SORT1_DANRE
ID SORT1_DANRE Reviewed; 814 AA.
AC Q6NUT7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Sortilin;
DE Flags: Precursor;
GN Name=sort1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as a sorting receptor in the Golgi compartment and
CC as a clearance receptor on the cell surface. Required for protein
CC transport from the Golgi apparatus to the lysosomes by a pathway that
CC is independent of the mannose-6-phosphate receptor (M6PR). Lysosomal
CC proteins bind specifically to the receptor in the Golgi apparatus and
CC the resulting receptor-ligand complex is transported to an acidic
CC prelysosomal compartment where the low pH mediates the dissociation of
CC the complex. The receptor is then recycled back to the Golgi for
CC another round of trafficking through its binding to the retromer. Also
CC required for protein transport from the Golgi apparatus to the
CC endosomes. May also mediate transport from the endoplasmic reticulum to
CC the Golgi. {ECO:0000250|UniProtKB:Q99523}.
CC -!- SUBUNIT: Interacts with the cytosolic adapter proteins GGA1 and GGA2.
CC Interacts with the heterotrimeric retromer cargo-selective complex
CC (CSC), also described as vacuolar protein sorting subcomplex (VPS),
CC formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35; which is involved
CC in retrograde trafficking of the receptor from endosomes to the Golgi
CC apparatus (By similarity). {ECO:0000250|UniProtKB:Q99523}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q99523}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q99523}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q99523}. Nucleus membrane
CC {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q99523}. Cell membrane
CC {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q99523}; Extracellular side
CC {ECO:0000250|UniProtKB:Q99523}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q99523}.
CC -!- PTM: Palmitoylated. Undergoes cysteine S-palmitoylation which promotes
CC the partitioning of the receptor into an endosomal membrane subdomain
CC where it can interact with the retromer cargo-selective complex which
CC mediates its retrograde trafficking to the Golgi apparatus.
CC {ECO:0000250|UniProtKB:Q99523}.
CC -!- SIMILARITY: Belongs to the VPS10-related sortilin family. SORT1
CC subfamily. {ECO:0000305}.
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DR EMBL; BC068433; AAH68433.1; -; mRNA.
DR RefSeq; NP_998395.1; NM_213230.1.
DR AlphaFoldDB; Q6NUT7; -.
DR SMR; Q6NUT7; -.
DR STRING; 7955.ENSDARP00000121875; -.
DR PaxDb; Q6NUT7; -.
DR GeneID; 406511; -.
DR KEGG; dre:406511; -.
DR CTD; 406511; -.
DR ZFIN; ZDB-GENE-040426-2329; sort1a.
DR eggNOG; KOG3511; Eukaryota.
DR InParanoid; Q6NUT7; -.
DR OrthoDB; 1046610at2759; -.
DR PhylomeDB; Q6NUT7; -.
DR PRO; PR:Q6NUT7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0006895; P:Golgi to endosome transport; IBA:GO_Central.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0016050; P:vesicle organization; IBA:GO_Central.
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; 1.
DR Pfam; PF15901; Sortilin_C; 1.
DR SMART; SM00602; VPS10; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Endoplasmic reticulum; Endosome;
KW Glycoprotein; Golgi apparatus; Lipoprotein; Lysosome; Membrane; Nucleus;
KW Palmitate; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..814
FT /note="Sortilin"
FT /id="PRO_0000045159"
FT TOPO_DOM 19..741
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 742..762
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 763..814
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 129..140
FT /note="BNR 1"
FT REPEAT 181..192
FT /note="BNR 2"
FT REPEAT 223..234
FT /note="BNR 3"
FT REPEAT 269..280
FT /note="BNR 4"
FT REPEAT 310..321
FT /note="BNR 5"
FT REPEAT 359..370
FT /note="BNR 6"
FT REPEAT 410..421
FT /note="BNR 7"
FT REPEAT 488..499
FT /note="BNR 8"
FT REPEAT 531..542
FT /note="BNR 9"
FT MOTIF 771..776
FT /note="Endocytosis signal"
FT /evidence="ECO:0000255"
FT LIPID 767
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q99523"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 666
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 70..539
FT /evidence="ECO:0000250"
FT DISULFID 240..260
FT /evidence="ECO:0000250"
FT DISULFID 430..440
FT /evidence="ECO:0000250"
FT DISULFID 595..634
FT /evidence="ECO:0000250"
FT DISULFID 617..649
FT /evidence="ECO:0000250"
FT DISULFID 651..705
FT /evidence="ECO:0000250"
FT DISULFID 684..722
FT /evidence="ECO:0000250"
SQ SEQUENCE 814 AA; 90980 MW; E6B5259A80DB96B3 CRC64;
MSTVLCCVLV LLISVALCMD FEERPSSSWR SEQTMFLKSH KSRNLLSLRD LQQPDHGKMK
RSEESAQNQC ESLHGYQSTL QNDTHTHNFN DLSGSVSLAW VGDGTGVLLV LTTFQVPLFI
MRFGQSKLYR SEDYGKTFQD ITDLINNTFI QTEFGIAIGP DNSGKVILTG DLAEGKVTKI
FRSVDFGKSF VTSELPFHPL MQITYNPKDS NILMVYSINY DLWLSKDFGA NWKKIHESVC
LVKWGIDDTI FLTTNPNGSC SDRGTLELRK SLDYGKTFKT IGNRIYSFGL GGRFVFASIM
TDSGSTRMIH VSVDQGETWD MAQLPTVGHE QFYSILAANN DMVFMHVDEP GDSGIGTIYI
SDDRGIVFSK SLERHLYTTT GGDTDFTNIT SLRGVYITSV LAEDGSVQTV ITFNQGGEWR
PLMKPWNGVC DSTAKHPSEC SLHIHASYSI SMKLNVPMQP LSETNAVGLV LAHGSVGGAV
SVLSPDVYVS DDGGYTWFQA LKGPHHYAIL DSGGLLVAVE HNPTHPISQI KFSTDEGQCW
HAHNFTDDPI YFTGLASEPG ARSMNVSLWG YRDTILNQYW VSVTVDFRQL LSRDCQENDY
IQWLAHSSDI NSPTDGCVLG YKERFLRLRR DSVCWNGRDY KVTKEPTTCP CTLTDFHDFG
FYHEENSSVC VEQPDLIGHS LEFCLHGRKE QLQTSGYRKI PGDHCEEGIT PERKEIDLSK
KCVSNLLRTE QLTKEHSFNS APIIAVVIIV LLISAVAGVI FIKKYVCGGR FLVHRYSVLQ
QHAEANGIDG LDDLDTLEGG KTHYHDDSDE DLLE
