT dbSNP:rs201530723)"
FT /evidence="ECO:0000269|PubMed:23773997"
FT /id="VAR_073424"
FT VARIANT 235
FT /note="Y -> C (found in a patient with left-sided
FT obstructive cardiac lesions; unknown pathological
FT significance; alters Ca(2+)-binding affinity;
FT dbSNP:rs191271656)"
FT /evidence="ECO:0000269|PubMed:23773997"
FT /id="VAR_073425"
FT VARIANT 475
FT /note="V -> I (found in a patient with left-sided
FT obstructive cardiac lesions; unknown pathological
FT significance; dbSNP:rs200107854)"
FT /evidence="ECO:0000269|PubMed:23773997"
FT /id="VAR_073426"
FT VARIANT 695
FT /note="A -> V (found in a patient with left-sided
FT obstructive cardiac lesions; unknown pathological
FT significance; dbSNP:rs370153540)"
FT /evidence="ECO:0000269|PubMed:23773997"
FT /id="VAR_073427"
FT VARIANT 877
FT /note="A -> T (in dbSNP:rs34193492)"
FT /id="VAR_033190"
FT CONFLICT 403
FT /note="Q -> H (in Ref. 1; AAT73060)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="S -> P (in Ref. 1; AAT73060)"
FT /evidence="ECO:0000305"
FT STRAND 508..520
FT /evidence="ECO:0007829|PDB:2EP6"
FT STRAND 524..528
FT /evidence="ECO:0007829|PDB:2EP6"
FT STRAND 532..538
FT /evidence="ECO:0007829|PDB:2EP6"
FT STRAND 541..544
FT /evidence="ECO:0007829|PDB:2EP6"
FT STRAND 558..565
FT /evidence="ECO:0007829|PDB:2EP6"
FT STRAND 570..579
FT /evidence="ECO:0007829|PDB:2EP6"
FT STRAND 582..586
FT /evidence="ECO:0007829|PDB:2EP6"
FT STRAND 591..593
FT /evidence="ECO:0007829|PDB:2EP6"
FT HELIX 594..596
FT /evidence="ECO:0007829|PDB:2EP6"
FT STRAND 617..628
FT /evidence="ECO:0007829|PDB:2EP6"
SQ SEQUENCE 878 AA; 99596 MW; 96BD26FA822C1F49 CRC64;
MDLDKPSVWG SLKQRTRPLL INLSKKKVKK NPSKPPDLRA RHHLDRRLSL SVPDLLEAEA
LAPEGRPYSG PQSSYTSVPS SLSTAGIFPK SSSSSLKQSE EELDWSQEEA SHLHVVETDS
EEAYASPAER RRVSSNGIFD LQKTSLGGDA PEEPEKLCGS SDLNASMTSQ HFEEQSVPGE
ASDGLSNLPS PFAYLLTIHL KEGRNLVVRD RCGTSDPYVK FKLNGKTLYK SKVIYKNLNP
VWDEIVVLPI QSLDQKLRVK VYDRDLTTSD FMGSAFVILS DLELNRTTEH ILKLEDPNSL
EDDMGVIVLN LNLVVKQGDF KRHRWSNRKR LSASKSSLIR NLRLSESLKK NQLWNGIISI
TLLEGKNVSG GSMTEMFVQL KLGDQRYKSK TLCKSANPQW QEQFDFHYFS DRMGILDIEV
WGKDNKKHEE RLGTCKVDIS ALPLKQANCL ELPLDSCLGA LLMLVTLTPC AGVSVSDLCV
CPLADLSERK QITQRYCLQN SLKDVKDVGI LQVKVLKAAD LLAADFSGKS DPFCLLELGN
DRLQTHTVYK NLNPEWNKVF TFPIKDIHDV LEVTVFDEDG DKPPDFLGKV AIPLLSIRDG
QPNCYVLKNK DLEQAFKGVI YLEMDLIYNP VKASIRTFTP REKRFVEDSR KLSKKILSRD
VDRVKRITMA IWNTMQFLKS CFQWESTLRS TIAFAVFLIT VWNFELYMIP LALLLIFVYN
FIRPVKGKVS SIQDSQESTD IDDEEDEDDK ESEKKGLIER IYMVQDIVST VQNVLEEIAS
FGERIKNTFN WTVPFLSSLA CLILAAATII LYFIPLRYII LIWGINKFTK KLRNPYSIDN
NELLDFLSRV PSDVQKVQYA ELKLCSSHSP LRKKRSAL
