ID A0A1L7WMB6_9HELO Unreviewed; 1502 AA.
AC A0A1L7WMB6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Vacuolar protein sorting/targeting protein 10 {ECO:0000256|ARBA:ARBA00015369};
DE AltName: Full=Carboxypeptidase Y receptor {ECO:0000256|ARBA:ARBA00031354};
DE AltName: Full=Sortilin VPS10 {ECO:0000256|ARBA:ARBA00031250, ECO:0000256|ARBA:ARBA00031902};
GN ORFNames=PAC_03794 {ECO:0000313|EMBL:CZR53912.1};
OS Phialocephala subalpina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Mollisiaceae; Phialocephala;
OC Phialocephala fortinii species complex.
OX NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR53912.1, ECO:0000313|Proteomes:UP000184330};
RN [1] {ECO:0000313|EMBL:CZR53912.1, ECO:0000313|Proteomes:UP000184330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR53912.1,
RC ECO:0000313|Proteomes:UP000184330};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00025569}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000256|ARBA:ARBA00004166}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004166}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Prevacuolar compartment membrane
CC {ECO:0000256|ARBA:ARBA00004488}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004488}.
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DR EMBL; FJOG01000004; CZR53912.1; -; Genomic_DNA.
DR STRING; 576137.A0A1L7WMB6; -.
DR OrthoDB; 5840at2759; -.
DR Proteomes; UP000184330; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007034; P:vacuolar transport; IEA:UniProt.
DR Gene3D; 2.10.70.80; -; 2.
DR Gene3D; 3.30.60.270; -; 2.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
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; 3.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000313|EMBL:CZR53912.1};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Hydrolase {ECO:0000313|EMBL:CZR53912.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000313|EMBL:CZR53912.1};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000184330};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022927}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1502
FT /note="Vacuolar protein sorting/targeting protein 10"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009875168"
FT TRANSMEM 1385..1409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1430..1452
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 56..682
FT /note="VPS10"
FT /evidence="ECO:0000259|SMART:SM00602"
FT DOMAIN 726..1374
FT /note="VPS10"
FT /evidence="ECO:0000259|SMART:SM00602"
SQ SEQUENCE 1502 AA; 168962 MW; DE14F3F835767ADB CRC64;
MRLHIAARSI WQSLLCSSLF LTSSLLPSTV SAKKDAPSIT ENKFSFIPFN VNYFEDSDVL
LFEDGMSRNT YRSADAGESW EKVKGGMEGK MIELVMHQFD HERAYIITED NGNKHYKTSD
RGETWDEFEV GSLASIFREV MTFHAGDPDR IIFNGMDCTG IFCEELTLVT KDGFKNEPKF
LRAGTSGCHW AKSTDLFTTG QKDLDENRIL CVVKGRFSPW RKDYRLLVSD NYFAEENGVI
QEFEPELEAG RTVQGIVNMA VVKPYLIVAA SAEGTDEMAL YVSDDTIKWH RAIFPHDHKL
TEEAYTILEG TNYSIQIDVM NSRPSAPMGV FLTSNSNGTY FTRKMEHTDR NVYGLVDFEK
VTGVQGIMLI NTVDNWEAVD TSNAEKKIKS QISFDDGNLF EPITYKKKEL HLHSVTDLSN
SGRVFSSPAP GLLMGIGNTG SYLKDYSEGN LYVSDDAGLT WHEALDGPHK YEFGDQGSIL
VAVKDEGFTD EIKYSLDHGK NWKEIELKTK LRPIQLTTTQ DSTSLKFILE GIDESKPDAH
GYIVAIDFDG LHERQCKDDD MEKWYARVDE NGEPTCIMGQ KQSYRRRKAD ADCFLKQEFK
DPQYISEECE CTDADFECDY NFVRSTDRKE CTLAGALALP EGECKAFGPD DTFKGSSGWR
KIPGNKCKRT SGKQKDDPVD RKCVDAGGTP PATGKPDQAQ QVFSGKVFKN KVYLERSGVI
STGDDETVLV RTEDGVFISQ DHGKKWEQIF KDEAIVAIYP HPFFNDMVFF LTPSKKVFYS
TDRGKNIRSF NAPNEPNVDG YPVMNFHPKN KDWIIWIGAK DCPGSECHAV ASLTTDRGDG
DWKTLQRYVR KCEFIREPDT GYLRLELAQK KVDVPENKRE KLIYCEVRKR ESNDLKDNPW
RLVSSVDFFN EEPKVHFENV VDFATMSEFI VVATKDEEKS TLKVDASIDG ATFAAADFPH
GFNVDHQQGY TVLDSSTHSV FLHVTVSNEQ GFEYGSIIKS NSNGTSYVMA LDAVDRDSVG
YVDFEKMFGI EGVAMVNVVS NYKDKNFKKD GKKLKTMITH NDGAEWDFLS PPKADADGKK
YGCGSNTEKC ALHIHGYTER SDKSHTYSSA SAIGLMLGTG NVGEYLTSAK DADTFMTSDA
GINWKFVKKG TYMWEFGDQG SIVVIVKERE PTKEVFYSLD EGDTWVSYPF SDAEVEIDDL
TTVPSDNSRN FLLWGKSRDG KLVTFNLDFS GLTDQECKLD EGDVTGGDYY LWTPKHPKQD
DDCLFGHESQ YHRKRTDKDC YNGRMIPHLH DIAKNCSCTR RDFECDFNYE RQSDGSCALV
SGLSPPDPQL VCKVDEDRIE YDDPTGYRRI PITTCVEGLQ MDKSVSHPCP GKGDQFNKKH
GLSGVAIFFI IIISVGLAAG FGYWVWMNWA NKFGQIRLGE QSSFDHEAWY IKYPVAGIAG
IITIIAAAPS IASTIWSSAR TAFGGNRPAR FTTRDSFARG GNYAIVDEDE GELLGEESDE
EV
//
