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SYTL5_RAT
ID   SYTL5_RAT               Reviewed;         753 AA.
AC   Q812E4;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Synaptotagmin-like protein 5;
GN   Name=Sytl5; Synonyms=Slp5;
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].
RC   STRAIN=Sprague-Dawley; TISSUE=Testis;
RX   PubMed=12590134; DOI=10.1074/jbc.m213090200;
RA   Fukuda M.;
RT   "Slp4-a/granuphilin-a inhibits dense-core vesicle exocytosis through
RT   interaction with the GDP-bound form of Rab27A in PC12 cells.";
RL   J. Biol. Chem. 278:15390-15396(2003).
CC   -!- FUNCTION: May act as Rab effector protein and play a role in vesicle
CC       trafficking. Binds phospholipids (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds RAB27A that has been activated by GTP-binding.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
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DR   EMBL; AB098162; BAC57423.1; -; mRNA.
DR   RefSeq; NP_848016.1; NM_178333.1.
DR   AlphaFoldDB; Q812E4; -.
DR   SMR; Q812E4; -.
DR   STRING; 10116.ENSRNOP00000004785; -.
DR   iPTMnet; Q812E4; -.
DR   PhosphoSitePlus; Q812E4; -.
DR   PaxDb; Q812E4; -.
DR   PRIDE; Q812E4; -.
DR   GeneID; 302538; -.
DR   KEGG; rno:302538; -.
DR   UCSC; RGD:631342; rat.
DR   CTD; 94122; -.
DR   RGD; 631342; Sytl5.
DR   eggNOG; KOG1028; Eukaryota.
DR   InParanoid; Q812E4; -.
DR   PhylomeDB; Q812E4; -.
DR   PRO; PR:Q812E4; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042043; F:neurexin family protein binding; IBA:GO_Central.
DR   GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0006887; P:exocytosis; ISO:RGD.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   CDD; cd04029; C2A_SLP-4_5; 1.
DR   CDD; cd04020; C2B_SLP_1-2-3-4; 1.
DR   CDD; cd15766; FYVE_Slp5; 1.
DR   Gene3D; 2.60.40.150; -; 2.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR041282; FYVE_2.
DR   InterPro; IPR010911; Rab_BD.
DR   InterPro; IPR037303; SLP-4/5_C2A.
DR   InterPro; IPR028702; Slp5.
DR   InterPro; IPR043567; SYTL1-5_C2B.
DR   InterPro; IPR042783; SYTL5_FYVE.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45716:SF6; PTHR45716:SF6; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF02318; FYVE_2; 1.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; SSF49562; 2.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS50916; RABBD; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..753
FT                   /note="Synaptotagmin-like protein 5"
FT                   /id="PRO_0000190221"
FT   DOMAIN          7..123
FT                   /note="RabBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT   DOMAIN          429..550
FT                   /note="C2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          590..717
FT                   /note="C2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   ZN_FING         64..106
FT                   /note="FYVE-type"
FT   REGION          145..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..241
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..283
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        324..342
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         147
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80T23"
SQ   SEQUENCE   753 AA;  83645 MW;  1D118D31B176A92D CRC64;
     MSKNSEFINL SFLLDHEKEM ILGVLKRDEY LKKVEDKRIR KLKNELLEAK RRSGKTHQEA
     NRVCVHCQKS LGLIFDRGAP CQACSLRVCS ECRVTGLDGS WKCTVCAKVA QLRIISGEWF
     LEEKAKRFKQ VNVLGTDVVR QSILRRSPGS EEIQNQEQAH QGADKSDTLS SVRQKATHDG
     PKRKGFLLSK FRSATRGEIK TPKAESGRSY SLDLDNQNLQ SFKSVSGSDR GSTTSSDLTD
     QEAGRGAPKG SCSNGGIPVT QRSPAPSARS VTSISSREHG FENSMALATI ESISEELTKS
     HRRNTSGTPS IAVSGTSLSS ERSRSELDLS ESFAEDLEDT SSIRSRSVPG ALDKDLNSLE
     DTEDGVDLVS SRFSANTHSL ASGLSTSSQA GSDRKRSYLH VPDADSDTTS LNSMMSVYSE
     TGDYGNVKVT GEILLHISYC YKTGGLYIFV KNCRNLAIGD EKKQRTDAYV KSYLLPDKTR
     NNKRKTKIRT GTNPEFNETL KYTISHTQLE TRTLQLSVWH YDRFGRNSFL GEVEIAFDSW
     NFENPCDEWF VLQPKVELAP DISLQYKGEL TIVLRYIPPE ENLIFPVEQP QGKKIFKKGK
     KKESPAISGG ILEVFIKEAK NLTAVKAGGT SDSFVKGYLL PDDNKATKHK TAVVKKSVNP
     QWNHVFIFSG LYPQDIQNAC LELTIWDKEA FSSNIFLGGV RLNSGSGISH GKAVDWMDSR
     GEEQRLWQKM ADNPGTSVEG VLMLRSSMAK CRL
 
 
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