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Database: UniProt
Entry: A0A1Z5SLI1_HORWE
LinkDB: A0A1Z5SLI1_HORWE
Original site: A0A1Z5SLI1_HORWE 
ID   A0A1Z5SLI1_HORWE        Unreviewed;      1453 AA.
AC   A0A1Z5SLI1;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=BTJ68_15575 {ECO:0000313|EMBL:OTA19079.1};
OS   Hortaea werneckii EXF-2000.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX   NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA19079.1, ECO:0000313|Proteomes:UP000194280};
RN   [1] {ECO:0000313|EMBL:OTA19079.1, ECO:0000313|Proteomes:UP000194280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA19079.1,
RC   ECO:0000313|Proteomes:UP000194280};
RA   Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA   Nislow C.E.;
RT   "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT   insights from long-read sequencing.";
RL   Submitted (JAN-2017) 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:OTA19079.1}.
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DR   EMBL; MUNK01000472; OTA19079.1; -; Genomic_DNA.
DR   STRING; 1157616.A0A1Z5SLI1; -.
DR   VEuPathDB; FungiDB:BTJ68_15575; -.
DR   InParanoid; A0A1Z5SLI1; -.
DR   OrthoDB; 5840at2759; -.
DR   Proteomes; UP000194280; 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; 2.120.10.10; -; 1.
DR   Gene3D; 3.30.60.270; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
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; 1.
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:UP000194280};
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:ARBA00022927}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1453
FT                   /note="Vacuolar protein sorting/targeting protein 10"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012757860"
FT   TRANSMEM        1318..1339
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1381..1402
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          46..677
FT                   /note="VPS10"
FT                   /evidence="ECO:0000259|SMART:SM00602"
FT   DOMAIN          680..1307
FT                   /note="VPS10"
FT                   /evidence="ECO:0000259|SMART:SM00602"
FT   REGION          1161..1182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1417..1453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1165..1182
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1453 AA;  163367 MW;  810F948E17FCBEBC CRC64;
     MHMSMARILG VLVALLALTV SAKKKDKPSV EETKFDSPQN LFYFEDSDVV LVTDTSERIA
     YRSEDAGVHW APLEDVKKGE VLEVINHPWN NQMAIVLGMN KKHWITRDQG KSWKAFELPE
     KPTLARPPIA FHATDSERLI VLTASCQSFE CKESAYYTLD GFDSKPKLLL DDAMSCLWAK
     STDLLQTDED DILCVVQGTF SPWSSDYKLL LSSDFFETDG VEPAMTEDGR PVSGIMNVAS
     VKSYLVAAAK SENTRELAMF VTADAKHWHR AEFGEHKLEE DAYTLLESTN YSMQVDVLTT
     KPSVPMGVLL TSNSNGTFFT KNIEHTNRNM HGFVDFEKIQ NIQGIVMVNT VDNWEDVEKK
     WLADKKIRTQ ISFDDGRTWQ PMKVDDKDLH LHSVTNQRNM GRIFSSPAPG IVMGVGNTGK
     HLKAYDEGDL FVSDDAGLTW MKALSRPHLY EFGDQGAILV AIEDEETDEI KWSLNHGKDW
     TTIELSDLDI KGKIKPTGLT TTPDSTSLKF LLSATKGKGS KLQHFVYSIN FEGLHEKQCK
     TDDFEQWYAR VDEDGEPSCI MGHTQMFRRR KADAECFVDE EFKDPVPKME DCKCKEVDFE
     CDYENNFTWD ADKEKLIPGN TCTKEGGEKL DEPVERDCDK APEESRPSGK IASEVTHFKG
     ERFAEYYYLE RCPDCSGTDE TVVMRTDRRD AWLSRDHGIK WEKIDTDGEE VVAIYPHQYL
     NDVVYLVTPS KTVFYSQNRG DKWHSFDAPE KPNQDHLQIL QFHPTQKDWL IWTGHAKDQT
     IAHVSTKGGD DWETLLRSVR KCQFVYREDR PESDQLIFCE QYESEDSAAP ISLFSSDDWF
     EHKKELKRDV INFATMAEYI VVASRDSDEK SLKVDTSIDG QMFADAKFPT NFKVPHQQAY
     TVLDSSTHAV FLHVTVNNQM DSEYGSIVKS NSNGTSYVLS VGEVNRNSPG YVDFEKMQGL
     EGVAVVNRVA NPKEADNGKM KKLKTYITHN DGADWALIPK PEKNVNGKNF KCKGGIEKCS
     LHLHGYTERK DPRDTFSSPS AVGLMIATGN VGQFLGAKKE AGTFATRDGG VTWTQIAEGN
     WMWEFGDQGS ILVIVKEDEP TDSVLYSLDE GVTWERFAFT ESSMQVEDIT TVPSDTSRRF
     LLWGKIKGEL ASVNLDFTGL EERSTPCESP DRPGAEGQSK DYDLWEPKHP LSDDNCLFGH
     VAQYHRKKLN ANCYNGREIQ HLHSIARNCT CTRRDFECDY NYEKQTDGSC ALVPGLSPPD
     PQDQCKNDGV DEYFDVTGYR RIPLTTCQGG QELDYTSRVS PCPGKEAEFE RKHGISGAGL
     FFAIVIPIAA AAGVGYWVWK NWDGKFGRIQ LGGDTPSMGL GGGGGYGGAF DRDAPWIKYP
     VMALSGVVAV VAALPMVANS LWRTISTRLG RNRAGGYSRP YTSRSSFSRG RGDYAVVDPD
     EGELLGEESD DEV
//
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