SYT8_RAT
ID SYT8_RAT Reviewed; 395 AA.
AC Q925B4; Q62749; Q925B9;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Synaptotagmin-8;
DE AltName: Full=Synaptotagmin VIII;
DE Short=SytVIII;
GN Name=Syt8;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shin O.-H., Suedhof T.C.;
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 97-229.
RX PubMed=7791877; DOI=10.1038/375594a0;
RA Li C., Ullrich B., Zhang J.Z., Anderson R.G.W., Brose N., Suedhof T.C.;
RT "Ca(2+)-dependent and -independent activities of neural and non-neural
RT synaptotagmins.";
RL Nature 375:594-599(1995).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=9689015; DOI=10.1152/ajprenal.1998.275.1.f131;
RA Kishore B.K., Wade J.B., Schorr K., Inoue T., Mandon B., Knepper M.A.;
RT "Expression of synaptotagmin VIII in rat kidney.";
RL Am. J. Physiol. 275:F131-F142(1998).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11309201; DOI=10.1242/jcs.114.9.1709;
RA Gut A., Kiraly C.E., Fukuda M., Mikoshiba K., Wollheim C.B., Lang J.;
RT "Expression and localisation of synaptotagmin isoforms in endocrine beta-
RT cells: their function in insulin exocytosis.";
RL J. Cell Sci. 114:1709-1716(2001).
CC -!- FUNCTION: Involved in the trafficking and exocytosis of secretory
CC vesicles in non-neuronal tissues. Mediates Ca(2+)-regulation of
CC exocytosis acrosomal reaction in sperm. May mediate Ca(2+)-regulation
CC of exocytosis in insulin secreted cells (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:11309201}.
CC -!- SUBUNIT: Homodimer or homooligomer. Homodimerization and
CC homooligomerization do not depend on Ca(2+). Interacts with SYNCRIP
CC isoform 2 C-terminus. Binds inositol 1,3,4,5-tetrakisphosphate (IP4).
CC Binds to AP2 in a Ca(2+)-independent manner. Interacts with STX1A,
CC STX1B and STX2; the interaction is Ca(2+)-dependent (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type III
CC membrane protein {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Strongly expressed in heart, kidney,
CC cerebral cortex, pancreas, and many insulin-secreting cells; lower
CC expression in spleen. Broadly distributed in kidney.
CC {ECO:0000269|PubMed:11309201, ECO:0000269|PubMed:9689015}.
CC -!- DOMAIN: The first C2 domain/C2A does not mediate Ca(2+)-dependent
CC phospholipid binding. {ECO:0000250}.
CC -!- DOMAIN: The second C2 domain/C2B is responsible for SYNCRIP and
CC inositol 1,3,4,5-tetrakisphosphate (IP4)-binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA87728.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF375462; AAK56957.1; -; mRNA.
DR EMBL; AF375467; AAK56962.1; -; mRNA.
DR EMBL; U20110; AAA87728.1; ALT_INIT; Genomic_DNA.
DR PIR; S58403; S58403.
DR RefSeq; NP_445777.1; NM_053325.1.
DR AlphaFoldDB; Q925B4; -.
DR SMR; Q925B4; -.
DR STRING; 10116.ENSRNOP00000027454; -.
DR PaxDb; Q925B4; -.
DR PRIDE; Q925B4; -.
DR GeneID; 60566; -.
DR KEGG; rno:60566; -.
DR UCSC; RGD:68399; rat.
DR CTD; 90019; -.
DR RGD; 68399; Syt8.
DR eggNOG; KOG1028; Eukaryota.
DR InParanoid; Q925B4; -.
DR OrthoDB; 925064at2759; -.
DR PhylomeDB; Q925B4; -.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q925B4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0031045; C:dense core granule; IBA:GO_Central.
DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
DR GO; GO:0030276; F:clathrin binding; IDA:BHF-UCL.
DR GO; GO:0001786; F:phosphatidylserine binding; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0007340; P:acrosome reaction; ISO:RGD.
DR GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IBA:GO_Central.
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:0048488; P:synaptic vesicle endocytosis; 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; IPR030540; SYT8.
DR PANTHER; PTHR10024:SF249; PTHR10024:SF249; 1.
DR Pfam; PF00168; C2; 2.
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 Cell membrane; Cytoplasmic vesicle; Membrane; Reference proteome; Repeat;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..395
FT /note="Synaptotagmin-8"
FT /id="PRO_0000183961"
FT TOPO_DOM 1..44
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 113..229
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 241..370
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT CONFLICT 102
FT /note="E -> D (in Ref. 2; AAA87728)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="Q -> R (in Ref. 2; AAA87728)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="M -> V (in Ref. 1; AAK56957)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 43980 MW; B75334EF829E2676 CRC64;
MQADRSMKMG HVSNPLSTSA PVDATAGPNL IPDLITKIPW PRWILFIAIL AAGVLLVSCL
LCVICYCCHR QRHRKQPKDK ETVGLGSARN STTTHLVQPD VECLEPCSGG DQPWGQLLLS
LEYDFGSQEI RVGLRQAKNL KAEGTADPYA RVSVSTQAGR RHETKVHRGT LCPMFEETCC
FLVPPAELPK ATLKVQLLDF KRFSEHEPLG ELQLPLGTVD LQHVLESWYQ LGPPGSTESE
QMGELCFSLR YVPSSGRLTV VILEARGLNP GLAEAYVKVQ LILNQRKWKK NKTSSKKGTT
NPYFNEAFVF LVPVSQLQSM DLVLAVWARG LQLLAEPVGK VLLGPRASGQ PLQHWADMLA
HARRPIAQWH HLRSPREVDR ALALQPRLPL LRPRS
