ID   VTH2_YEAST              Reviewed;        1549 AA.
AC   P40890; D6VVX5;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   02-SEP-2026, entry version 183.
DE   RecName: Full=VPS10 homolog 2;
DE   AltName: Full=Sortilin VTH2;
DE   Flags: Precursor;
GN   Name=VTH2; OrderedLocusNames=YJL222W; ORFNames=HRC1549, J0213;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7725802; DOI=10.1002/yea.320101216;
RA   Vandenbol M., Durand P., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
RT   "Sequence analysis of a 40.2 kb DNA fragment located near the left telomere
RT   of yeast chromosome X.";
RL   Yeast 10:1657-1662(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   FUNCTION.
RX   PubMed=8662642; DOI=10.1074/jbc.271.20.11865;
RA   Westphal V., Marcusson E.G., Winther J.R., Emr S.D., van den Hazel H.B.;
RT   "Multiple pathways for vacuolar sorting of yeast proteinase A.";
RL   J. Biol. Chem. 271:11865-11870(1996).
RN   [5]
RP   FUNCTION.
RX   PubMed=8636229; DOI=10.1083/jcb.133.3.529;
RA   Cooper A.A., Stevens T.H.;
RT   "Vps10p cycles between the late-Golgi and prevacuolar compartments in its
RT   function as the sorting receptor for multiple yeast vacuolar hydrolases.";
RL   J. Cell Biol. 133:529-541(1996).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
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.
CC       {ECO:0000269|PubMed:8636229, ECO:0000269|PubMed:8662642}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC   -!- MISCELLANEOUS: Present with 279 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the VPS10-related sortilin family.
CC       {ECO:0000305}.
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DR   EMBL; Z34098; CAA83988.1; -; Genomic_DNA.
DR   EMBL; Z49497; CAA89519.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08591.1; -; Genomic_DNA.
DR   PIR; S50705; S50705.
DR   RefSeq; NP_012313.1; NM_001181655.1.
DR   AlphaFoldDB; P40890; -.
DR   SMR; P40890; -.
DR   BioGRID; 33560; 12.
DR   DIP; DIP-6665N; -.
DR   FunCoup; P40890; 122.
DR   IntAct; P40890; 1.
DR   STRING; 4932.YJL222W; -.
DR   GlyCosmos; P40890; 3 sites, No reported glycans.
DR   GlyGen; P40890; 3 sites.
DR   iPTMnet; P40890; -.
DR   PaxDb; 4932-YJL222W; -.
DR   PeptideAtlas; P40890; -.
DR   EnsemblFungi; YJL222W_mRNA; YJL222W; YJL222W.
DR   GeneID; 853233; -.
DR   KEGG; sce:YJL222W; -.
DR   AGR; SGD:S000003758; -.
DR   SGD; S000003758; VTH2.
DR   VEuPathDB; FungiDB:YJL222W; -.
DR   eggNOG; KOG3511; Eukaryota.
DR   HOGENOM; CLU_000700_0_0_1; -.
DR   InParanoid; P40890; -.
DR   OrthoDB; 443634at2759; -.
DR   BioCyc; YEAST:G3O-31644-MONOMER; -.
DR   PRO; PR:P40890; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P40890; protein.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005048; F:signal sequence binding; IGI:SGD.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0006895; P:Golgi to endosome transport; IBA:GO_Central.
DR   GO; GO:0006896; P:Golgi to vacuole transport; IGI:SGD.
DR   GO; GO:0006623; P:protein targeting to vacuole; IGI:SGD.
DR   CDD; cd15482; Sialidase_non-viral; 1.
DR   FunFam; 3.30.60.270:FF:000005; Sortilin; 1.
DR   FunFam; 3.30.60.270:FF:000008; Vacuolar protein sorting/targeting protein PEP1; 1.
DR   FunFam; 2.130.10.10:FF:000998; VPS10 homolog 2; 1.
DR   FunFam; 2.130.10.10:FF:002485; VPS10 homolog 2; 1.
DR   Gene3D; 2.10.70.80; -; 1.
DR   Gene3D; 2.120.10.10; -; 1.
DR   Gene3D; 3.30.60.270; -; 2.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR036278; Sialidase_sf.
DR   InterPro; IPR031777; Sortilin_C.
DR   InterPro; IPR031778; Sortilin_N.
DR   InterPro; IPR006581; VPS10.
DR   InterPro; IPR050310; VPS10-sortilin.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR12106; SORTILIN RELATED; 1.
DR   PANTHER; PTHR12106:SF27; SORTILIN-RELATED RECEPTOR; 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; 2.
DR   PROSITE; PS52072; VPS10P; 2.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Golgi apparatus; Membrane;
KW   Nucleotide-binding; Protein transport; Receptor; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..1549
FT                   /note="VPS10 homolog 2"
FT                   /id="PRO_0000014331"
FT   TOPO_DOM        22..1369
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1370..1390
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1391..1549
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          23..694
FT                   /note="Vps10p 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01417"
FT   REPEAT          57..68
FT                   /note="BNR 1"
FT   REPEAT          101..112
FT                   /note="BNR 2"
FT   REPEAT          159..170
FT                   /note="BNR 3"
FT   REPEAT          228..239
FT                   /note="BNR 4"
FT   REPEAT          393..404
FT                   /note="BNR 5"
FT   REPEAT          465..476
FT                   /note="BNR 6"
FT   REPEAT          511..522
FT                   /note="BNR 7"
FT   DOMAIN          704..1356
FT                   /note="Vps10p 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01417"
FT   REPEAT          740..751
FT                   /note="BNR 8"
FT   REPEAT          837..848
FT                   /note="BNR 9"
FT   REPEAT          1040..1051
FT                   /note="BNR 10"
FT   REPEAT          1119..1130
FT                   /note="BNR 11"
FT   REPEAT          1160..1171
FT                   /note="BNR 12"
FT   REGION          23..566
FT                   /note="10-bladed beta-propeller 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01417"
FT   REGION          575..623
FT                   /note="10CCa cysteine-knot 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01417"
FT   REGION          626..694
FT                   /note="10CCb cysteine-knot 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01417"
FT   REGION          704..1216
FT                   /note="10-bladed beta-propeller 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01417"
FT   REGION          1224..1280
FT                   /note="10CCa cysteine-knot 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01417"
FT   REGION          1282..1356
FT                   /note="10CCb cysteine-knot 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01417"
FT   REGION          1479..1549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1489..1501
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1535..1549
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        479
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        769
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        986
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        418..426
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01417"
FT   DISULFID        575..607
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01417"
FT   DISULFID        590..623
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01417"
FT   DISULFID        626..679
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01417"
FT   DISULFID        633..645
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01417"
FT   DISULFID        658..692
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01417"
FT   DISULFID        1066..1074
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01417"
FT   DISULFID        1224..1263
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01417"
FT   DISULFID        1247..1280
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01417"
FT   DISULFID        1282..1339
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01417"
FT   DISULFID        1289..1301
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01417"
FT   DISULFID        1316..1354
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01417"
SQ   SEQUENCE   1549 AA;  174402 MW;  B260CF7C927B4E4F CRC64;
     MALFRALYII WVFLLIPLSN AEEFTPKVTR TLSRYVFDIV NFDDSNTLIR AEEDSVEISF
     DAGENWKTID EIEEPIESFV VDPFRGHDRA FAFVKTAPKF YVTDDQGKSW RPLTIPISEK
     ASNYFCDVTT HPIKKKHLII RCDLLTIKNS GLMYVGREIY TTNDGVSFSQ VKPSFGKIDG
     HISTARCDFI KSSEDSDLGG NDASILCLFR NTEYIESTGS TIDKSELILS ADGGETFKEL
     VQFKDKVVSR YEILKHHVIV LTQDDMYNEM SSTNIWISND VSTFQVARTP TKIRHVNMGQ
     IHEDSIGRIV LPVSRERDDE DSNQPGAAEV LISDSEGLKF LPINWIPNNQ FGYINVAYPG
     FLKGTFFGSF HPFIEYSDRK RKYSRQKVRE ETKVSVDNGL TWTNLKVVDR ENVDLFGCDV
     TKPERCSLQT HFYDLRNLNP SAGIMMISGI VGDGSAYNWK EEKTFISRDS GLTWRLVHNS
     TGLYTTGDLG NIIMYIPYRS NENGDVPSKF YYSLDQGKTW GEYDLIMPIY PYRLVSTISD
     GSGSKFILTG TSITEDPIFI TYSIDFSAVF DYKSCEEGDF EDWNLADGKC VNGAKYKYRR
     RKQDAQCLVK KAFKDLSLDE TPCNSCTGSD YECSFEFVRD AKGDCIPDYN LIALSDICDK
     SKGKSVLVKP LQLIKGDKCK TPMKIESVDI PCDEIPKEGS SDKEIVTTEN KFDFEIKFYQ
     YFDTVADESL VMLNSIGDAY ISHDGGQTIK RFDTDGEKIV EIVFNPYFNS SAYLFGSKGN
     IFLTHDRGYS FMIAKLPEAR QLGMPLDFSA KAQDTFIYYG GKNCESILSP ECHAVAYLTK
     DGGETFTEML DNAIHCEFAG TLFKYPSNDD MVMCQVKEKF SQTRSLVSST DFFQDDRKTV
     FENIIGYLST GGYIIVAVPH EDNELRAYVT NDGAEFTEAK FPYDEDIGKQ DAFTILGSEE
     GSIFLHLATN LESGHDFGNL LKSNSNGTSF VTLEHAVNRN TFGYVDFEKV QGLEGIIITN
     IVSNSEKVGE NKEDEQLKTK ITFNDGSDWN FLKPPKKDSE GKKFPCDSVS LDKCSLHLHG
     YTERKDIRDT YSSGSALGMM FGVGNVGDRL LPYEECSTFL TTDGGETWTE VKKGPHQWEY
     GDHGGVLVLV PENAETDSIS YSTDFGKTWK DYKFCGDKVL VKDIITVPRD SALRFLLFGE
     AKNMGSGSFR TYTIDFRNIF ERQCEFDITG RKRADFKYSP LGSRTGCLFG HKTEFLRKTD
     EKCFIGNIPL SEFSRNVKNC PCTRQDFECD YNFYKASDGT CKLVKGLSSA NGADICKKEP
     DLIEYYDSSG YRKIPLSTCK GGLKLDAHLA PHPCPGKEKA FREKYSINTG AYALVFVTIL
     LVIFFVAWFV YDRGIRRNGG FSRFEEIRLG DDGLIENNRT DRVVNIIVRL GLCISLITKS
     AFQRAKAGTA QLSSKFRARF GNKKGATYSS LLHDQLSDEP DGFHEDSNDL SSFRGQGSNS
     EIEQEDVDTS QQEHTSRTDL LGASNIPDAL PARSASHESD LAAARSEDK
//