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Database: UniProt
Entry: A0A163JD38_DIDRA
LinkDB: A0A163JD38_DIDRA
Original site: A0A163JD38_DIDRA 
ID   A0A163JD38_DIDRA        Unreviewed;      1481 AA.
AC   A0A163JD38;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=ST47_g2590 {ECO:0000313|EMBL:KZM26286.1};
OS   Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS   rabiei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX   NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM26286.1, ECO:0000313|Proteomes:UP000076837};
RN   [1] {ECO:0000313|EMBL:KZM26286.1, ECO:0000313|Proteomes:UP000076837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ArDII {ECO:0000313|EMBL:KZM26286.1,
RC   ECO:0000313|Proteomes:UP000076837};
RX   PubMed=27091329; DOI=10.1038/srep24638;
RA   Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT   "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT   Ascochyta rabiei provides insight into the necrotrophic effector
RT   repertoire.";
RL   Sci. Rep. 6:24638-24638(2016).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZM26286.1}.
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DR   EMBL; JYNV01000110; KZM26286.1; -; Genomic_DNA.
DR   STRING; 5454.A0A163JD38; -.
DR   Proteomes; UP000076837; 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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007034; P:vacuolar transport; IEA:UniProt.
DR   CDD; cd15482; Sialidase_non-viral; 1.
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; 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   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; 2.
PE   4: Predicted;
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076837};
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..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1481
FT                   /note="Vacuolar protein sorting/targeting protein 10"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007843278"
FT   TRANSMEM        1355..1379
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1411..1432
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          48..666
FT                   /note="VPS10"
FT                   /evidence="ECO:0000259|SMART:SM00602"
FT   DOMAIN          710..1347
FT                   /note="VPS10"
FT                   /evidence="ECO:0000259|SMART:SM00602"
FT   REGION          643..674
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1022..1051
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1451..1481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        646..674
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1481 AA;  166474 MW;  CD5012B09AEE3BE9 CRC64;
     MRYNAGLLLP ALLALAPSIA AKKETPLVET TAFKNEIVNI LYFDDSAVAL LQELESGRIW
     RSKDAGKGWK REEEMNGNGI LKSPYDNNVA TVLGETKHWI TYDQGENWSS FKTELPPSPE
     APLSWHATDP KKILINEIDN CFTAPCLGRT YYTTDGFKSE PKLLIEDRRM CQWAKGSERF
     LMDSDKHDDR ILCITRGKYS DRTKDFRLLT SDNYFKDFDE PVMSSGRTVQ GMANMAAVKG
     YIVAAAKADH SSELTLYVTT DTDTWHHAEF GDHKVEQDAY TILESTNYSI QVDVMTSKYT
     AMGTLYTSNS NGTYFTKNVE HMNRNERGFV DFEKIANIQG VVMVNLVDNW KDYEKKGSPK
     KLKSKISFDD GRTFEKLEVK GKDKDLHLHS VTDLHNSGRV FSSLAPGMVM GVGNTGDQLG
     KYTDGDLYVS DDAGLTWELA LEEAHKYEFG DQGSILVAVY DEGDTDKVMY SLKHGRKNTW
     KEIDVGYKFR ARELTTLPDS TSQKFMLYAS KKKDGGGREH VIIHLDFSEL HERKCGEKDF
     EDWSVRKEDD GKPSCVMGHK QLFKRRKWDA DCFVSEPFKD PTPRFEPCEC DAVRDYECDV
     NFTPNGEGKE MKCEPSDQVR LPAGACKGDD KTYKGSSGWR KIPGNQCKGE TERDREVERP
     CGDAERPPPK SDKITSEITK FKGSNFMEHY YLERDAQNRD DSDNARDRDE TIVLLTSERE
     AYITHDHGKK WKKAVDDEIV RIYPHTYENN YVYFLTASKK VYYSEDRGLK DSIHSFEAPV
     MPNTQLLQIL QFHPKQKGWL IWLGGEHCEK LGDKDCHTVS YVSQKNGVSG SWEAMLPYVK
     KCAFVWREAG RDVKEERVFC EQYTKEEMGA PVELISSDDW FKKKDVKFES VVEFATMSEF
     IIVATKGKDG KSLELSASLD ANIFAEAKFP PKFAVDHQTA YTVLDSSTHA IFLHVTVNPR
     PDQEYGSIIK SNSNGTSYVM SLNGVNRNTE GYVDFEKMQG LEGVALANII ANVDEVNKGT
     KKRKQTRITH NDGAEWAPLD APEKDSDGKS YSCDVSNPAK CSLHIHGYTE RSDPRETYSS
     PTAVGLMLGV GNVGSELATL GESSTFMTTD AGITWKEIKK GAYAWEFGDQ GSVIVIVRRG
     EDTDHLYYSL DSGDKWTLYK FAEHAVRIDA ITTVPSDTSL NFLLWGKDGK ELVAINVDFS
     GLEEFSKKCN LDEKNPGSGD YDLWTPQHPM QQDQPECLFG HVAEYHRKKR DARCRNGERI
     DHMHEIARNC TCTRRDFECA YNYERQPGGE CTLIPGLTLE DPKAVCSKGA REYWDNSAFR
     KIPLSTCEGG QEFDHVGAPH PCPGFEEEFQ KKHGIGGFAL FLAIVLPFAA AGGIGYYVWR
     NWNGIGKFGA IRLGDSGGGF NSDAPWVKYP VAVVSGLVAI IAAIPMLVGS LWRMVSGGRG
     GGGYGGRTYT SRSSFSRGRG DYAVVDPDEG ELLGDESDEE V
//
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