VPS10_CANGA
ID VPS10_CANGA Reviewed; 1514 AA.
AC Q6FPF1;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
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; OrderedLocusNames=CAGL0J04312g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380956; CAG60842.1; -; Genomic_DNA.
DR RefSeq; XP_447893.1; XM_447893.1.
DR AlphaFoldDB; Q6FPF1; -.
DR SMR; Q6FPF1; -.
DR STRING; 5478.XP_447893.1; -.
DR EnsemblFungi; CAG60842; CAG60842; CAGL0J04312g.
DR GeneID; 2889655; -.
DR KEGG; cgr:CAGL0J04312g; -.
DR CGD; CAL0133276; CAGL0J04312g.
DR VEuPathDB; FungiDB:CAGL0J04312g; -.
DR eggNOG; KOG3511; Eukaryota.
DR HOGENOM; CLU_000700_0_0_1; -.
DR InParanoid; Q6FPF1; -.
DR OMA; IFMHVTT; -.
DR Proteomes; UP000002428; Chromosome J.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1514
FT /note="Vacuolar protein sorting/targeting protein 10"
FT /id="PRO_0000407511"
FT TOPO_DOM 20..1351
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1352..1372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1373..1514
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 55..64
FT /note="BNR 1"
FT REPEAT 151..160
FT /note="BNR 2"
FT REPEAT 359..368
FT /note="BNR 3"
FT REPEAT 423..433
FT /note="BNR 4"
FT REPEAT 469..479
FT /note="BNR 5"
FT REPEAT 717..727
FT /note="BNR 6"
FT REPEAT 814..824
FT /note="BNR 7"
FT REPEAT 1099..1109
FT /note="BNR 8"
FT REPEAT 1141..1150
FT /note="BNR 9"
FT REGION 651..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1480..1514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1490..1514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 746
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 966
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1514 AA; 170452 MW; 8A684BBF502DC919 CRC64;
MRLPSIFLVF FYLFARTLCW SPEVSLLHGV DSLASIIPFD DSSTILSVGR KGVNVSHDYG
RTWETKLRNK GEYPVSVTLN TFRPNSRAFV FLNGKLYGTH NEGSDWFESK FPSDRQLTKA
LTIDFSPFAK DVIIASFVAK DNQNDEKEFN YVSTDDGKSF RVLDVGQEYE SMRCRFLSIS
HESNFPHNDN IICMTKTSSP DQNKLLLSEN RGKSFKELSI GEDIAFDNFY LTNSYLVIRS
IRDIHNKAAE VDLYVSSDAK DFKKAYLPTT LRRSDIRRII ELLGRKMFIT LTRSSESNVQ
DDNGNTLFTD GLVSNSDGLK FTSFSTSASK SRTTITPVEF LNGTFIQKQV GRNSGGYSIS
IDNGNTWRKL KYSDKGNKNP IKCQDENDCN LELLIPQIFH GPTAGILVML GHINDNFSDQ
QTFISRDGGL NWEMGLEFPG IYATGDLGNV IVACPVDPSS DNDPQSEIYY SLDQGMTWSE
YQLDEMFIPI DVINITPDGS GLSFILTGFS LDKPDDQRPN IDNRVTYLID FNNVHDGKKC
KAKDYEKFEL AEGSCINGAK YTFNRRKQSA KCIGGEVFKD LLFDMEVCTE CQEQDYECSS
EFIKDSKGVC VVDEKWLSAT GNCPSTDIKK PAMRLIADNM CKKELPIQSK SVSCKNKNPS
DPKDIPKKPK EGDRPTFGTG DIQATFNTFK GKVRFYQYFD TDEDESLILA TSEGEAYISH
DSGQTYTHFN YNKPKVHEIV FNEYFNSSAY IFDIDGNLHV THDRGYTFDT IRLPASLQLG
LPLNFHSKDP NTFIYYGGKN CKSIFDTNCH IVAFITRDGG KSFSELLPNA IHCEFVGSSL
KLSDSDDLLF CQVKDETSSK TRQRSLVSTT DYFETEPKVV FQKILGYMTN GEYVIIAVPG
ENHEITAYVT MDGDEFAETL LPYDLDIEQP EAFTVLGSST GSVFLHFTSF QENSVAFGSL
LKSNTNGTSY VKLQSNVNRN EAGYVDFEKV QGLDGIILTN VVTNADEIKD GSSQKHLRTK
ITFNDGVDWE YIKPPKKDSS GDSYHCKSNK LEHCSLNLHS YTERKDFRDT FSSGSALGMM
IGVGNVGDKL LPFEECSTFL TIDGGKSWTE IKKGAYQWEF GDHGGILILS RDGEMTNSIS
YSTDFGKSWY DYQFSDEKVL VSDIVTVPQD SALRFLLITA DRIGRGFESG TVTVDFSGLF
KRQCVLDFNN ENHDDFDYFS IGNSENECIF GHKVKYLRKN SEECYVGAVS LSQFTRVMKN
CTCTRADFEC DYNFVRQYDG TCKLVDGLQP GNEAAICKKD PDLVEYFQST GYRKIPLSTC
QGGLKLDGRT EPLPCPGKEK EFKQKYGISG SSFFLLFFVP FLFFVSAGWF VYDRGIRRNG
GFARFGEIRL GDDQLIEENT TDKVVNTIIR FGVASFEVMA GGFGIIRRIA NNSFNRITGR
MNGRYRPSYS NLMHDDFLDE ADDLLAGHDD DANDLASFMD DDSNFDIEDE TTSVNDSGYR
DQSPETENVV DSNN
