VPS10_YEAS6
ID VPS10_YEAS6 Reviewed; 1577 AA.
AC B5VDW2;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=Vacuolar protein sorting/targeting protein PEP1;
DE AltName: Full=Carboxypeptidase Y receptor;
DE Short=CPY receptor;
DE AltName: Full=Carboxypeptidase Y-deficient protein 1;
DE AltName: Full=Sortilin VPS10;
DE AltName: Full=Vacuolar carboxypeptidase sorting receptor VPS10;
DE AltName: Full=Vacuolar protein sorting-associated protein 10;
DE AltName: Full=Vacuolar protein-targeting protein 1;
DE Flags: Precursor;
GN Name=PEP1; Synonyms=VPS10, VPT1; ORFNames=AWRI1631_20820;
OS Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=545124;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI1631;
RX PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL FEMS Yeast Res. 8:1185-1195(2008).
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. Binds the Golgi-modified P2 form
CC of CPY, and this interaction is dependent on the presence of an intact
CC CPY vacuolar protein sorting signal (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; ABSV01000082; EDZ73884.1; -; Genomic_DNA.
DR AlphaFoldDB; B5VDW2; -.
DR SMR; B5VDW2; -.
DR Proteomes; UP000008988; 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; -; 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 Repeat; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1577
FT /note="Vacuolar protein sorting/targeting protein PEP1"
FT /id="PRO_0000407545"
FT TOPO_DOM 22..1391
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1392..1412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1413..1577
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 58..68
FT /note="BNR 1"
FT REPEAT 101..111
FT /note="BNR 2"
FT REPEAT 179..187
FT /note="BNR 3"
FT REPEAT 414..423
FT /note="BNR 4"
FT REPEAT 485..495
FT /note="BNR 5"
FT REPEAT 531..541
FT /note="BNR 6"
FT REPEAT 762..771
FT /note="BNR 7"
FT REPEAT 859..869
FT /note="BNR 8"
FT REPEAT 1141..1150
FT /note="BNR 9"
FT REPEAT 1183..1192
FT /note="BNR 10"
FT REGION 1531..1577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 791
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1008
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1577 AA; 177554 MW; 8E9210A024ABEB87 CRC64;
MILLHFVYSL WALLLIPLIN AEEFTPKVTK TIAQDSFEIL SFDDSNTLIR KQDASVTISF
DDGETWEKVE GIEDEITWIY IDPFNRHDRA VATSMYESRL YITNDQGKSW ERITLPDSEK
NISSRGCYIE THPLNKNYFL AKCNYCEKTE VDNEENSGDE EGAPVIFNIT HCTDKVFASN
DGGKSFSEIK SSLERNENSA ISISDCGFAK TGKDSDLESS DTSIICLFQN MQLIMDEFSS
PYTESKLVLT TDWGKSLKEF DQFKDKVVNG YRILKSHMVV ITQGDRYNDM SSMDVWVSND
LSNFKMAYMP TQLRHSMQGE IYEDAMGRII LPMSRERSDQ EEDKGIVSEI LISDSQGLKF
SPIPWTANEV FGYINLYQPT YLKGTMIASL YPLSRRRNRK GKAKGVKNKG VTKISVDNGL
TWTVLKVVDP DNADSFDCDI TDFENCSLQN MFYTREGSTP TAGILMTTGI VGDGSVFDWG
DQRTFISRDG GLTWKLAFDF PCLYAVGDYG NVIVAIPYNA DEDDDPQSEF YYSLDQGKTW
TEYQLETTIY PNEVMNTTPD GSGAKFILNG FTLAHMDGTT NFIYAIDFST AFNDKTCEEN
DFEDWNLAEG KCVNGVKYKI RRRKQDAQCL VKKVFEDLQL FETACDKCTE ADYECAFEFV
RDATGKCVPD YNLIVLSDVC DKTKKKTVPV KPLQLVKGDK CKKPMTVKSV DISCEGVPKK
GTNDKEIVVT ENKFDFKIQF YQYFDTVTDE SLLMINSRGE AYISHDGGQT IRRFDSNGET
IIEVVFNPYY NSSAYLFGSK GSIFSTHDRG YSFMTAKLPE ARQLGMPLDF NAKAQDTFIY
YGGKNCESIL SPECHAVAYL TNDGGETFTE MLDNAIHCEF AGSLFKYPSN EDMVMCQVKE
KSSQTRSLVS STDFFQDDKN TVFENIIGYL STGGYIIVAV PHENNELRAY VTIDGTEFAE
AKFPYDEDVG KQEAFTILES EKGSIFLHLA TNLVPGRDFG NLLKSNSNGT SFVTLEHAVN
RNTFGYVDFE KIQGLEGIIL TNIVSNSDKV AENKEDKQLK TKITFNEGSD WNFLKPPKRD
SEGKKFSCSS KSLDECSLHL HGYTERKDIR DTYSSGSALG MMFGVGNVGP NLLPYKECST
FFTTDGGETW AEVKKTPHQW EYGDHGGILV LVPENSETDS ISYSTDFGKT WKDYKFCADK
VLVKDITTVP RDSALRFLLF GEAADIGGSS FRTYTIDFRN IFERQCDFDI TGKESADYKY
SPLSSKSNCL FGHQTEFLRK TDENCFIGNI PLSEFSRNIK NCSCTRQDFE CDYNFYKAND
GTCKLVKGLS PANAADVCKK EPDLIEYFES SGYRKIPLST CEGGLKLDAP SSPHACPGKE
KEFKEKYSVS AGPFAFIFIS ILLIIFFAAW FVYDRGIRRN GGFARFGEIR LGDDGLIENN
NTDRVVNNIV KSGFYVFSNI GSLLQHTKTN IAHVISKIRG RFGNRTGPSY SSLIHDQFLD
EADDLLAGHD EDANDLSSFM DQGSNFEIEE DDVPTLEEEH TSYTDQPTTT DVPDALPEGN
EENIDRPDST APSNENQ
