VPS10_TRIVH
ID VPS10_TRIVH Reviewed; 1486 AA.
AC D4D4B1;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 34.
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=TRV_01926;
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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}.
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; ACYE01000103; EFE43258.1; -; Genomic_DNA.
DR RefSeq; XP_003023876.1; XM_003023830.1.
DR AlphaFoldDB; D4D4B1; -.
DR SMR; D4D4B1; -.
DR PRIDE; D4D4B1; -.
DR EnsemblFungi; EFE43258; EFE43258; TRV_01926.
DR GeneID; 9582508; -.
DR KEGG; tve:TRV_01926; -.
DR HOGENOM; CLU_000700_0_0_1; -.
DR Proteomes; UP000008383; 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 Repeat; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1486
FT /note="Vacuolar protein sorting/targeting protein 10"
FT /id="PRO_0000407538"
FT TOPO_DOM 26..1349
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1350..1370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1371..1401
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1402..1422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1423
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REPEAT 377..386
FT /note="BNR 1"
FT REPEAT 437..447
FT /note="BNR 2"
FT REPEAT 483..493
FT /note="BNR 3"
FT REPEAT 718..728
FT /note="BNR 4"
FT REPEAT 1100..1110
FT /note="BNR 5"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 900
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 965
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1486 AA; 166914 MW; E69FBFA0B6E1FB10 CRC64;
MIVRSLLLAG SLLLASVVPA SFTLAKSDGP QIKVKEFDKV PTDVHYFEDT DTIILSGKKA
ELYISTDAAA SWNLLEGKTG ILYPNKYHTQ SAVIYGPNRK HWVTFDAAKT WREFEVPDKL
AFGGGFMPFT FHGKDAEKVL LSAEECQFMT CRHVTYYTTD GFKTVKRLFE GDMGCFWAVG
NPAFGEGEPH LPDKLDDRVF CIWPHATPLD LTRRLVYSDT YFSDRKAVAV EAGGRDIKGV
NNMASVKKFL LLAASSVGTS EAAIYVSKDA VHWDRADFYG GPKVRGGKFT VLESTNYSIQ
VNVASRRSRV PIGSLFTSDS TGTSFTMNLD GVNEDKDMIT DFEQVSGIQG IFLVNIVENA
EEVKKGATRE KKLVSRISFD DGRTFKPLKC GDKELHLHSI TRPSNIGRTY SSPAPGLVMG
IGNTGDKLGT YETGDTFVSN DAGVTWRKAL DKAHKYEFGD QGSLLVAVFD EYKDKIFTDE
ISYSLNHGKD WKKAKLPHRV TALQLTTTPD STSLQFLLVA EDEKKKFYVM SIDFSDVHER
KCEKKDFERW PARLDEKGEP DCLMGHKQFY KRRKADADCF VKEKFKEPLP ETEPCQCTKE
DFECAAGFLR NKDYECEPHR KVSPPEGKCK NPDDKFMGPS GYRLIPGDDC LKKGGVDLEK
EVERTCKDAT KAPVSGQISV ETTPFKTKNL NYRYLERSDT SSGDDETVIL KTDDGDLFVT
RDHGKTWQRG KFKEPISLYI PHKYDNDVIY LLTEGKKAYW SIDRAHTFHS FEGKLPITRT
LGTLPLYFHP DHPDWLIWIG GQDCKGKKCT DLAYYSKNRG DEWDLLLRGV GKCMFVGKEG
ELTADDLIFC SQHEHEDPSK SLRLISSDDM FTKKTSIHFD GKPIVGYAKM SEFIVVATKN
GTELSSFTSV DGKTFAHAAF PPNYHIDAEY AYTVLDSSTH SIFLHVTDHP AKMHEFGSIL
KSNSNGTSYV LSLPNANRND RDYVDFEKIQ VVEGVALANI VINPDEVKGK GQEKKFRTLI
THNDGSEWAL LPPPKKDVDG KSFDCKVKDK GTDDCALHLH GFTERRENRD SMSSGSAVGL
IIGVGNVGSS LTPRAESDTY MSRDAGITWH QIKKGRYQWE FGDQGSIVVV VAEEKPTKVL
SYSLDEGETW TDFEFSDKEV TVEDISTVPS DTSRNFILWC RPGSSNEIVA YNVDFSGLKE
REKQCVLKKE SPEADDYYLW SPKHPMQKNN CLFGHVSMYH RKRPEAKCYN GPKLDRLSSE
KKNCECTRQD YECDYNYGRQ SDGSCALVKG LKPADPMQIC KDDPEAIEYF EPTGYRKLPV
STCEGGHQLD HLVARPCPNK KKEFDEKHPG IGGFGLFFAI FFPVAIATGV GYWAFSKWDG
KFGRIRLGES QPESIFSRDS PLISVPVTIV AGTVAVITAL PLLFSSLWRS FRGYTRLPGS
WWGQRQRPYA SRGAFAARRG EYVGVVDDED ELLGAEEFEG DEEEDV
