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SPE39_BOVIN
ID   SPE39_BOVIN             Reviewed;         481 AA.
AC   A5D796;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Spermatogenesis-defective protein 39 homolog;
DE            Short=SPE-39;
DE   AltName: Full=VPS33B-interacting protein in apical-basolateral polarity regulator;
DE   AltName: Full=VPS33B-interacting protein in polarity and apical restriction;
GN   Name=VIPAS39; Synonyms=SPE39, VIPAR;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Proposed to be involved in endosomal maturation implicating
CC       in part VPS33B. In epithelial cells, the VPS33B:VIPAS39 complex may
CC       play a role in the apical RAB11A-dependent recycling pathway and in the
CC       maintenance of the apical-basolateral polarity. May play a role in
CC       lysosomal trafficking, probably via association with the core HOPS
CC       complex in a discrete population of endosomes; the functions seems to
CC       be independent of VPS33B. May play a role in vesicular trafficking
CC       during spermatogenesis. May be involved in direct or indirect
CC       transcriptional regulation of E-cadherin (By similarity).
CC       {ECO:0000250|UniProtKB:Q23288, ECO:0000250|UniProtKB:Q9H9C1}.
CC   -!- SUBUNIT: Interacts with VPS33B. Associates with the homotypic fusion
CC       and vacuole protein sorting (HOPS) complex; impaired by VPS33B.
CC       Interacts with RAB11A (By similarity). {ECO:0000250|UniProtKB:Q8BGQ1,
CC       ECO:0000250|UniProtKB:Q9H9C1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle
CC       {ECO:0000250}. Early endosome {ECO:0000250|UniProtKB:Q9H9C1}. Recycling
CC       endosome {ECO:0000250|UniProtKB:Q9H9C1}. Late endosome
CC       {ECO:0000250|UniProtKB:Q9H9C1}. Note=Colocalizes in clusters with
CC       VPS33B at cytoplasmic organelles. {ECO:0000250|UniProtKB:Q9H9C1}.
CC   -!- SIMILARITY: Belongs to the VIPAS39 family. {ECO:0000305}.
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DR   EMBL; BC140476; AAI40477.1; -; mRNA.
DR   RefSeq; NP_001091469.1; NM_001098000.1.
DR   AlphaFoldDB; A5D796; -.
DR   SMR; A5D796; -.
DR   STRING; 9913.ENSBTAP00000027283; -.
DR   PaxDb; A5D796; -.
DR   PRIDE; A5D796; -.
DR   Ensembl; ENSBTAT00000027283; ENSBTAP00000027283; ENSBTAG00000020475.
DR   GeneID; 508872; -.
DR   KEGG; bta:508872; -.
DR   CTD; 63894; -.
DR   VEuPathDB; HostDB:ENSBTAG00000020475; -.
DR   VGNC; VGNC:36798; VIPAS39.
DR   eggNOG; KOG4677; Eukaryota.
DR   GeneTree; ENSGT00390000013955; -.
DR   HOGENOM; CLU_029487_0_0_1; -.
DR   InParanoid; A5D796; -.
DR   OMA; QIQSTLY; -.
DR   OrthoDB; 812306at2759; -.
DR   TreeFam; TF319640; -.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000020475; Expressed in trachea and 108 other tissues.
DR   ExpressionAtlas; A5D796; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR   GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR   GO; GO:0099023; C:vesicle tethering complex; IEA:Ensembl.
DR   GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR   GO; GO:0032963; P:collagen metabolic process; IEA:Ensembl.
DR   GO; GO:0008333; P:endosome to lysosome transport; ISS:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR   GO; GO:0017185; P:peptidyl-lysine hydroxylation; IEA:Ensembl.
DR   GO; GO:0043687; P:post-translational protein modification; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0007034; P:vacuolar transport; IBA:GO_Central.
DR   Gene3D; 1.10.150.780; -; 1.
DR   InterPro; IPR040057; Spe-39.
DR   InterPro; IPR006925; Vps16_C.
DR   InterPro; IPR038132; Vps16_C_sf.
DR   PANTHER; PTHR13364; PTHR13364; 1.
DR   Pfam; PF04840; Vps16_C; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoplasmic vesicle; Differentiation; Endosome; Phosphoprotein;
KW   Protein transport; Reference proteome; Spermatogenesis; Transcription;
KW   Transcription regulation; Transport.
FT   CHAIN           1..481
FT                   /note="Spermatogenesis-defective protein 39 homolog"
FT                   /id="PRO_0000395738"
FT   REGION          122..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         21
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9C1"
FT   MOD_RES         116
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BGQ1"
FT   MOD_RES         120
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9C1"
FT   MOD_RES         123
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9C1"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9C1"
FT   MOD_RES         131
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H9C1"
SQ   SEQUENCE   481 AA;  55615 MW;  D523D3499A26D6A1 CRC64;
     MNRTKGDEEE YWNSSKFKAF TFDDEDDELS QLKESKRAVN SLRDFVDDDD EDDLERVSWT
     GEPVGSISWS IKETAGNSGS SHEREQLKNR NSFSTYAQLP KPASTYSLSS FFRGRTRPGS
     FQSLSDALSD TPAKSYAPEL GRPKGEYRDY SNDWSPSDTV RRLRKGKDKI QLLEEAVSMH
     DGNVITAVLI FLKRTLSKEI LFRELEVRQV ALRHLIHFLK EIGDQKLLLD LFRFLDRTEE
     LALSHYREHL NIQDPEKRKE FLKTCIGLPF SAEDSAHIQD HYTLLERQII IEANDRHLEL
     AGQTEVFRKH PRKASILNMP LVTTLFYSCF YHYTEAEGTF SSPVNLKKTF KIPDKQYVLT
     ALAARAKLRA WHDVDALFTT KNWLGYTKKR APIGFHRVVE ILHKNSAPVQ VLQEYVNLVE
     DVDTKLNLAT KFKCHDVVID TCRDLKDRQQ LLAYRSKVDK GSAEEEKIDA LLNSSQIRWK
     N
 
 
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