VPS10_ASPOR
ID VPS10_ASPOR Reviewed; 1488 AA.
AC Q2TVY7;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 81.
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 protein sorting-associated protein 10;
DE Flags: Precursor;
GN Name=vps10; ORFNames=AO090010000769;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20622126; DOI=10.1128/aem.03087-09;
RA Yoon J., Aishan T., Maruyama J., Kitamoto K.;
RT "Enhanced production and secretion of heterologous proteins by the
RT filamentous fungus Aspergillus oryzae via disruption of vacuolar protein
RT sorting receptor gene Aovps10.";
RL Appl. Environ. Microbiol. 76:5718-5727(2010).
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. {ECO:0000269|PubMed:20622126}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Prevacuolar
CC compartment membrane {ECO:0000269|PubMed:20622126}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:20622126}. Note=Cycles between the Golgi
CC apparatus and the prevacuolar compartment. {ECO:0000250}.
CC -!- DOMAIN: The lumenal domain contains two regions of approximately 650 AA
CC that exhibit 20% identity. The cytoplasmic domain may serve as a Golgi
CC retention/recycling signal.
CC -!- MISCELLANEOUS: Present with 7210 molecules/cell in log phase SD medium.
CC -!- SIMILARITY: Belongs to the VPS10-related sortilin family.
CC {ECO:0000305}.
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DR EMBL; AP007175; BAE66586.1; -; Genomic_DNA.
DR RefSeq; XP_001827719.1; XM_001827667.1.
DR AlphaFoldDB; Q2TVY7; -.
DR SMR; Q2TVY7; -.
DR STRING; 510516.Q2TVY7; -.
DR PRIDE; Q2TVY7; -.
DR EnsemblFungi; BAE66586; BAE66586; AO090010000769.
DR GeneID; 5999853; -.
DR KEGG; aor:AO090010000769; -.
DR VEuPathDB; FungiDB:AO090010000769; -.
DR HOGENOM; CLU_000700_0_0_1; -.
DR OMA; ATMSEFI; -.
DR Proteomes; UP000006564; Chromosome 8.
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:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:UniProtKB.
DR GO; GO:0007034; P:vacuolar transport; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 3.
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; 2.
DR SMART; SM00602; VPS10; 2.
DR SUPFAM; SSF50939; SSF50939; 1.
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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1488
FT /note="Vacuolar protein sorting/targeting protein 10"
FT /id="PRO_0000407507"
FT TOPO_DOM 24..1351
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1352..1372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1373..1405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1406..1426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1427..1488
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REPEAT 63..72
FT /note="BNR 1"
FT REPEAT 380..389
FT /note="BNR 2"
FT REPEAT 440..450
FT /note="BNR 3"
FT REPEAT 482..490
FT /note="BNR 4"
FT REPEAT 720..730
FT /note="BNR 5"
FT REPEAT 1102..1112
FT /note="BNR 6"
FT REPEAT 1144..1153
FT /note="BNR 7"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 845
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 967
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1488 AA; 165742 MW; FE39AF373CE0865B CRC64;
MIYRWLLLVS CLLLALLAQR GAAKSSSPKI APPTKIDHKP SSLFYFEDTD TVLMNTVNGD
LLRSVDAGET WSVVEGDDGG MKHHVLLIRQ HPYDNKKAYA LGPNGRHWVT TDQAKTWASF
NIAEFPAIRH YPLVFHGGDS SKVIFQGEEC AGRYCIVRSY YTTDDFATVK LLRESTGGCA
WAVGHPQFAE DLNLAEEIKD RSFCVVPGLK VPLPHANRLV YSDDYFKGNA EGTETKLQEG
RPVSGVISTA AVKKFIVAAA KSKGTEELAL YVTVDAKNWH RAEFDGHRIE EDAYTMLEST
NYSLQVDVLT SPRSGMGVLF TSNSNGTYFT RNIEHTNRNS EGMVDFEKIA GIQGIVLVNT
VQNPEEVESG SAKKKITSRI SFDDGRTFQP LKSDGENLHL HSVTALRNIG RVFSSPAPGL
VMGIGNTGNH LQEYAECNLY ISDDAGVTWR RAIKHPHKYE FGDQGAVVIA VRDEGRVDKI
NYSLDHGKEW ASVELQHKIY PTMVTTTPDS TSLKFIVVGS LKESQDGEHV IYSIDFDGLH
ERKCEEDDFE KWPARLDEHG KPDCLMGHKQ FYMRRRANAN CFVDEEFKDP QPIFEACKCT
AEDFECEYRR TEDGKGCVIP SPLTPPEGEC KKPDDKFMGP SGWRLIPGDA CIRDGGENLD
KEIERSCKDA SSPSTDGKIR VTLQLLEARD YAQYYYLERQ SSSSGSDETI IMLSSEHEVY
VTHDHGKTWE RPLKGEEITR VYLHPYSSDV AFLLTDGKEG FWTEDRGHTF KPFQAPAPPT
QDRFLQVMAF HPVHKDRLIW TGAVDCHSGD CHSDAFIKKG RGKNWEPLLS YVQKCEFESR
ETRPNSTNLV YCEQFEKQSK NGRLQLLSSD DFFNDNEVQF VDVINYATMS EFIIVASRQP
ENPDSLVAST SVDGRTFARA QFPPNVQVPV QTAYTVLESS THAVFLHVTA SSTEGGEYGP
IIKSNSNGTS YVLSISAVNR NSLGYVDFEK AQGLEGVAVV NVVSNVADVS KKVPKKLKTM
ITHNDGAQWM LLPPPTKDAD GKSFGCSVVA GKGTDDCSLH LHGYTERKDE RDTFASGSAI
GLMMAVGNVG DHLAGGDEAD TFITNDGGIS WKSVKKGKYM WEYGDSGSVI VIVPESKPTK
TIHYSLDEGD TWEEFQFSDV EVRINDISTV PSDTSKNFLL WARLSNSEVQ DKFATFNIDF
SGVRPRPCLL DENQGNSDDY YIWEPKHPFQ ENNCLFGHSE QYHRKKPSAQ CWNDWRESHV
HSIGTNCTCT RADYECDYNY EPQSDGSCAL VPGLPKPDAM EICKKDPDTI EYWEPTGYRR
IPQTTCQGGL NLDHFVSKPC PNKEEEYKQK HGISGVGLFF AIVTPLAVAG AAGYYAYSKW
DGKFGQIRLG ESAGTSQSFL SRDSWLVTVP IAIVAGTVAV ARALPLLVTS LWRGASGFIR
LGRGRGYSRP YASRGSFAAR RGDYTSIVDD EDELLGVEDA ELDEDDEA
