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Database: UniProt
Entry: VPS10_KOMPG
LinkDB: VPS10_KOMPG
Original site: VPS10_KOMPG 
ID   VPS10_KOMPG             Reviewed;        1542 AA.
AC   C4R192;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, 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; OrderedLocusNames=PAS_chr2-1_0625;
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864;
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(2009).
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; FN392320; CAY69266.1; -; Genomic_DNA.
DR   RefSeq; XP_002491546.1; XM_002491501.1.
DR   AlphaFoldDB; C4R192; -.
DR   SMR; C4R192; -.
DR   STRING; 644223.C4R192; -.
DR   GlyCosmos; C4R192; 6 sites, No reported glycans.
DR   EnsemblFungi; CAY69266; CAY69266; PAS_chr2-1_0625.
DR   GeneID; 8198939; -.
DR   KEGG; ppa:PAS_chr2-1_0625; -.
DR   eggNOG; KOG3511; Eukaryota.
DR   HOGENOM; CLU_000700_0_0_1; -.
DR   InParanoid; C4R192; -.
DR   OMA; WIANQID; -.
DR   OrthoDB; 5840at2759; -.
DR   Proteomes; UP000000314; Chromosome 2.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007034; P:vacuolar transport; IEA:UniProt.
DR   Gene3D; 2.10.70.80; -; 2.
DR   Gene3D; 3.30.60.270; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
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   PANTHER; PTHR12106; SORTILIN RELATED; 1.
DR   PANTHER; PTHR12106:SF27; VPS10 HOMOLOG 1-RELATED; 1.
DR   Pfam; PF15902; Sortilin-Vps10; 2.
DR   Pfam; PF15901; Sortilin_C; 2.
DR   SMART; SM00602; VPS10; 2.
DR   SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 1.
DR   SUPFAM; SSF50939; Sialidases; 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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..1542
FT                   /note="Vacuolar protein sorting/targeting protein 10"
FT                   /id="PRO_0000407532"
FT   TOPO_DOM        21..1387
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1388..1408
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1409..1445
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1446..1466
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1467..1542
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REPEAT          56..65
FT                   /note="BNR 1"
FT   REPEAT          102..112
FT                   /note="BNR 2"
FT   REPEAT          373..383
FT                   /note="BNR 3"
FT   REPEAT          439..449
FT                   /note="BNR 4"
FT   REPEAT          484..494
FT                   /note="BNR 5"
FT   REPEAT          732..742
FT                   /note="BNR 6"
FT   REPEAT          1128..1138
FT                   /note="BNR 7"
FT   REPEAT          1170..1178
FT                   /note="BNR 8"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        454
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        633
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        714
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        922
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        989
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1542 AA;  173835 MW;  EFA9944A7A879667 CRC64;
     MWIERNLIAS ILLFSTSAYA AFKPRIVKKE FDDLLNPIYF NDSSTVLGLV DQTLLISNDD
     GKSWTNLQEV ITPGEIDPLT IVNIEFNPSA SKAFVFTASK HYLTLDKGST WKEFQIPLEK
     YGNRIAYDVE FNFVNEEHAI IRTRSCKRRF DCKDEYFYSL DDLQSVDKIT ISDEIVNCQF
     SQSSTSSDSR KNDAITCVTR KLDSNRHFLE SNVLTTLNFF KDVTSLPASD PLTKMLIKDI
     RVVQNYIVLF VSSDRYNKYS PTLLFISKDG NTFKEASLPD SEGTSPSVHF LKSPNPNLIR
     AIRLGKKNSL DGGGFYSEVL QSDSTGLHFH VLLDHLEANL LSYYQIENLA NLEGIWIANQ
     IDTSSKFGSK SVITFDAGLT WSPVTVDEDE DKSLHIIAFA GENSLYESKF PVSTPGIALR
     IGLIGDSSDA LDIGSYRTFL TRDAGLTWSQ VFDNVSVCGF GNYGNIILCC SYDPLLRSEP
     LKFRYSLDQG LNWESIDLGF NGVAVGVLNN IDNSSPQFLV MTIATDGKSS KAQHFLYSVD
     FSDAYEKKIC DVTKDELFEE WTGRIDPVTK LPICVNGHKE KFRRRKADAE CFSGELFQDL
     TPIEEPCDCD PDIDYECSLG FEFDAESNRC EPNLSILSSH YCVGKNLKRK VKVDRKSKVA
     GTKCKKDVKL KDNSFTLDCS KTSEPDLSEQ RIVSTTISFE GSPVQYIYLK QGTNTTLLDE
     TVILRTSLRT VYVSHNGGTT FDRVSIEDDV SFIDIYTNHY FPDNVYLITD TDELYVSDNR
     AISFQKVDMP SRAGLELGVR ALTFHKSDPN KFIWFGEKDC NSIFDRSCQT QAYITEDNGL
     SFKPLLENVR SCYFVGTTFD SKLYDFDPNL IFCEQRVPNQ RFLKLVASKD YFYDDKEELY
     PKIIGIATTM SFVIVATINE DNRSLKAFIT ADGSTFAEQL FPADLDFGRE VAYTVIDNWE
     SKTPNFFFHL TTSEDKDLEF GALLKSNYNG TTYTLAANNV NRNDRGYVDY EIVLNLNGIA
     LINTVINSKE LESEQSLETA KKLKTQITYN DGSEWVYLKP PTIDSEKNKF SCVKDKLSLE
     KCSLNLKGAT DRPDSRDSIS SGSAVGLLFG VGNVGEYLNQ DSSGLALYFS KDAGISWKEI
     AKGDYMWEFG DQGTILVIVE FKKKVDTLKY SLDEGETWFD YKFANEKTYV LDLATVPSDT
     SRKFIILANR GEEGDHETVV HTIDFSKVHQ RQCLLNLQDS NAGDDFEYWS PKNPSAVDGC
     MLGHEESYLK RIASHSDCFI GNAPLSEKYK VIKNCACTRR DYECDYNFAL ANDGTCKLVE
     GESPLDYSEV CRRDPTSIEY FLPTGYRKVG LSTCEGGLEL DNWNPVPCPG KTREFNRKYG
     TGATGYKIVV IVAVPLLVLL SATWFLYEKG IKRNGGFARF GVIRLGEDDD DDLQMIEENN
     TDKVVNVVVK GLIHAFRAVF VSYLFFRKRA AKMFGGSSFS HRHILPQDED AQAFLASDLE
     SESGELFRYA SDDDDAREID SVIEGGIDVE DDDEENINFD SR
//
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