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Database: UniProt
Entry: A0A0F0IMI9_ASPPU
LinkDB: A0A0F0IMI9_ASPPU
Original site: A0A0F0IMI9_ASPPU 
ID   A0A0F0IMI9_ASPPU        Unreviewed;      1992 AA.
AC   A0A0F0IMI9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
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=P875_00117520 {ECO:0000313|EMBL:KJK67098.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK67098.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK67098.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) 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}.
CC   -!- SIMILARITY: Belongs to the VPS10-related sortilin family.
CC       {ECO:0000256|ARBA:ARBA00008251}.
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:KJK67098.1}.
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DR   EMBL; JZEE01000201; KJK67098.1; -; Genomic_DNA.
DR   STRING; 1403190.A0A0F0IMI9; -.
DR   Proteomes; UP000033540; 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; 3.
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   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.
DR   SUPFAM; SSF50939; Sialidases; 1.
PE   3: Inferred from homology;
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:UP000033540};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, 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:ARBA00022448}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1992
FT                   /note="Vacuolar protein sorting/targeting protein 10"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002443559"
FT   TRANSMEM        1860..1881
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1909..1928
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          554..1179
FT                   /note="VPS10"
FT                   /evidence="ECO:0000259|SMART:SM00602"
FT   DOMAIN          1212..1849
FT                   /note="VPS10"
FT                   /evidence="ECO:0000259|SMART:SM00602"
FT   REGION          257..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          419..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..338
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1992 AA;  222947 MW;  DD849971F2543767 CRC64;
     MAKSVGPSSR MICGWIPLAL ALLESKCQTI IYGVDWALES REAASHGCLA FFSNVERLRL
     AHGDRWDGFH YQRRLAKVPR RLPFCTLQGR SYPTSAIKPL NKNRKCHPHK SSFPNTTKKL
     RKVDSLHSVH LAAQVDSRCF HSLPPKIQQK LFSKEEQDWF YRAQFEARFF DAAGEAPYPL
     EKARHCSRHQ PPEIRFSDGN SIATSRSSTL YFDLSDSDLS SDTDMDNSLC DNFRWFDDNG
     DLDLRLDEYH AHVAKVLPNS PPRRRPSLRT APSFNPDVSI RQPTSAVSRQ KAQSVHRSST
     FPTAPMNTMT RNSSTRPSSS QSQTHMPRSS TSSIDPSAQY YQDPEARLKL RVYLASPQNF
     DEAVEFGFPA QNNERTMPAE RKTKPPIFTG TFLDEEGTSV SDERCDKRMN VARLSYVHNS
     RSSDSGRPYP RHQSWLLPPR PGNQQHTGSN REMTLKMTLT RPDLRTTVPP PRVDPLKLPL
     EDSGSHLWGS CEDEQGLMRK MWPVMIYRWL LLVSCLLLAL LAQRGAAKSS SPKIAPPTKI
     DHKPSSLFYF EDTDTVLMNT VNGDLLRSVD AGETWSAVEG DDGGMKHHVL LIRQHPYDNK
     KAYALGPNGR HWVTTDQAKT WASFNIAEFP AIRHYPLVFH GGDSSKVIFQ GEECAGRYCI
     VRSYYTTDDF ATVKLLREST GGCAWAVGHP QFAEDLNLAE EIKDRSFCVV PGLKVPLPHA
     NRLVYSDDYF RGNAEGTETK LQEGRPVSGV ISTAAVKKFI VAAAKSKGTE ELALYVTVDA
     KNWHRAEFDG HRIEEDAYTM LESTNYSLQV DVLTSPRSGM GVLFTSNSNG TYFTRNIEHT
     NRNSEGMVDF EKIAGIQGIV LVNTVQNPEE VESGSAKKKI TSRISFDDGR TFQPLKSDGE
     NLHLHSVTAL RNIGRVFSSP APGLVMGIGN AGNHLQEYAE CNLYISDDAG VTWRRALKHP
     HKYEFGDQGA VVIAVRDDGR VDKINYSLDH GKEWASVELQ HKIYPTMVTT TPDSTSLKFI
     VVGSLKEGQD GEHVIYSIDF DGLHERKCEE GDFEKWPARL DEHGKPDCLM GHKQFYMRRR
     ANANCFVDEE FKDPEPIFEA CKCTTEDFEC EYRRTEDGKG CALPSPLTPP EGECKNPDDK
     FMGPSGWRLI PGDACIRDGG ENLDKEIERS CKDASSPSTD GKIGVTLQLF EARDYVQYYY
     LERQSSSSGS DETIIMLSSE HEVYVTHDHG KTWERPLKGE EITRVYLHPY SSDVAFLLTD
     GKEGFWTEDR GHTFKPFQAP APPTQDRFLQ VMAFHPVHKD RLIWTGAVDC HSGDCHSDAF
     IKKERGKNWE PLLSYVQKCE FESRETRPNS TNLVYCEQFE KQSKNGRLQL LSSDDFFNDN
     EVQFVDVINY ATMSEFIIVA SRQPENPDSL VASTSVDGRT FARAQFPPNV QVPVQTAYTV
     LESSTHAVFL HVTASSTEGG EYGPIIKSNS NGTSYVLSIS AVNRNSLGYV DFEKAQGLEG
     VAVVNVVSNA AEVSKKVPKK LKTMITHNDG AQWMLLPPPA KDADGKSFGC SVVAGKGTDD
     CSLHLHGYTE RKDERDTFAS GSAIGLMMAV GNVGDHLAGG DEADTFITND GGISWKSVKK
     GKYMWEYGDS GSVIVIVPES KPTKTIHYSL DEGDTWEEFR FSDVEVRIND ISTVPSDTSK
     NFLLWARVSN SEVQDKFATF NIDFSGVRPR PCLLDENQGN SDDYYIWEPK HPFQENNCLF
     GHSEQYHRKK PSAQCWNDWR ESHVHSIGTN CTCTRADYEC DYNYEPQSDG SCALVTGLPK
     PNAMEICKKD PDTIEYWEPT GYRRIPQTTC QGGLNLDHFV SKPCPNKEEE YKQKHGISGV
     GLFFAIVTPL AAAGAAGYYA YSKWDGKFGQ IRLGESAGTS QNFLSRDSWL VTVPIAIVAG
     TVAVARALPL LVTSLWRGAS GFIRLGRGRG YSRPYASRGS FAARRGDYTS IVDDEDELLG
     VEDADLDEDD EA
//
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