SYT6_HUMAN
ID SYT6_HUMAN Reviewed; 510 AA.
AC Q5T7P8; B1AMB8; B3KPK1;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Synaptotagmin-6;
DE AltName: Full=Synaptotagmin VI;
DE Short=SytVI;
GN Name=SYT6;
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).
RC TISSUE=Teratocarcinoma;
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 GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION BY
RP 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: May be involved in Ca(2+)-dependent exocytosis of secretory
CC vesicles through Ca(2+) and phospholipid binding to the C2 domain or
CC may serve as Ca(2+) sensors in the process of vesicular trafficking and
CC exocytosis. May mediate Ca(2+)-regulation of exocytosis in acrosomal
CC reaction in sperm (By similarity). {ECO:0000250|UniProtKB:Q9R0N8}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2
CC domains. {ECO:0000250|UniProtKB:P40748};
CC -!- SUBUNIT: Isoform 1: Homodimer; disulfide-linked via the cysteine motif.
CC Isoform 1: Can also form heterodimers with SYT3, SYT7, SYT9 and SYT10.
CC Isoform 1: Interacts with STX1A, STX1B and STX2; the interaction is
CC Ca(2+)-dependent. Isoform 2: Is not able to form homodimer and
CC heterodimers. {ECO:0000250|UniProtKB:Q9R0N8}.
CC -!- INTERACTION:
CC Q5T7P8-2; Q8WTP8-2: AEN; NbExp=3; IntAct=EBI-10246152, EBI-12119298;
CC Q5T7P8-2; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-10246152, EBI-10961624;
CC Q5T7P8-2; Q8N137: CNTROB; NbExp=3; IntAct=EBI-10246152, EBI-947360;
CC Q5T7P8-2; Q92997: DVL3; NbExp=6; IntAct=EBI-10246152, EBI-739789;
CC Q5T7P8-2; P51114-2: FXR1; NbExp=3; IntAct=EBI-10246152, EBI-11022345;
CC Q5T7P8-2; P51116: FXR2; NbExp=6; IntAct=EBI-10246152, EBI-740459;
CC Q5T7P8-2; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-10246152, EBI-2548508;
CC Q5T7P8-2; Q08379: GOLGA2; NbExp=6; IntAct=EBI-10246152, EBI-618309;
CC Q5T7P8-2; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-10246152, EBI-2549423;
CC Q5T7P8-2; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-10246152, EBI-10961706;
CC Q5T7P8-2; P42858: HTT; NbExp=3; IntAct=EBI-10246152, EBI-466029;
CC Q5T7P8-2; Q63ZY3: KANK2; NbExp=6; IntAct=EBI-10246152, EBI-2556193;
CC Q5T7P8-2; Q7L273: KCTD9; NbExp=6; IntAct=EBI-10246152, EBI-4397613;
CC Q5T7P8-2; Q5T7B8-2: KIF24; NbExp=3; IntAct=EBI-10246152, EBI-10213781;
CC Q5T7P8-2; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-10246152, EBI-14069005;
CC Q5T7P8-2; Q6A162: KRT40; NbExp=3; IntAct=EBI-10246152, EBI-10171697;
CC Q5T7P8-2; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-10246152, EBI-1216080;
CC Q5T7P8-2; Q9Y6D9: MAD1L1; NbExp=3; IntAct=EBI-10246152, EBI-742610;
CC Q5T7P8-2; P23508: MCC; NbExp=3; IntAct=EBI-10246152, EBI-307531;
CC Q5T7P8-2; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-10246152, EBI-742948;
CC Q5T7P8-2; Q15025: TNIP1; NbExp=3; IntAct=EBI-10246152, EBI-357849;
CC Q5T7P8-2; Q63HR2: TNS2; NbExp=3; IntAct=EBI-10246152, EBI-949753;
CC Q5T7P8-2; Q12933: TRAF2; NbExp=3; IntAct=EBI-10246152, EBI-355744;
CC Q5T7P8-2; P14373: TRIM27; NbExp=3; IntAct=EBI-10246152, EBI-719493;
CC Q5T7P8-2; Q13049: TRIM32; NbExp=6; IntAct=EBI-10246152, EBI-742790;
CC Q5T7P8-2; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-10246152, EBI-744794;
CC Q5T7P8-2; O43298: ZBTB43; NbExp=6; IntAct=EBI-10246152, EBI-740718;
CC Q5T7P8-2; Q96BR9: ZBTB8A; NbExp=3; IntAct=EBI-10246152, EBI-742740;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:Q9R0N8}; Single-pass membrane
CC protein {ECO:0000250|UniProtKB:Q9R0N8}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane
CC {ECO:0000250|UniProtKB:Q9R0N8}; Single-pass membrane protein
CC {ECO:0000250}. Note=Localized predominantly to endoplasmic reticulum
CC (ER) and/or Golgi-like perinuclear compartment (By similarity).
CC {ECO:0000250|UniProtKB:Q9R0N8}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9R0N8}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9R0N8}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9R0N8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5T7P8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T7P8-2; Sequence=VSP_036619;
CC -!- DOMAIN: The cysteine motif mediates homo- or heterodimer formation via
CC formation of disulfide bonds. {ECO:0000250|UniProtKB:O35681}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR EMBL; AK056448; BAG51713.1; -; mRNA.
DR EMBL; AL162594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56596.1; -; Genomic_DNA.
DR CCDS; CCDS871.1; -. [Q5T7P8-2]
DR RefSeq; NP_001257734.1; NM_001270805.1. [Q5T7P8-2]
DR RefSeq; NP_995320.1; NM_205848.3. [Q5T7P8-2]
DR AlphaFoldDB; Q5T7P8; -.
DR SMR; Q5T7P8; -.
DR BioGRID; 127139; 141.
DR IntAct; Q5T7P8; 34.
DR MINT; Q5T7P8; -.
DR STRING; 9606.ENSP00000477344; -.
DR iPTMnet; Q5T7P8; -.
DR PhosphoSitePlus; Q5T7P8; -.
DR BioMuta; SYT6; -.
DR DMDM; 209572719; -.
DR EPD; Q5T7P8; -.
DR jPOST; Q5T7P8; -.
DR MassIVE; Q5T7P8; -.
DR PaxDb; Q5T7P8; -.
DR PeptideAtlas; Q5T7P8; -.
DR PRIDE; Q5T7P8; -.
DR ProteomicsDB; 64676; -. [Q5T7P8-1]
DR ProteomicsDB; 64677; -. [Q5T7P8-2]
DR Antibodypedia; 53758; 332 antibodies from 28 providers.
DR DNASU; 148281; -.
DR Ensembl; ENST00000607941.5; ENSP00000476507.1; ENSG00000134207.17. [Q5T7P8-2]
DR Ensembl; ENST00000609117.5; ENSP00000477344.1; ENSG00000134207.17. [Q5T7P8-2]
DR Ensembl; ENST00000610222.3; ENSP00000476396.1; ENSG00000134207.17. [Q5T7P8-1]
DR GeneID; 148281; -.
DR KEGG; hsa:148281; -.
DR MANE-Select; ENST00000610222.3; ENSP00000476396.1; NM_001253772.2; NP_001240701.1.
DR UCSC; uc001eev.4; human. [Q5T7P8-1]
DR CTD; 148281; -.
DR DisGeNET; 148281; -.
DR GeneCards; SYT6; -.
DR HGNC; HGNC:18638; SYT6.
DR HPA; ENSG00000134207; Group enriched (brain, pancreas).
DR MIM; 607718; gene.
DR neXtProt; NX_Q5T7P8; -.
DR OpenTargets; ENSG00000134207; -.
DR PharmGKB; PA38614; -.
DR VEuPathDB; HostDB:ENSG00000134207; -.
DR eggNOG; KOG1028; Eukaryota.
DR GeneTree; ENSGT00940000157665; -.
DR HOGENOM; CLU_023008_8_3_1; -.
DR InParanoid; Q5T7P8; -.
DR OMA; VMRVGCN; -.
DR OrthoDB; 925064at2759; -.
DR PhylomeDB; Q5T7P8; -.
DR TreeFam; TF315600; -.
DR PathwayCommons; Q5T7P8; -.
DR SignaLink; Q5T7P8; -.
DR BioGRID-ORCS; 148281; 12 hits in 1066 CRISPR screens.
DR ChiTaRS; SYT6; human.
DR GenomeRNAi; 148281; -.
DR Pharos; Q5T7P8; Tbio.
DR PRO; PR:Q5T7P8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5T7P8; protein.
DR Bgee; ENSG00000134207; Expressed in cortical plate and 105 other tissues.
DR ExpressionAtlas; Q5T7P8; baseline and differential.
DR Genevisible; Q5T7P8; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; ISS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0030276; F:clathrin binding; IDA:BHF-UCL.
DR GO; GO:0001786; F:phosphatidylserine binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:BHF-UCL.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IDA:BHF-UCL.
DR GO; GO:0060478; P:acrosomal vesicle exocytosis; IMP:BHF-UCL.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IBA:GO_Central.
DR GO; GO:0071277; P:cellular response to calcium ion; IBA:GO_Central.
DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IBA:GO_Central.
DR GO; GO:0014059; P:regulation of dopamine secretion; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001565; Synaptotagmin.
DR InterPro; IPR028701; SYT6.
DR PANTHER; PTHR10024:SF45; PTHR10024:SF45; 1.
DR Pfam; PF00168; C2; 2.
DR PRINTS; PR00360; C2DOMAIN.
DR PRINTS; PR00399; SYNAPTOTAGMN.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Cytoplasm;
KW Cytoplasmic vesicle; Disulfide bond; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Synapse; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..510
FT /note="Synaptotagmin-6"
FT /id="PRO_0000183954"
FT TOPO_DOM 1..59
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..510
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 229..350
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 361..494
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 12..38
FT /note="Cysteine motif"
FT /evidence="ECO:0000250|UniProtKB:O35681"
FT REGION 157..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..510
FT /note="Necessary for cell membrane association (isoform 2)"
FT /evidence="ECO:0000250|UniProtKB:Q9R0N8"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 318
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 318
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 319
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 320
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 320
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 320
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 323
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 452
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 454
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1..85
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036619"
SQ SEQUENCE 510 AA; 57325 MW; DE5478F5B95693D3 CRC64;
MSGVWGAGGP RCQEALAVLA SLCRARPPPL GLDVETCRSF ELQPPERSPS AAGAGTSVSL
LAVVVIVCGV ALVAVFLFLF WKLCWMPWRN KEASSPSSAN PPLEALQSPS FRGNMADKLK
DPSTLGFLEA AVKISHTSPD IPAEVQMSVK EHIMRHTRLQ RQTTEPASST RHTSFKRHLP
RQMHVSSVDY GNELPPAAEQ PTSIGRIKPE LYKQKSVDGE DAKSEATKSC GKINFSLRYD
YETETLIVRI LKAFDLPAKD FCGSSDPYVK IYLLPDRKCK LQTRVHRKTL NPTFDENFHF
PVPYEELADR KLHLSVFDFD RFSRHDMIGE VILDNLFEAS DLSRETSIWK DIQYATSESV
DLGEIMFSLC YLPTAGRLTL TVIKCRNLKA MDITGYSDPY VKVSLLCDGR RLKKKKTTIK
KNTLNPVYNE AIIFDIPPEN MDQVSLLISV MDYDRVGHNE IIGVCRVGIT AEGLGRDHWN
EMLAYPRKPI AHWHSLVEVK KSFKEGNPRL
