SYT1_ANSCY
ID SYT1_ANSCY Reviewed; 421 AA.
AC A0A075F932;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Synaptotagmin-1 {ECO:0000312|EMBL:AIE76331.1};
DE AltName: Full=Synaptotagmin I {ECO:0000250|UniProtKB:P21579};
DE Short=SytI {ECO:0000250|UniProtKB:P21579};
GN Name=SYT1 {ECO:0000312|EMBL:AIE76331.1};
OS Anser cygnoid (Swan goose).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anserinae; Anser.
OX NCBI_TaxID=8845 {ECO:0000312|EMBL:AIE76331.1};
RN [1] {ECO:0000312|EMBL:AIE76331.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND PHYLOGENETIC
RP ANALYSIS.
RX PubMed=25146222; DOI=10.1186/1477-7827-12-83;
RA Luan X., Luo L., Cao Z., Li R., Liu D., Gao M., Liu M., Wang L.;
RT "Molecular cloning and expression analysis of the Synaptotagmin-1 gene in
RT the hypothalamus and pituitary of Huoyan goose during different stages of
RT the egg-laying cycle.";
RL Reprod. Biol. Endocrinol. 12:83-83(2014).
RN [2]
RP DEVELOPMENTAL STAGE.
RX PubMed=25049869; DOI=10.5713/ajas.2013.13083;
RA Luan X., Cao Z., Xu W., Gao M., Wang L., Zhang S.;
RT "Gene expression profiling in the pituitary gland of laying period and
RT ceased period huoyan geese.";
RL Asian-Australas. J. Anim. Sci. 26:921-929(2013).
CC -!- FUNCTION: Calcium sensor that participates in triggering
CC neurotransmitter release at the synapse (By similarity). May have a
CC regulatory role in the membrane interactions during trafficking of
CC synaptic vesicles at the active zone of the synapse. It binds acidic
CC phospholipids with a specificity that requires the presence of both an
CC acidic head group and a diacyl backbone. May play a role in dendrite
CC formation by melanocytes (By similarity). May play a role in regulating
CC the secretion of hormones relevant to the reproduction and egg-laying
CC of female geese (PubMed:25146222). {ECO:0000250|UniProtKB:P21579,
CC ECO:0000250|UniProtKB:P46096, ECO:0000269|PubMed:25146222}.
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:P21707};
CC -!- SUBUNIT: Homotetramer (Probable). {ECO:0000250|UniProtKB:P21707}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000250|UniProtKB:P21707}; Single-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC membrane {ECO:0000250|UniProtKB:P21707}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P21707}. Cytoplasmic vesicle, secretory vesicle,
CC chromaffin granule membrane {ECO:0000250|UniProtKB:P21707}; Single-pass
CC membrane protein {ECO:0000250|UniProtKB:P21707}. Cytoplasm
CC {ECO:0000250|UniProtKB:P21707}. Note=Synaptic vesicles and chromaffin
CC granules. {ECO:0000250|UniProtKB:P21707}.
CC -!- DEVELOPMENTAL STAGE: Expressed during egg-laying cycle in the
CC hypothalamus and pituitary. Expression increases from the pre-laying
CC period to the peak laying period reaching its highest level in the peak
CC laying period and then decreases in the ceased period
CC (PubMed:25146222). Expression is up-regulated in the pituitary gland
CC during egg-laying period and down-regulated during ceased period
CC (PubMed:25049869). {ECO:0000269|PubMed:25049869,
CC ECO:0000269|PubMed:25146222}.
CC -!- DOMAIN: The first C2 domain mediates Ca(2+)-dependent phospholipid
CC binding. {ECO:0000250|UniProtKB:P21707}.
CC -!- DOMAIN: The second C2 domain mediates interaction with SV2A and
CC probably with STN2. {ECO:0000250|UniProtKB:P21707}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR EMBL; KJ734994; AIE76331.1; -; mRNA.
DR AlphaFoldDB; A0A075F932; -.
DR SMR; A0A075F932; -.
DR Proteomes; UP000694521; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0048609; P:multicellular organismal reproductive process; IEP:UniProtKB.
DR GO; GO:0007269; P:neurotransmitter secretion; IEA:InterPro.
DR GO; GO:1903861; P:positive regulation of dendrite extension; ISS:UniProtKB.
DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; ISS:UniProtKB.
DR GO; GO:0046883; P:regulation of hormone secretion; IEP:UniProtKB.
DR GO; GO:1903305; P:regulation of regulated secretory pathway; ISS:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; ISS:UniProtKB.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001565; Synaptotagmin.
DR InterPro; IPR015428; Synaptotagmin1.
DR PANTHER; PTHR10024:SF239; PTHR10024:SF239; 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 2: Evidence at transcript level;
KW Calcium; Cytoplasm; Cytoplasmic vesicle; Differentiation; Glycoprotein;
KW Lipoprotein; Membrane; Metal-binding; Palmitate; Reference proteome;
KW Repeat; Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..421
FT /note="Synaptotagmin-1"
FT /id="PRO_0000434728"
FT TOPO_DOM 1..60
FT /note="Vesicular"
FT /evidence="ECO:0000305"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 141..260
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 272..405
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..381
FT /note="Phospholipid binding"
FT /evidence="ECO:0000250|UniProtKB:P21707"
FT COMPBIAS 98..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 363
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 363
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 365
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 365
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 371
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT LIPID 77
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21707"
FT LIPID 78
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21707"
FT LIPID 80
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21707"
FT LIPID 82
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21707"
FT LIPID 85
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21707"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 421 AA; 47208 MW; E6249E77D9495DCA CRC64;
MVSESHHEAL AAPPATTVAA APPSNVTEPA SPGGGGGKED AFSKLKEKFM NELNKIPLPP
WALIAIAIVA VLLILTCCFC LCKKCLFKKK NKKKGKEKGG KNAINMKDVK DLGKTMKDQD
DDAETGLTDG EEKEEPKEVE KLGKIQYSLD YDFQNNQLLV GIIQAAELPA LDMGGTSDPY
VKVFLLPDKK KKYETKVHRK TLNPVFNEQF TFKVPYSELG GKTLVMAVYD FDRFSKHDII
GEYKVAMNTV DFGHVTEEWR DLQSAEKEEQ EKLGDICFSL RYVPTAGKLT VVILEAKNLK
KMDVGGLSDP YVKIHLMQNG KRLKKKKTTI KKNTLNPYYN ESFSFEVPFE QIQKVQIVVT
VLDYDKIGKN DAIGKVFVGY NSTGAELRHW SDMLANPRRP IAQWHTLQPE EEVDAMLAVK
K
