VTH2_YEAS8
ID VTH2_YEAS8 Reviewed; 1495 AA.
AC C8ZAZ9;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=VPS10 homolog 2;
DE AltName: Full=Sortilin VTH2;
DE Flags: Precursor;
GN Name=VTH2; ORFNames=EC1118_1J11_0078g;
OS Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=643680;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lalvin EC1118 / Prise de mousse;
RX PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(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.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 319 molecules/cell in log phase SD medium.
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; FN393075; CAY80565.2; -; Genomic_DNA.
DR AlphaFoldDB; C8ZAZ9; -.
DR SMR; C8ZAZ9; -.
DR PRIDE; C8ZAZ9; -.
DR EnsemblFungi; CAY80565; CAY80565; EC1118_1J11_0078g.
DR HOGENOM; CLU_000700_0_0_1; -.
DR Proteomes; UP000000286; Chromosome X, Scaffold EC1118_1J11.
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; 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 3: Inferred from homology;
KW Glycoprotein; Golgi apparatus; Membrane; Protein transport; Receptor;
KW Repeat; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1495
FT /note="VPS10 homolog 2"
FT /id="PRO_0000407549"
FT TOPO_DOM 23..1369
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1370..1390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1391..1495
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 58..67
FT /note="BNR 1"
FT REPEAT 101..111
FT /note="BNR 2"
FT REPEAT 229..238
FT /note="BNR 3"
FT REPEAT 394..403
FT /note="BNR 4"
FT REPEAT 465..475
FT /note="BNR 5"
FT REPEAT 511..520
FT /note="BNR 6"
FT REPEAT 740..750
FT /note="BNR 7"
FT REPEAT 837..847
FT /note="BNR 8"
FT REPEAT 1119..1129
FT /note="BNR 9"
FT REPEAT 1161..1170
FT /note="BNR 10"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 CARBOHYD 1279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1495 AA; 168533 MW; D132877BB3EE9328 CRC64;
MALFRALYII WVFLLIPLFN AEEFTPKVTR TLSRYVFDIV NFDDSNTLIR ADEDSVEISF
DAGENWKTID GIEEPIESFV VDPFRGHDRA FAFVKTAPKF YVTDDQGKSW RPLTIPISEK
ASNYFCGITT HPIKKKHLII RCDLLTINDS GVMHVGREIY TTNDGVSFSQ VKPSFGKIDG
HISTARCDFI KSSEDSDLGG NDASILCLFR NTEYIESTGS TIDKSELILS ADGGETFKEL
VQFKDKVVRR YEILKYHVVV LTQDDMYNEM SSMDIWISND VCTFQIAHTP TKIRHVNMGQ
IHEDSIGRIV LSVSRERDDE DSNQPGAAEV LISDSEGLKF LPIKWIPNNQ FGYINVAYPG
FLKGTFFGSF HPFIEYSDRK RKYSRQKVRE ETKVSVDNGL TWSNLKVVDR ENVDSFGCDV
TKPERCSLHT YFYDLRNLRP SAGIMMISGI VGDGSVYDWN EEKTFISRDS GLTWRLVHNS
TGLYTTGDLG NIIMYIPYRS NENGDVPSKF YYSLDQGKTW GEYDLIMPIY PYRLISTISD
GSGSKFILTG TSITDDPISI TYSIDFSAVF DYKSCEEGDF EDWNLADGKC VNGAKYKYRR
RKQDAQCLVK KAFKDLSLDE TPCNSCTGSD YECSFEFVRD AKGDCIPDYN LIALSDICDK
SKDKSVLVEP LQLIKGDKCK TPMKIEPVDI PCDEIPEEGS SDKEIVTTEN KFDFEIKFYQ
YFDTVADESL VMLNSIGDAY ISHDGGQTIK RFDTDGEKIV EVVFNPYFNS SAYLFGSKGN
IFLTHDRGYS FMIAKLPEAR QLGMPLDFSA KAQDTFIYYG GKNCESILSP ECHAVAYLTK
DGGETFTEML DNAIHCEFAG TLFKYPSNDD MVMCQVKEKF SQTRSLVSST DFFQDDKKTV
FENIIGYLST GGYIIVAVPH ENNELRAYVT NDGAEFAEAK FPYDEDIGKQ DAFTILGSEE
GSIFLHLATN LESGHDFGNL LKSNSNGTSF VTLEHAVNRN TFGYVDFEKV QGLEGIIITN
IVSNSEKVGE HKGDEQLKTK ITFNDGSDWN FLKPPKKDSE GKKFLCDSVS LDKCSLHLHG
YTERKDIRDT YSSGSALGMM FGVGNVGDRL LPYEECSTFL TTDGGETWTE VKKGPHQWEY
GDHGGVLVLV PENAETDSIS YSTDFGKTWK DYKFCGDKVL VKDVITVPRD SALRFLLFGE
AKNMGSGSFR TYTIDFRNIF ERQCEFDITG KKRADFKYSP LGSRTDCLFG HKTEFLRKTD
EKCFIGNIPL SEFSRNVKNC SCTRQDFECD YNFYKASDGT CKLVKGLSSA NGADICKKEP
DLIEYYDSSG YRKIPLSTCK GGLKLDAHLA PHPCPGKEKA FREKYPINTG AYALVFVTIL
LVIFFAAWFV YDRGIRRNGG FSRFEEIRLG DDGLIENNRT DRVVNIIVRL GLCISLITKS
AFQRAKAGTA QLSSKFRARF GNKKGATYSS LLHDQLSDAF QRAKAGTAQL SCFKI
