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EXOC5_RAT
ID   EXOC5_RAT               Reviewed;         708 AA.
AC   P97878; A1A5N5;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Exocyst complex component 5;
DE   AltName: Full=71 kDa component of rsec6/8 secretory complex;
DE   AltName: Full=Exocyst complex component Sec10;
DE   AltName: Full=p71;
GN   Name=Exoc5; Synonyms=Sec10l1;
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], PARTIAL PROTEIN SEQUENCE, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=9073068; DOI=10.1016/s0378-1119(96)00720-2;
RA   Hazuka C.D., Hsu S.C., Scheller R.H.;
RT   "Characterization of a cDNA encoding a subunit of the rat brain rsec6/8
RT   complex.";
RL   Gene 187:67-73(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION IN EXOCYST COMPLEX.
RC   TISSUE=Brain;
RX   PubMed=9405631; DOI=10.1073/pnas.94.26.14438;
RA   Kee Y., Yoo J.-S., Hazuka C.D., Peterson K.E., Hsu S.-C., Scheller R.H.;
RT   "Subunit structure of the mammalian exocyst complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:14438-14443(1997).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-395; THR-405 AND SER-412, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA   Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT   "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT   regulation of aquaporin-2 phosphorylation at two sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
CC   -!- FUNCTION: Component of the exocyst complex involved in the docking of
CC       exocytic vesicles with fusion sites on the plasma membrane.
CC   -!- SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3, EXOC4,
CC       EXOC5, EXOC6, EXOC7 and EXOC8 (PubMed:9405631). Interacts with EXOC3L1
CC       (By similarity). {ECO:0000250|UniProtKB:Q3TPX4,
CC       ECO:0000269|PubMed:9405631}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O00471}. Midbody
CC       {ECO:0000250|UniProtKB:O00471}. Note=Localization at the midbody
CC       requires the presence of RALA, EXOC2 and EXOC3.
CC       {ECO:0000250|UniProtKB:O00471}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9073068}.
CC   -!- SIMILARITY: Belongs to the SEC10 family. {ECO:0000305}.
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DR   EMBL; U79417; AAC53096.1; -; mRNA.
DR   EMBL; BC128739; AAI28740.1; -; mRNA.
DR   PIR; JC6329; JC6329.
DR   RefSeq; NP_071540.1; NM_022204.3.
DR   AlphaFoldDB; P97878; -.
DR   SMR; P97878; -.
DR   CORUM; P97878; -.
DR   STRING; 10116.ENSRNOP00000062799; -.
DR   iPTMnet; P97878; -.
DR   PhosphoSitePlus; P97878; -.
DR   jPOST; P97878; -.
DR   PaxDb; P97878; -.
DR   PRIDE; P97878; -.
DR   Ensembl; ENSRNOT00000067735; ENSRNOP00000062799; ENSRNOG00000013804.
DR   GeneID; 60627; -.
DR   KEGG; rno:60627; -.
DR   UCSC; RGD:708408; rat.
DR   CTD; 10640; -.
DR   RGD; 708408; Exoc5.
DR   eggNOG; KOG3745; Eukaryota.
DR   GeneTree; ENSGT00390000012837; -.
DR   HOGENOM; CLU_020771_1_0_1; -.
DR   InParanoid; P97878; -.
DR   OMA; PLCKHHY; -.
DR   OrthoDB; 225235at2759; -.
DR   Reactome; R-RNO-264876; Insulin processing.
DR   Reactome; R-RNO-5620916; VxPx cargo-targeting to cilium.
DR   PRO; PR:P97878; -.
DR   Proteomes; UP000002494; Chromosome 15.
DR   Bgee; ENSRNOG00000013804; Expressed in ileum and 20 other tissues.
DR   Genevisible; P97878; RN.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR   GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR   GO; GO:1904019; P:epithelial cell apoptotic process; ISO:RGD.
DR   GO; GO:0001736; P:establishment of planar polarity; ISO:RGD.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0006893; P:Golgi to plasma membrane transport; IBA:GO_Central.
DR   GO; GO:1905515; P:non-motile cilium assembly; ISO:RGD.
DR   GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR033960; EXOC5/Sec10.
DR   InterPro; IPR009976; Sec10-like.
DR   PANTHER; PTHR12100; PTHR12100; 1.
DR   PANTHER; PTHR12100:SF4; PTHR12100:SF4; 1.
DR   Pfam; PF07393; Sec10; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Cytoplasm; Direct protein sequencing; Exocytosis;
KW   Phosphoprotein; Protein transport; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O00471"
FT   CHAIN           2..708
FT                   /note="Exocyst complex component 5"
FT                   /id="PRO_0000118945"
FT   COILED          40..101
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O00471"
FT   MOD_RES         122
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O00471"
FT   MOD_RES         395
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:16641100"
FT   MOD_RES         405
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:16641100"
FT   MOD_RES         412
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16641100"
SQ   SEQUENCE   708 AA;  81737 MW;  567BEE0E5E43EF59 CRC64;
     MATTAELFEE PFVADEYIER LVWRTPGGGS RGGPEAFDPK RLLEEFVNHI QELQIMDERI
     QRKVEKLEQQ CQKEAKEFAK KVQELQKSNQ VAFQHFQELD EHISYVATKV CHLGDQLEGV
     NTPRQRAVEA QKLMKYFNEF LDGELKSDVF TNPEKIKEAA DVIQKLHLIA QELPFDRFSE
     VKSKIASKYH DLECQLIQEF TSAQRRGEVS RMREVAAVLL HFKGYSHCID VYIKQCQEGA
     YLRNDIFEDA AILCQRVNKQ VGDIFSNPEA VLAKLIQNVF EVKLQSFVKD QLEECRKSDA
     EQYLKSLYDL YTRTTSLSSK LMEFNLGTDK QTFLSKLIKS IFVSYLENYI EVEIGYLKSR
     SAMILQRYYD SKNHQKRSIG TGGIQDLKER IRQRTNLPLG PSIDTHGETF LSQEVVVNLL
     QETKQAFERC HRLSDPSDLP RNAFRIFTIL VEFLCIEHID YALETGLAGI PSSDSRNANL
     YFLDVVQQAN TIFHLFDKQF NDHLMPLISS SPKLSECLQK KKEIIEQMEM KLDTGIDRTL
     NCMIGQMKHI LAAEQKKTDF KPEDENNVLI QYTNACVKVC AYVRKQVEKI KNSMDGKNVD
     TVLMELGVRF HRLTYEHLQQ YSYSCMGGML AICDVAEYRK CAKDFKIPMV LHLFDTLHAL
     CNLLVVAPDN LKQVCSGEQL ANLDKNILHS FVQLRADYRS ARLARHFS
 
 
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