ID   VPS10_LEPMJ             Reviewed;        1477 AA.
AC   E4ZVX1;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 2.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Vacuolar protein sorting/targeting protein 10;
DE   AltName: Full=Carboxypeptidase Y receptor;
DE            Short=CPY receptor;
DE   AltName: Full=Sortilin VPS10;
DE   AltName: Full=Vacuolar carboxypeptidase sorting receptor VPS10;
DE   Flags: Precursor;
GN   Name=VPS10; ORFNames=Lema_P028990.1;
OS   Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS   (Blackleg fungus) (Phoma lingam).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC   Leptosphaeria; Leptosphaeria maculans species complex.
OX   NCBI_TaxID=985895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8;
RX   PubMed=21326234; DOI=10.1038/ncomms1189;
RA   Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA   Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA   Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA   Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA   Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA   Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA   Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA   Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT   "Effector diversification within compartments of the Leptosphaeria maculans
RT   genome affected by Repeat-Induced Point mutations.";
RL   Nat. Commun. 2:202-202(2011).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Prevacuolar
CC       compartment membrane {ECO:0000250}; Multi-pass membrane protein
CC       {ECO:0000250}. Note=Cycles between the Golgi apparatus and the
CC       prevacuolar compartment. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the VPS10-related sortilin family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CBX95747.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; FP929127; CBX95747.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_003839226.1; XM_003839178.1.
DR   AlphaFoldDB; E4ZVX1; -.
DR   SMR; E4ZVX1; -.
DR   STRING; 985895.E4ZVX1; -.
DR   GeneID; 13288633; -.
DR   eggNOG; KOG3511; Eukaryota.
DR   InParanoid; E4ZVX1; -.
DR   OrthoDB; 1046610at2759; -.
DR   Proteomes; UP000002668; Genome.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 2.
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   Pfam; PF15902; Sortilin-Vps10; 2.
DR   Pfam; PF15901; Sortilin_C; 2.
DR   SMART; SM00602; VPS10; 2.
DR   SUPFAM; SSF50939; SSF50939; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Golgi apparatus; Membrane; Protein transport; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..1477
FT                   /note="Vacuolar protein sorting/targeting protein 10"
FT                   /id="PRO_0000407521"
FT   TOPO_DOM        22..1356
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1357..1377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1378..1405
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1406..1426
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1427..1477
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REPEAT          100..110
FT                   /note="BNR 1"
FT   REPEAT          367..377
FT                   /note="BNR 2"
FT   REPEAT          429..439
FT                   /note="BNR 3"
FT   REPEAT          723..734
FT                   /note="BNR 4"
FT   REPEAT          1106..1116
FT                   /note="BNR 5"
FT   REPEAT          1147..1157
FT                   /note="BNR 6"
FT   REGION          645..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1019..1050
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        647..667
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        288
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        974
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1018
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1477 AA;  167426 MW;  2DF22AD8055AF5FB CRC64;
     MKYLRGLLLP ALLALAPSIA AKKDEPLIET TAFKNDLINL MYFDDSGVAL VQEIENGNVW
     RSHDAGKGWS QIKDVSKVLR ITKSPYDNKA AIVLGEKKHW ITYDRGENWD SFETEFPPSP
     VAPVGWHASD NKKILVNEIE DCFLAPCLGR TYYTTDGFKS KPKVLVEDRR MCQWAKGSER
     FLEGEDKHDS RILCITRGKY SDRSKDFRLL ISDNFFKDSE EPKMSSGRTV QGMTNMAAVK
     GYIVVASKPD HSNELSLYTT QDTETWHHAQ FGDHKIEEDA YTILESTNYS IQVDVMTSKY
     VDMGNMYTSN SRGTYFTKNV EHTNRNQDGF VDFEKIANIQ GVVLVNTVDN WKEYEKSGQN
     KKLKSRISFD DGRSFEKLTV KGKDDELHLH SVTNLHNSGR VFSSPAPGIV MGVGNTGEHL
     GKYTDGDLYV SDDAGLTWEM ALSEAHKYEF GDQGSVLVAV FDEGDTDEIR YSFKHGRKDS
     WKKIKLDYKI RARELTTLPD ATSLKFMMYA SRKKEGGGRE HVIIHLDFAD MLPKCEDKDF
     DDKWSVRQET DGKPSCVMGH KQLFRRRKWD AECFIGDVFN DPVPTFEPCD CDEIRDYECD
     FGFDPSGEGK DKKCVPSDSR KLPEGACEGD AKTFKDKSGW RKIPGNQCKG ETDREKEVER
     PCGDAEKQPP KSNKITSELT KFKGGNFQEY YYLERNAQAD DDKPNDRDKD ETVVMLTDER
     TAWITHDHGK KWKKAVDDEI VRIYPHQYEN NYVYFLTATK KVYYSEDRGL HDSIHSFQAP
     TMPNTERLEI MRFHPNQKGW LIWMGGKNCE KVGDKDCHTV SYISQKNGQE ESWEPMVPYV
     KKCVFIWREA GRKVKEEQVF CEQYTNEEMG APLQLISSDD WFKKKEVKFK SVVEFATMAE
     FIVVATKADD GTLHLDATLD GSTFAEAKFP PKFFDVHQTA YTVLDSSTHA VFLHVTVNPQ
     RDQEYGSIIK SNSNGTSYVM SLSGVNRNTE GYVDFEKMQG LEGVAVANIV ANVDEVNNGT
     KKRKQSRITH NDGAAWEPLQ APEKDSEDQP YKCDVSDKEK CSLHIHGYTE RADPREMYSS
     PTAVGMMLAV GNVGSELTTF GEASTFMTID AGITWKEIKK GTYAWEFGDQ GAIIAIVRRG
     EDTDHIYYSL DYGEKWNLYK FSEHKIRVDA ITTVPSDTSL NFLLWGKDSK ELVAVNIDFS
     GLPDFKRKCE IDEDNPTAGD FDLWSPQHPL QDGDQDCLFG HVAQYHRKKR GAQCKTQQRI
     DHMHNIARNC TCTRRDYECA YNYERKPGGE CEKIPGLELA DPKEVCSKGA KEWWDPSPYR
     KIPLSTCQGK EMDQIGEVHA CPGFEEEFEK KHGLSGFGIF LAVVLPFLAA GGIGYYVWRN
     WDGKFGRIRL GENGGSFDSD AAWVKWPVAA VSGLVAVVTA IPLVMGSLWN FLASRMGGGY
     GGRTYTSRSS FARGRGDYAV VDPDEGELLG EESDEEV