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VPS10_PHANO
ID   VPS10_PHANO             Reviewed;        1421 AA.
AC   Q0TVB2;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Vacuolar protein sorting/targeting protein 10;
DE   AltName: Full=Carboxypeptidase Y receptor;
DE            Short=CPY receptor;
DE   AltName: Full=Sortilin VPS10;
DE   AltName: Full=Vacuolar carboxypeptidase sorting receptor VPS10;
DE   Flags: Precursor;
GN   Name=VPS10; ORFNames=SNOG_16552;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
CC   -!- FUNCTION: Functions as a sorting receptor in the Golgi compartment
CC       required for the intracellular sorting and delivery of soluble vacuolar
CC       proteins, like carboxypeptidase Y (CPY) and proteinase A. Executes
CC       multiple rounds of sorting by cycling between the late Golgi and a
CC       prevacuolar endosome-like compartment (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Prevacuolar
CC       compartment membrane {ECO:0000250}; Multi-pass membrane protein
CC       {ECO:0000250}. Note=Cycles between the Golgi apparatus and the
CC       prevacuolar compartment. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the VPS10-related sortilin family.
CC       {ECO:0000305}.
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DR   EMBL; CH445374; EAT76092.2; -; Genomic_DNA.
DR   RefSeq; XP_001806659.1; XM_001806607.1.
DR   AlphaFoldDB; Q0TVB2; -.
DR   SMR; Q0TVB2; -.
DR   STRING; 13684.SNOT_16552; -.
DR   EnsemblFungi; SNOT_16552; SNOT_16552; SNOG_16552.
DR   GeneID; 5983591; -.
DR   KEGG; pno:SNOG_16552; -.
DR   eggNOG; KOG3511; Eukaryota.
DR   HOGENOM; CLU_000700_0_0_1; -.
DR   InParanoid; Q0TVB2; -.
DR   OrthoDB; 1046610at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0006895; P:Golgi to endosome transport; IBA:GO_Central.
DR   GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central.
DR   GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR036278; Sialidase_sf.
DR   InterPro; IPR031777; Sortilin_C.
DR   InterPro; IPR031778; Sortilin_N.
DR   InterPro; IPR006581; VPS10.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   Pfam; PF15902; Sortilin-Vps10; 2.
DR   Pfam; PF15901; Sortilin_C; 3.
DR   SMART; SM00602; VPS10; 2.
DR   SUPFAM; SSF50939; SSF50939; 2.
PE   3: Inferred from homology;
KW   Glycoprotein; Golgi apparatus; Membrane; Protein transport; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..1421
FT                   /note="Vacuolar protein sorting/targeting protein 10"
FT                   /id="PRO_0000407531"
FT   TOPO_DOM        22..1296
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1297..1317
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1318..1349
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1350..1370
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1371..1421
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REPEAT          100..110
FT                   /note="BNR 1"
FT   REPEAT          367..376
FT                   /note="BNR 2"
FT   REPEAT          415..425
FT                   /note="BNR 3"
FT   REPEAT          671..682
FT                   /note="BNR 4"
FT   REPEAT          1049..1059
FT                   /note="BNR 5"
FT   REGION          596..625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..622
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        288
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        922
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1421 AA;  160204 MW;  59CBF8AE5654D936 CRC64;
     MKYLKGLLLP ALLALAPSAT AAKDAPSIET TTFSNELVNL QYFDDSTVAL VQELGSGKIY
     RSPDAGKAWK ELKDLKKGLG IIKNPYDNKV ALVLGEEQHW ITYDQGETWQ DFKTEYSPSP
     NGPVSWHSQD NKKILIHEIE DCLFTPCLGL TYYTTDGFKT KPKTLVEGRR MCQWAKGSER
     FLEGQEKHDD RILCILRGKY SDRSKDFRLM ISDDYFKTAE EPVMSSGRTV QGMANMAAVK
     GYLVAAVKAD HSSELSLYVT QDTENWHHAQ FGNGKIEEDA YTILESTNYS IQVDVMSSKY
     VSIGSLYTSN SDGLYFTKNV DNTNRNPDGF VDFEKIANIQ GVVLVNIVDN AKAVQERGAH
     KKLKSRISFD DGRTFEELKV KGSDKELHLH SSPGIVMGVG NTGDELGKYT DGDLYVSDDA
     GLTWELALDE AHKYEFGDQG SVLVAVFDEG DTDKVMYSLK HGRKDTWKSI DLGYKIRARE
     LTTLSDSTSL RFLLYGSKKK DGGGREHVLI QLDFNDLHER KCEDKDFDPK WSDPTPTFES
     CECDEFRDFE CDFGFKPEGE GKDKKCVPEK LTLPKDACKN GDSTYMGSSG WRKISGNQCK
     GGSKKDEKTE RKCDEADLPP PKSDKITSEI TRFKGSNFLE QYYLERSTQN DDDETDHDET
     VVMLTDERTA WITHDHGKQW KKAVDDEVVR IYPHQYDNNY VYFLTASKKV HYSEDRGLRN
     SIHSFEAPVM PNQEMLQILQ FHPKQKGWLI WMGGKNCEKV NSKECHTAAY VSQKNGKDES
     WEPLVSYVKK CAFVWREAGR DVKEERVFCE QHANEETGAP LQLISSDDWF KKQDVKFKSV
     VEIALMSEFI IVATKEKDDT LRLDASLDAN TFAEARFPPK FFDIHQTAYT VLDSSTHAIF
     LHVTVNPRVD QEYGSIIKSN SNGTSYVLSL NAVNRNTEGY VDFEKMQGLE GVAIANVVVN
     VNEVNDGAKK KKQTRITHND GADWREKDAE GKAYECAGKG EEKCALHVHG YTERADPREM
     YSSPTAVGLM LAVGNVGEEL GTFGEADTYM TTDAGLTWKE IKKGSYAWEF GDQGSVIVIV
     RRGEDTDHVY YTLDSGEKWN LYQFSERKIR VDAITTVPSD TSLNFLLWGK DGKELVAVNL
     DFSGLPQFQR KCDLDEKDPE KGDFDLWIPQ HPLQPDDKQC LFGHVAEYHR KKRDAECRNG
     QRIDHMHNIQ RNCTCTRRDY ECAYNYERQP GGECKLIEGL DLEDPTAVCS KGAKEFWDVS
     PYRKIPLSTC EGGNEFDHMG DVHPCPGFEE EFEKKHGISG FGLFMAIVLP FAAAGGIGYY
     VWRNWDGKFG RIRLGENGGA FDSDSRWVQW PIAAISGLVA VVAAIPMLVG SLYRMVTGRM
     GGGYGGRTYT SRSSFARGRG DYAVVDPDEG ELLGDDSDEE V
 
 
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