VPS10_CHAGB
ID VPS10_CHAGB Reviewed; 1526 AA.
AC Q2HAB1;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 62.
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=CHGG_02843;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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}.
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DR EMBL; CH408030; EAQ90908.1; -; Genomic_DNA.
DR RefSeq; XP_001229359.1; XM_001229358.1.
DR AlphaFoldDB; Q2HAB1; -.
DR SMR; Q2HAB1; -.
DR STRING; 38033.XP_001229359.1; -.
DR PRIDE; Q2HAB1; -.
DR EnsemblFungi; EAQ90908; EAQ90908; CHGG_02843.
DR GeneID; 4389580; -.
DR eggNOG; KOG3511; Eukaryota.
DR HOGENOM; CLU_000700_0_0_1; -.
DR InParanoid; Q2HAB1; -.
DR OMA; ATMSEFI; -.
DR OrthoDB; 1046610at2759; -.
DR Proteomes; UP000001056; 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; -; 2.
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1526
FT /note="Vacuolar protein sorting/targeting protein 10"
FT /id="PRO_0000407512"
FT TOPO_DOM 25..1385
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1386..1406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1407..1437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1438..1458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1459..1526
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REPEAT 64..74
FT /note="BNR 1"
FT REPEAT 107..118
FT /note="BNR 2"
FT REPEAT 453..463
FT /note="BNR 3"
FT REPEAT 497..507
FT /note="BNR 4"
FT REPEAT 793..803
FT /note="BNR 5"
FT REPEAT 847..856
FT /note="BNR 6"
FT REPEAT 1134..1144
FT /note="BNR 7"
FT REPEAT 1180..1189
FT /note="BNR 8"
FT REGION 1470..1498
FT /note="Disordered"
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 938
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1003
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1526 AA; 170724 MW; 1BDC04340A328FC4 CRC64;
MRVRGALQAA AVLATALWAT PLAAKKNDRP TFHTKAFENA PRSLNYFPDS DTVLFQDQSA
NNVYLSSDHG VKWERVDAVP EGKAWMLSMH GFDSNRAYIL TEGTTHFRTS DRGKTWEKFK
SGIQLSLFRP DILRFHANDP DRILFNGMIC EGLDCQEVAQ YTTDGFKTPA KELRRNTDGC
WWAKSSDLFT TGAEDLDNNR VLCVVRDSFS PFKQDQRLLI SDNFFRTSDD SSDIQEFEPD
LDMNKPVQGV VSIAVVKKYL LVATTSMNTD EMALFITGDT KKWHRAVFPA NHEGHDHRVL
QEAYTALEST NYSIQIDVMT TRPSNPMGVM FTSNSNGTYF TENVPHTNRN ERGHVDFEKV
TGIQGVFLVN KVDNWEDVAK KASTKKKVVS EITFDDGRTF EPVTAGDKRI HLHSVTELSN
VGPVFSSPAP GLLMAIGNRG DYLKNYWDDG NLYVSDDAGM TWNKALDGPH KYEFGDQGSI
LVAVRDSKEV DVSEISYSLD HGLTWTKQAL PDDLKIRPYI LTTTQESASL KFLLIGMVKE
SPSWQVISID FDGLHEATCK EDDMEEWFAR VDKDGKPTCL MGHTQSFPRR KKKAECFLKQ
EFKHPVSKTE NCECTDKDYE CDFNFAREDG KCVAKGPIIP PEGVCRDAKP DDTFKGTSGY
RKILGNTCKE TKEMDDKYKD VERKCSEIGG GGGGKPSTPA TDKIEQIENV FDKDWDRWEK
HYLERGESSS SEGETIIMRG RTKSKLGPIY VTENHGKEWH VPKYLKEEEI VHIVPHQYFK
DMVFFITTGK KIIYTTDRGR TYHSFKAPNE PSDDVMPLSF HPDKKNWLIW NGKKCESSDD
CFGVVSYSKD GGDHWQTGGS IYTRRCEFTG SRAYKYPGRK EEQILCLKHE KESKAKDNPM
VLISTNDWFD NEEIRQKNVR EFATMAEFVV VATENSANKT LQASASLDGA TFADALFPHG
FVVPHQHIYT VLDSSTHAVN LFVATSMDGN LCNYGSILKS NSNGTSYVVS VGNVNCDEDS
YVDFDKIAGL EGVALVNVVA NPDAESSAPK RLQTKITHND GAQWAYLSTP PNDDIGKFPC
QSSGDEKCAL HLHGYTERRL RGNTWYSSES AVGIMVAWGN VGDSLGPRKD SDTFMTTDAG
LTWKRVKQGQ WTWAIGDQGG IIVLIQTTSV SRKKTKSLVY SLDQGKTWKE HEFASDEVEV
WDVTTLRSGS SQNFLLWGKG SKGPFTLKLD FSGFSEDVCK VDDDPDKSDY YLWSPKHPMQ
PDGCLFGHVS QYLRKKSDRK CYNDFKLQPL YGKEDCKCTR EDFECDYNYQ LDPFGQCSLV
PGLEPADPSA WCKQHPDEIE YHEPTGYRRI PLTTCVGGRQ PDKESPVHAC AGHEEDFERK
HAVSGLALFF AITVPFALAG AAGWYVWRNW NGKFGQIRLG DQGAAVFEAD RPWVRYPVIV
LSAVAAVVVA LPVVVGAVWR SVSGLLGGRG GAGGGDGRGR WSRLGGGGGG GGRRFTTRDS
FARGGDYAVV DDDEGELLGE DSDEEV
