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VPS10_PYRTR
ID   VPS10_PYRTR             Reviewed;        1491 AA.
AC   B2WDP9;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 54.
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=PTRG_08108;
OS   Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS   (Drechslera tritici-repentis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=426418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP;
RX   PubMed=23316438; DOI=10.1534/g3.112.004044;
RA   Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA   Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA   Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA   Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA   Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT   "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT   repentis, reveals transduplication and the impact of repeat elements on
RT   pathogenicity and population divergence.";
RL   G3 (Bethesda) 3:41-63(2013).
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; DS231622; EDU51027.1; -; Genomic_DNA.
DR   RefSeq; XP_001938440.1; XM_001938405.1.
DR   AlphaFoldDB; B2WDP9; -.
DR   SMR; B2WDP9; -.
DR   STRING; 45151.EDU51027; -.
DR   PRIDE; B2WDP9; -.
DR   EnsemblFungi; EDU51027; EDU51027; PTRG_08108.
DR   GeneID; 6346387; -.
DR   eggNOG; KOG3511; Eukaryota.
DR   HOGENOM; CLU_000700_0_0_1; -.
DR   InParanoid; B2WDP9; -.
DR   OMA; ATMSEFI; -.
DR   OrthoDB; 1046610at2759; -.
DR   Proteomes; UP000001471; Unassembled WGS sequence.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
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; 2.
DR   SMART; SM00602; VPS10; 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..1491
FT                   /note="Vacuolar protein sorting/targeting protein 10"
FT                   /id="PRO_0000407533"
FT   TOPO_DOM        22..1354
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1355..1375
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1376..1405
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1406..1426
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1427..1491
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REPEAT          97..107
FT                   /note="BNR 1"
FT   REPEAT          364..374
FT                   /note="BNR 2"
FT   REPEAT          426..436
FT                   /note="BNR 3"
FT   REPEAT          719..730
FT                   /note="BNR 4"
FT   REPEAT          1102..1112
FT                   /note="BNR 5"
FT   REPEAT          1143..1153
FT                   /note="BNR 6"
FT   REGION          640..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1018..1047
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1464..1491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        644..667
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1477..1491
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        309
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        970
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1491 AA;  167576 MW;  9A6051365327E7C7 CRC64;
     MKHLKGLLLP ALLALASSAA AKDPLVETTP FKNELVNLMY FDDSGVALVQ ELDNGKIFRS
     HDAGKGWKEI KDVQGLGIIK SPYDNKVALI LGEKKHWITY DQGENWDSFE TKLPPSPQGP
     VGWHAQDNKK ILLNEIENCF TAPCLGKTYY TTDGFKTDPK TLVDDRRMCQ WAKASERFLQ
     GVDKHDDRIL CITRGKYSDR SKDFRLLMSD NFFKETEEPV MSSGRTVQGM ANMAAVKGYI
     VAAAKAEHSS ELALYVTQDT DSWHHARFGD HKIEEDAYTI LESTNYSIQV DVMTSKYVTM
     GNLYTSNSNG TYFTKNVEHT NRNDAGYVDF EKIANIQGVV LVNTVDNYKE VEKSGQSKKL
     KSRISFDDGR SFEKLTVKGK DGELHLHSVT NLHNSGRVFS SPAPGIVMGV GNTGDYLGKY
     TDGDLYVSDD AGLTWELALE EAHKYEFGDQ GSVLVAVFDE GDTDEIRYSF KHGRKDTWQK
     IKLDYKIRAR ELTTLPDSTS LKFMIYGSRK KDGGGREHVI VHLDFSDMLK KCGDSDFDDE
     WSVRKDADGD PSCVMGHKQL FRRRKWDAEC SVGELFKDPV PKFKPCDCDK FRDYECDFNF
     TPTGEGKDKK CEPSESFSLP KGACEGDAKS YKGSSGWRKI PGNQCKGETE RDKQVERECK
     DAERPRPKTD KITSEITKFK GSNFMEQYYL ERNTQSDGTD NDRGKDETVV MLTDERTAYI
     THDHGKKWKK AVDDEIVRIY PHQYENNNVY FLTASKKVYY SKDRGLHDSI NSFEAPVMPN
     TEMLPIMQFH PKQKDWIIWL GGKNCEKLGN KDCHTVAYVS QKNGEDSSWE SLVPYVKKCA
     FVWREAGRSV KEEQVFCEQH TNEEKNAPLE LISSDDWFKK KDVKFKSVVE FATMSEFIIV
     ATKAEDNTLH LDASLDAHTF AEAKFPPKFF DIHQTAYTVL DSSTHAVFLH VTVNPQRDQE
     YGSIIKSNSN GTSYVMSLAA VNRNTEGYVD FEKMQGLEGV AVANVIVNVD EVNKGAKKKK
     QSRITHNDGA DWEPLQAPEK DSDDKPYDCD IADKKKCGLH IHGYTERADP REMYSSPTAV
     GLMLAVGNVG PELTTFGEAN TFMTTDAGIT WKEVKKGTYA WEFGDQGSVI VIVRRGEDTD
     HVYYSVDSGA KWDLYQFADH KMRVDAITTV PSDTSLNFLL WGKDSRELFA VNLDFSGLPE
     FQKECKLDEN DPTKGDYDLW SPQHPLQQDE PECLFGHVAQ YHRKKRDVKC RNGQRIDQMH
     DIARNCSCTR RDFECAYNYE RDSSGDCVLV PGLSLPDPAK VCSNKNVKEY YSNTRFRKIP
     LSTCQGGTEY DKTGDVHPCP GFEEDFKKNH GVGGFTLFLA IVLPFAAAAG VGYWVWRNWD
     GKFGRIRLGE PGGGSAFDSD APWVRWPIAA VSGLVAVGAA LPLVVGSVWR WVVGRMGGRG
     GGGGGYSGLG GSGFGRAYTS RSSFARGRGE YSVVDPDEGE LLGDEESDED V
 
 
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