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VPS10_VANPO
ID   VPS10_VANPO             Reviewed;        1601 AA.
AC   A7TT43;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 65.
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=Kpol_361p4;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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}; Single-pass type I membrane protein {ECO:0000250}.
CC       Prevacuolar compartment membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}. Note=Cycles between the Golgi apparatus
CC       and the prevacuolar compartment. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the VPS10-related sortilin family.
CC       {ECO:0000305}.
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DR   EMBL; DS480541; EDO14567.1; -; Genomic_DNA.
DR   RefSeq; XP_001642425.1; XM_001642375.1.
DR   AlphaFoldDB; A7TT43; -.
DR   SMR; A7TT43; -.
DR   STRING; 436907.A7TT43; -.
DR   PRIDE; A7TT43; -.
DR   EnsemblFungi; EDO14567; EDO14567; Kpol_361p4.
DR   GeneID; 5542578; -.
DR   KEGG; vpo:Kpol_361p4; -.
DR   eggNOG; KOG3511; Eukaryota.
DR   HOGENOM; CLU_000700_0_0_1; -.
DR   InParanoid; A7TT43; -.
DR   OMA; IFMHVTT; -.
DR   OrthoDB; 1046610at2759; -.
DR   PhylomeDB; A7TT43; -.
DR   Proteomes; UP000000267; 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; -; 2.
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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..1601
FT                   /note="Vacuolar protein sorting/targeting protein 10"
FT                   /id="PRO_0000407541"
FT   TOPO_DOM        21..1430
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1431..1451
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1452..1601
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          58..67
FT                   /note="BNR 1"
FT   REPEAT          100..110
FT                   /note="BNR 2"
FT   REPEAT          439..448
FT                   /note="BNR 3"
FT   REPEAT          510..520
FT                   /note="BNR 4"
FT   REPEAT          556..566
FT                   /note="BNR 5"
FT   REPEAT          796..806
FT                   /note="BNR 6"
FT   REPEAT          838..849
FT                   /note="BNR 7"
FT   REPEAT          893..903
FT                   /note="BNR 8"
FT   REPEAT          1178..1188
FT                   /note="BNR 9"
FT   REPEAT          1220..1228
FT                   /note="BNR 10"
FT   REGION          349..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1558..1601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..369
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1571..1591
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        457
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        505
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1044
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1289
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1339
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1601 AA;  180588 MW;  BB67E9D9DC56C85F CRC64;
     MLLSQWLLTT CILISSYVHA ADQFKPKVVR TESTGWFNIY PFDDSKVILK NEDTFLSISD
     NNGETWRPIE GINDVRWSWI DKLYPKTRAF ANSKVGNKIY MTDDQGKTWT TVKINEKEYS
     NGSKSELSCN LISHPTKPEI LLAECYVCDY DEEQSNGSIT KRAVSSLFDN FLNSIMRDPT
     CRNEVFISTN SGKDFTKLNI DLKEREESNL LYSTLNCQFA IASKQSKNTE TDSTIYCTRK
     HFYGQKFNDK NEADKTYLVS SFVKTSNWGK TFEELPELKG YLVNYFEAFD SQLLVITQDD
     AYNRHSTQKV WISKDFKTFK EAHMPTQLRF MINGLISEDS VGRLTMPILR TNPDKKDSSD
     KNEDNKKMHH TDSVVSDILI SDSRGTKFTF IEWMNSNDVT YRQISSFKYL KGTLFGHTQE
     YPNLGNKGPS FEMILRSKVS VDNGNTWSNL KIVDPENKSK YSCNIDIPES CSLNIMSMFG
     TPDFITPGIM MVNGAVSDGH HASWNETKTF ISRDGGVSWK LAFEFQTATA FGDHGNVIVA
     VPYDPESDDD PQSEFYYSLD QGTTWTEYQL EKTILPMQLI STTPDGSGLT FILNGLSMDS
     TGGSRWRWND KKETNFVYSI DFSDAFEEKA CVDSDLEKWY VAGGNCINGA KYRFDRRRAD
     SKCLMRKIYD DLAYTEEICE KCSDDDYECS YEFVKDSSGK CVADFELLSL SGSCAKAKNG
     KISLKPKQRI VNTLCKVDMK IEDVLVPCTE VDSPENPDNI ITVSENKFDS ALLTYKYFDT
     ASDESLLMMT LDNEVYVSHD GGKNIKKVNT NREKIVEIVF NPFYSKDAYL FGRDGGLYIT
     HDRGQTFTKS QLPETRQLGL KLEFHATKQN TFIYYGGKDC DSMFSEKCHA VAYITTDGGE
     TFSEMLNNGI HCKFSGSTFK DPYNEDQIIC QILDSSNGKK KLVSSTNFFK SDSQTETLFE
     EVIGFMSTGE FLVVALPHGD DELRAYATLD GKEFAEANLP KDLSDIKQES FTILGSESGS
     IFMHLATSQN IQGEFGRLLK SNSNGTSFVS LESAVNRNSA GFVDFEKIQG LEGIVLINVV
     ENTDEVERGT TKTKKLKSKI TFNDGSDWSF INPPLKDSNG KKYTCSGKGL KKCSLHLHGY
     TERNDIRDTF SSGSAFGMLI AVGNVGEHLL PKDECSTFMT IDGGATWTEV RKGPFQWEYG
     DHGGILVLIP DGSESDTLLY STDFGKTWID YKFAGEKIQM RDIVTVPRDS AMRFLIIGQS
     NSIRGGTTTV FSVDFSKIFS RQCVYDLDNA SNDDFEFVSF NPVKNQCLFG HQAEYLRKIH
     TDCFIGSAPL EESFRIVKNC SCTRNDFECD YNYYKANDGT CKLVEGLTPS DPKDICKKNP
     DAYEYFKPTG YRKIPLSTCV DGLNLEGTSS PLPCPGKVEE FRKNHKINGR SFSLLFILPF
     LILLGIAWFI YDRGIRRNGG FSRFGEIRLG DEVIEENNVD KAVNNIVRTG LLLTSSVFSG
     LQLVKRFIGK SFQSLRERVT GRRGPSYTTL FNDQFLEGAD DLLEGHDEDA NDLTSFLSND
     NNFDIDTEDD GNTFAPFREE ASEEDHGPVT GDSSNNEEVS S
 
 
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