VPS10_FUSV7
ID VPS10_FUSV7 Reviewed; 1516 AA.
AC C7YGZ0;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 25-MAY-2022, entry version 57.
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=NECHADRAFT_30652;
OS Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL
OS 45880 / 77-13-4) (Fusarium solani subsp. pisi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex; Fusarium vanettenii.
OX NCBI_TaxID=660122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4;
RX PubMed=19714214; DOI=10.1371/journal.pgen.1000618;
RA Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C.,
RA Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C.,
RA Freitag M., Ma L.-J., Danchin E.G.J., Henrissat B., Coutinho P.M.,
RA Nelson D.R., Straney D., Napoli C.A., Barker B.M., Gribskov M., Rep M.,
RA Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L.,
RA Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E.,
RA Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E.,
RA VanEtten H.D.;
RT "The genome of Nectria haematococca: contribution of supernumerary
RT chromosomes to gene expansion.";
RL PLoS Genet. 5:E1000618-E1000618(2009).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG698896; EEU48543.1; -; Genomic_DNA.
DR RefSeq; XP_003054256.1; XM_003054210.1.
DR AlphaFoldDB; C7YGZ0; -.
DR SMR; C7YGZ0; -.
DR STRING; 140110.NechaP30652; -.
DR EnsemblFungi; NechaT30652; NechaP30652; NechaG30652.
DR GeneID; 9676870; -.
DR KEGG; nhe:NECHADRAFT_30652; -.
DR eggNOG; KOG3511; Eukaryota.
DR HOGENOM; CLU_000700_0_0_1; -.
DR InParanoid; C7YGZ0; -.
DR OMA; ATMSEFI; -.
DR OrthoDB; 1046610at2759; -.
DR Proteomes; UP000005206; Unassembled WGS sequence.
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; -; 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 Pfam; PF15902; Sortilin-Vps10; 2.
DR Pfam; PF15901; Sortilin_C; 2.
DR SMART; SM00602; VPS10; 2.
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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1516
FT /note="Vacuolar protein sorting/targeting protein 10"
FT /id="PRO_0000407524"
FT TOPO_DOM 27..1390
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1391..1411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1412..1441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1442..1462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1463..1516
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REPEAT 108..118
FT /note="BNR 1"
FT REPEAT 390..400
FT /note="BNR 2"
FT REPEAT 451..461
FT /note="BNR 3"
FT REPEAT 495..504
FT /note="BNR 4"
FT REPEAT 756..766
FT /note="BNR 5"
FT REPEAT 798..807
FT /note="BNR 6"
FT REPEAT 852..861
FT /note="BNR 7"
FT REPEAT 1137..1147
FT /note="BNR 8"
FT REPEAT 1184..1193
FT /note="BNR 9"
FT REGION 642..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 917
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1007
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1516 AA; 169957 MW; 46590A2223D14059 CRC64;
MMRSVAWAAL SWRVFWLSLL WTAVSAKQDK PKIDSVMLEH PPLNLNYFED SDVIVFQDIE
ERNIYRSEDA GFTWNKVKEL PDGGSAFLYL HPFESSTAFV LTKDRKHYKT EDRGKSWTEF
DSGSMPSAFQ PDTLIFHAGD PKRIIFNGMN CDGIFCDEET TYTLDGFKTI QPLRPSTSGC
WWAKSNTEFT TGDEDLDKTR ILCIVTDPLS IFKTSQKLCV SDTFFKKENN GKYQEFEPTL
DSNRDVTGVV SLAAVKSFIL VASSSANSDE MALYVTSNAN QWHRAMFPSD DSHDHSHQIN
QEAYTVLEST NYSIQIDVMT SHPSRPMGVI FTSNSNGTYF TENIPYTNRN IKGHVDFEKI
SGIQGIFLVN TVENGKDVDE GSAEKVVVTQ ITFDDGRTFE PVKAGDQRIH LHSMTQINNI
GRIFSSPAPG LVMGNGNTGK SLGKFDDSNL YVSDDAGVTW KQALEGPHKY EFGDSGTILV
AVRDSAKEDV DKVSYSLNYG DTWESVPLPK DLKIRPALLT TTQDSTSLKF LLIGEHDKRY
HMVALDFEAL EKSTCGDKDM ESWNARVDDK GQATCIMGRK QTYKRRTKKA DCFIKSNFKD
PEPINEPCDC TDADFECDYN FQRDPEDRTV CKRVGSIPMP QGACKDKDDK FKGSSGWRMI
PGNQCKRTKG AQKDDEVERK CSEGGGGNSG GDGSSPSVPA NGEISHKKND FDSEALDMQK
YYLIRGDSSS GTDETIIARP IGERTGNSVQ VENKVWLTSD HGKSWKRILD QEDIMKIFHH
DYFKDVMFFS TKTDKILYTI DRGQTFHSFK TPVASDDFTL SFHPDKKDWL IWVGKHCDDV
SGSKSCFPAA SISTDRGDHW KTLVRYATKC EFTGNSAYKY RPLTQIVCLV HQEENLESPK
TIVTINDFLA DDKLIHNGTV ASFATMNEFI LATDEVTEAG KEKAGLQAIA SLDGQHFEAA
QFPYNFHDSH SSLYTVLDSS NHAVNLFVAT DLSDGRRRGS IIKSNSNGTT YVLSASNVNS
DEAGYVDFEK VAGLEGVTLI NVVANPDKKD GKKEIQTKIS HNDGAEWDFL PPPSKDVDGK
AYKCSSAGDS KCALHLHHYT ERDNKRRTFS ASKAIGLIFG VGNVGSTLGE MKDADTFMSA
DGGINWKNVK KGAWTWQYGD QGSIIVLAER ATHGNGAKTK TVSYSLDEGE TWNEYEFTDK
EVTILDLTSV KTGAARNFLV WCRSDSKQLF SVNIDFTGLT DKACEYKDDA SASDYELWSP
KHPLQKNDCF FGHVAKYLRK KKDRKCFNKA TLSLLHGYEN CECTRRDFEC AYNYELDNHG
QCSLVPGFQP LSGEEWCKQN PNETTWFEPT GYRRLPLTTC KDGVELDKTS DEHACEGYED
EFKRKHRTSG WVIFFAVVIP IGLAAAIGWY VWRNWSGKFG QIRLGDNSST FDSDQPWIKY
PVIAISAVAA VAAAMPLVII SLWRSATGVY ERVSNRSRGG NWSRRYTTRD SFARSDYSMV
DDDEGELLGE ESDEEV