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Database: UniProt
Entry: A0A177D7V1_ALTAL
LinkDB: A0A177D7V1_ALTAL
Original site: A0A177D7V1_ALTAL 
ID   A0A177D7V1_ALTAL        Unreviewed;      1480 AA.
AC   A0A177D7V1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=CC77DRAFT_1099524 {ECO:0000313|EMBL:OAG14999.1};
OS   Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Alternaria; Alternaria alternata complex.
OX   NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG14999.1, ECO:0000313|Proteomes:UP000077248};
RN   [1] {ECO:0000313|EMBL:OAG14999.1, ECO:0000313|Proteomes:UP000077248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG14999.1,
RC   ECO:0000313|Proteomes:UP000077248};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-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; KV441496; OAG14999.1; -; Genomic_DNA.
DR   RefSeq; XP_018380420.1; XM_018530012.1.
DR   STRING; 5599.A0A177D7V1; -.
DR   GeneID; 29115606; -.
DR   KEGG; aalt:CC77DRAFT_1099524; -.
DR   VEuPathDB; FungiDB:CC77DRAFT_1099524; -.
DR   OMA; ATMSEFI; -.
DR   OrthoDB; 5840at2759; -.
DR   Proteomes; UP000077248; 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:0046907; P:intracellular transport; IEA:UniProt.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; 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:UP000077248};
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:ARBA00022448}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1480
FT                   /note="Vacuolar protein sorting/targeting protein 10"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008059093"
FT   TRANSMEM        1354..1375
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          49..668
FT                   /note="VPS10"
FT                   /evidence="ECO:0000259|SMART:SM00602"
FT   DOMAIN          706..1343
FT                   /note="VPS10"
FT                   /evidence="ECO:0000259|SMART:SM00602"
FT   REGION          646..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1016..1043
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1459..1480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        647..675
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1480 AA;  166707 MW;  C2E74595B9FD6FC0 CRC64;
     MMKYLKGLLL PALLALASTA AAKKEEPLVE TTAFKNDIVN ILYFDDSGVA LLQELETGSI
     WRSHDAGKGW KQLQDLHGLG IIKSPYDNKV ALVLGEKKHW VTYDQGENWD SFETELPPSP
     QVPVNWHAQD SKKILIHEIE NCFTAPCLGR TYYTTDGFKS KPKILIDDRR MCQWAKGAER
     FLQGQDKHDD RILCITRGKY SDRSKDFRLL ISDNYFKDEE EPVMSSGRTV QGMANMAAVK
     GYIVAAAKAD HSNELALYVT QDTETWHHAQ FGDHKIEEDA YTILESTNYS IQVDVMTSKY
     VDMGNLYTSN SNGTHFTKNM EHTNRNEGGY VDFEKIANIQ GVVLVNTVDN WKQVEKSGQG
     KKLKSRISFD DGRSFEKLTV KGKKDAELHL HSVTNLHNSG RVFSSPAPGI VMGVGNTGDY
     LGKYTDGDLY VSDDAGLTWE LALEDAHKYE IGDQGSILVA VFDEGDTDEI RYSFKHGRKD
     TWKKIKLDYK IRARELTTLP DSTSLKFMLY ASKKKDGGGR EHVIIHLDFT DMLKKCGDSD
     FDDEWSVRKD ADGDPSCVMG HKQLFRRRKW DAECFVEEVF KDPTPNFKPC DCDEFRDYEC
     DFGFTPTGEG KDKKCEPNDS FKLPKGACEG DAKTYKASSG WRKIPGDQCK GETERDKQVE
     RECGDTERPP PKSDKITSEI TRFKGGEFLE QYYLEGNTQS DDDKDETVVM LTDERTAYIT
     HDHGKKWKKA VDDEVVRIYP HQYDNNRVYF LTAGKKFYYS TDRGRRDSIR SHEAPVMPNK
     ERLSIMQFHP KEESWIIWMG GKHCDKAGDK DCHTVAYVSQ KNGEDESWEP LVPYVKKCAF
     VWREAGRSVK EEQIFCEQHT NEEMGAPLEL ISSEDWFKKK DVKFKSVVEF ATMSEFIVVA
     TKADDGTLHL DASLDANTFA EAKFPPKFFD VHQTAYTVLD SSTHAVFLHV TVNPTRDQEY
     GSIIKSNSNG TSYVMSLAAV NRNMEGYVDF EKMQGLEGVA VANVIVNVDE VNKGSKKKKQ
     SRITHNDGAD WEPLQAPEKD SEGKAYECDV SDKYKCGLHI HGYTERADPR EMYSSPTAVG
     MMLAVGNVGS ELSTFGEANT FMTTDAGITW TEIKKGTYAW EFGDQGSVIV IVRRGEDTDH
     VYYSLDNGSK WNLYQFSDHK IRVEAITTVP SDTSLNFLLW GKDSKELVAV NLDFSGLPEF
     SKKCELNENN PTSGDYDLWI PQHPLQKEEP QCLFGHVAQY HRKKRDAKCK NGQRIDQMHD
     IARNCSCTRR DFECAYNYER DASGDCKLVA GLTLPEASAV CKDKNVKEYY TDVRFRRIPL
     STCEGGQEFD KTGDPHPCPG FEEDFQKKHG IGGFSLFLAI VLPFAAAGGV GYYVWKHWDG
     KFGRIRLGDG SGSGAFDSDA PWVKWPIAAV SGLVAVISAL PLLVGSVYRW AAGRMGGGGG
     YGGYGRTYTS RSSFARGRGD YAVVDPDEGE LLGDDSDEEV
//
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