VTH2_YEAST
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 03-AUG-2022, entry version 166.
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 IntAct; P40890; 1.
DR STRING; 4932.YJL222W; -.
DR iPTMnet; P40890; -.
DR MaxQB; P40890; -.
DR PaxDb; P40890; -.
DR PRIDE; P40890; -.
DR EnsemblFungi; YJL222W_mRNA; YJL222W; YJL222W.
DR GeneID; 853233; -.
DR KEGG; sce:YJL222W; -.
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 BioCyc; YEAST:G3O-31644-MON; -.
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:0016021; C:integral component of membrane; IBA:GO_Central.
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:0006892; P:post-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006623; P:protein targeting to vacuole; IGI:SGD.
DR Gene3D; 2.130.10.10; -; 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 Pfam; PF15902; Sortilin-Vps10; 2.
DR Pfam; PF15901; Sortilin_C; 2.
DR SMART; SM00602; VPS10; 2.
DR SUPFAM; SSF50939; SSF50939; 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
