VPS10_TALMQ
ID VPS10_TALMQ Reviewed; 1504 AA.
AC B6QMS8;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 25-MAY-2022, entry version 55.
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; ORFNames=PMAA_060750;
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; DS995903; EEA22297.1; -; Genomic_DNA.
DR RefSeq; XP_002150906.1; XM_002150870.1.
DR AlphaFoldDB; B6QMS8; -.
DR SMR; B6QMS8; -.
DR STRING; 441960.B6QMS8; -.
DR EnsemblFungi; EEA22297; EEA22297; PMAA_060750.
DR GeneID; 7028387; -.
DR KEGG; tmf:PMAA_060750; -.
DR VEuPathDB; FungiDB:PMAA_060750; -.
DR HOGENOM; CLU_000700_0_0_1; -.
DR OrthoDB; 1046610at2759; -.
DR PhylomeDB; B6QMS8; -.
DR Proteomes; UP000001294; Unassembled WGS sequence.
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; -; 1.
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.
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..31
FT /evidence="ECO:0000255"
FT CHAIN 32..1504
FT /note="Vacuolar protein sorting/targeting protein 10"
FT /id="PRO_0000407530"
FT TOPO_DOM 32..1370
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1371..1391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1392..1423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1424..1444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1445..1504
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REPEAT 70..80
FT /note="BNR 1"
FT REPEAT 118..128
FT /note="BNR 2"
FT REPEAT 394..403
FT /note="BNR 3"
FT REPEAT 455..465
FT /note="BNR 4"
FT REPEAT 739..749
FT /note="BNR 5"
FT REPEAT 1120..1130
FT /note="BNR 6"
FT REPEAT 1161..1171
FT /note="BNR 7"
FT REGION 1485..1504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
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 998
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1504 AA; 168450 MW; 56DE5CF18E0AB491 CRC64;
MTRQWLHLTT SPLLLLLLLI TISSLTGGAV AKSDGPKIAL KEVEVVPEQP FYFENTDTVL
FLSAATGEVY RSFDGGLEWH VIGKGEGEEG LTNDAVVILP HKYDNKKAYI LGRHGAHWVT
TDQGRTWRRF EVPAAPSMLL YERLRFHGED SRKVIFMGER CSLVACLETA FYTLDDFETV
APLRDTARGC FWAVGTPAFA ESTTEYAKEI GDRVLCIVHG LKNPFAAAYR LVYSDSFFKD
NEDGIEANLN AGRPVAGIIN AAARTKYIMV AAKSQGTDEL AMFVTDDAIT WHRAEFGNHK
IEEGAYTVLG GTNYSIQVDV KNTDRSESMG VLFTSNSNGT YFTRNIEHTN RNMEGYVDFE
DIIGVQGIVL VNVVDNWEEV EKKFDADKKV ISKISFDDGR TFQPLKANDK DLHVHSVTDF
QNIGRVFSSP APGIVLGVGN TGSHLKSYTK DGNLYVSDDA GVTWRLALEK PHKYEIGNKG
AVIVAIKDDG DPTGKIQFSI NHGKDWDTAE LDHKIIPFYL TTTPDSTSLK FLLVGFSEES
RKWSIFAIDF EGLHERECKE SDFEEWPARL DEKGEPDCLM GHKQYYRRRK SDADCFITET
MFKTPTPEFK ACKCTAEDFE CDYNFVRSED RTKCVPATPL KAPEGACKSE DDTFKGPSGW
RLIPGNACIR DGGEELDKEI DRPCKDVLKA PPGDAKAISS TVNYIEAEMF KSFYYLERAG
SSRGEDETIV MLTSNGKLYV THNHGKTWTH ELTDVKFEEI VRNPYLNDRA FFLTNGKKQF
YTINRAETFE SFTAPAEKNP DPGMTLGFHE IYKDWMIWTG PSDCSHGNCP KDSYFTKHRG
DGWEILLRAV INCEFMAQES RGEESNNLIF CNQHEAEEVD GQRMLVTSND FFDTSKTPLP
RIIAFAKASE FIIIAKPDPE KEHAMKFDVS VDGVTFADAE YSVNLEVSME LGYTLLQSTT
HSVFMHVTLN DQRDHQYGLL IKSNSNGTSY VLSLSDVNRS NDGYVDFEKL QGLEGVVIAN
VVSNTKDVEK GSEKKLRTMI THNDGAQWTL IPPPVKDSEG KGYNCGSDGK PTDKCALHLH
GYTERRDSRN TFASASAIGL SFGVGNVGES LVSKADASTF FSRDGGISWK EVKKGSHFWE
YGDQGSVLVL VAEGKPTREV FFSTDEGDTW EVYQFSEKEV TVLDFSTVPS DTSKNFLIWA
REAGSDKLVT INLDFSGLRD RTCHLDEDTG ESEDYYIWEP KHPLQEGNCL FGHVEQYHRK
NPKSHCWNDW SEAHVHSISH NCSCTFQDYE CDYNYERQTD GSCALVPGLP KPNAIEYCKE
NPDAVEYWEP TGYRRIPITT CTGGKNLDQW ISHPCPGHQE EYERKHGVSG AVIFFAIIIP
IAIAVAAGYW VYTHWDGKFG QIRLGEGGGQ SFITSRGDSP FITIPVVIIA GTVAAVKVLP
LLFMSLWRSA SGYVHLPGSR GPRPYATRGA FASRRGDYTN VVDDEDELLG DDEFEDEEGD
EERS
