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 27-MAR-2024, entry version 173. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 IntAct; P40890; 1. DR STRING; 4932.YJL222W; -. DR GlyCosmos; P40890; 3 sites, No reported glycans. DR GlyGen; P40890; 3 sites. DR iPTMnet; P40890; -. DR MaxQB; 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 GeneTree; ENSGT01030000234563; -. DR HOGENOM; CLU_000700_0_0_1; -. DR InParanoid; P40890; -. DR OrthoDB; 5840at2759; -. 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; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0005048; F:signal sequence binding; IGI:SGD. 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 GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR CDD; cd15482; Sialidase_non-viral; 2. 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; 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; 2. PE 1: Evidence at protein level; KW Glycoprotein; Golgi apparatus; Membrane; Nucleotide-binding; KW Protein transport; Receptor; Reference proteome; Repeat; Signal; KW 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 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 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 1479..1549 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1489..1505 FT /note="Polar 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" 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 //