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