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SYT14_MOUSE
ID   SYT14_MOUSE             Reviewed;         555 AA.
AC   Q7TN84;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Synaptotagmin-14;
DE   AltName: Full=Synaptotagmin XIV;
DE            Short=SytXIV;
GN   Name=Syt14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ;
RX   PubMed=12801916; DOI=10.1093/jb/mvg082;
RA   Fukuda M.;
RT   "Molecular cloning, expression, and characterization of a novel class of
RT   synaptotagmin (Syt XIV) conserved from Drosophila to humans.";
RL   J. Biochem. 133:641-649(2003).
RN   [2]
RP   TISSUE SPECIFICITY.
RX   PubMed=21835308; DOI=10.1016/j.ajhg.2011.07.012;
RA   Doi H., Yoshida K., Yasuda T., Fukuda M., Fukuda Y., Morita H., Ikeda S.,
RA   Kato R., Tsurusaki Y., Miyake N., Saitsu H., Sakai H., Miyatake S.,
RA   Shiina M., Nukina N., Koyano S., Tsuji S., Kuroiwa Y., Matsumoto N.;
RT   "Exome sequencing reveals a homozygous SYT14 mutation in adult-onset,
RT   autosomal-recessive spinocerebellar ataxia with psychomotor retardation.";
RL   Am. J. Hum. Genet. 89:320-327(2011).
CC   -!- FUNCTION: May be involved in the trafficking and exocytosis of
CC       secretory vesicles in non-neuronal tissues. Is Ca(2+)-independent.
CC   -!- SUBUNIT: Homodimer. Can also form heterodimers (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type III
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in heart and testis. Expressed in brain
CC       (especially in the cerebellum). {ECO:0000269|PubMed:12801916,
CC       ECO:0000269|PubMed:21835308}.
CC   -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR   EMBL; AB102947; BAC76808.1; -; mRNA.
DR   CCDS; CCDS48489.1; -.
DR   RefSeq; NP_853524.1; NM_181546.3.
DR   AlphaFoldDB; Q7TN84; -.
DR   SMR; Q7TN84; -.
DR   STRING; 10090.ENSMUSP00000016344; -.
DR   iPTMnet; Q7TN84; -.
DR   PhosphoSitePlus; Q7TN84; -.
DR   PaxDb; Q7TN84; -.
DR   PRIDE; Q7TN84; -.
DR   ProteomicsDB; 254791; -.
DR   Antibodypedia; 51697; 32 antibodies from 15 providers.
DR   DNASU; 329324; -.
DR   Ensembl; ENSMUST00000195354; ENSMUSP00000142190; ENSMUSG00000016200.
DR   GeneID; 329324; -.
DR   KEGG; mmu:329324; -.
DR   UCSC; uc007edu.2; mouse.
DR   CTD; 255928; -.
DR   MGI; MGI:2444490; Syt14.
DR   VEuPathDB; HostDB:ENSMUSG00000016200; -.
DR   eggNOG; KOG1028; Eukaryota.
DR   GeneTree; ENSGT00940000159420; -.
DR   InParanoid; Q7TN84; -.
DR   PhylomeDB; Q7TN84; -.
DR   TreeFam; TF351132; -.
DR   BioGRID-ORCS; 329324; 1 hit in 75 CRISPR screens.
DR   PRO; PR:Q7TN84; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q7TN84; protein.
DR   Bgee; ENSMUSG00000016200; Expressed in otolith organ and 151 other tissues.
DR   ExpressionAtlas; Q7TN84; baseline and differential.
DR   Genevisible; Q7TN84; MM.
DR   GO; GO:0016021; C:integral component of membrane; ISS:MGI.
DR   GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR   GO; GO:0005543; F:phospholipid binding; IDA:MGI.
DR   Gene3D; 2.60.40.150; -; 2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR028696; SYT14.
DR   InterPro; IPR043541; SYT14/14L/16.
DR   PANTHER; PTHR46129; PTHR46129; 1.
DR   PANTHER; PTHR46129:SF3; PTHR46129:SF3; 1.
DR   Pfam; PF00168; C2; 2.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; SSF49562; 2.
DR   PROSITE; PS50004; C2; 2.
PE   2: Evidence at transcript level;
KW   Membrane; Reference proteome; Repeat; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..555
FT                   /note="Synaptotagmin-14"
FT                   /id="PRO_0000183979"
FT   TOPO_DOM        1..24
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..47
FT                   /note="Helical; Signal-anchor for type III membrane
FT                   protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..555
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          260..379
FT                   /note="C2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          415..550
FT                   /note="C2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          76..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          205..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..250
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   555 AA;  62044 MW;  7728CA866BFBA84E CRC64;
     MAIEGGERTC GVHELICIRK VSPEAVGFLS AVGVFIVLML LLFLYINKKF CFENVGGFPD
     LGSGYNTRTN SQDKMYNSYM DRDEPGSSSE SEDEALGKYH EALSRTHNSR WPLVDSRQKS
     YAWETRQKYS PLSAEYDGYS TEASMEDGNC IQRMRRTPPL DELQPPPYQD DSGSPHLSCT
     PSEIGDAKCE ISHCSNSPRC SFNKCPSEGS TGHEAESYHN KGYEDDVPSD STAVLSPEDM
     SAQGSSSQLP KPFDPEPEAK YGTLDVTFDY DSERQKLLVT VTAVTDIPTY NRTGGNSWQV
     HLVLLPIKKQ RAKTSIQRGP CPVFTETFKF NHVESEMIGN YAVRFRLYGV HRMKKEKIVG
     EKIFYLTKLN LQGKMSLPVI LEPSYNPSGC DSQVSLSEAS CGDSTSSCQS LQHGSVPEIL
     IGLLYNATTG RLSAEVIKGS HFKNLAANRP PNTYVKLTLL NSMGQEMSKC KTSTRRGQPN
     PVYKETFVFQ VALFQLSDVT LILSVYNRRS MKRKEMIGWI SLGLNSSGEE ELRHWTAMKE
     SKGQQVCRWH ALLES
 
 
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