ID A0A1U7QMW1_MESAU Unreviewed; 2214 AA.
AC A0A1U7QMW1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Sortilin-related receptor {ECO:0000256|ARBA:ARBA00013467};
DE AltName: Full=Low-density lipoprotein receptor relative with 11 ligand-binding repeats {ECO:0000256|ARBA:ARBA00029896};
DE AltName: Full=Sorting protein-related receptor containing LDLR class A repeats {ECO:0000256|ARBA:ARBA00032450};
GN Name=Sorl1 {ECO:0000313|RefSeq:XP_005069459.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005069459.1};
RN [1] {ECO:0000313|RefSeq:XP_005069459.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004212}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004212}. Early endosome membrane
CC {ECO:0000256|ARBA:ARBA00004158}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004158}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004115}. Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004530}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004530}. Endosome, multivesicular body membrane
CC {ECO:0000256|ARBA:ARBA00004545}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004545}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004614}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004614}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000256|ARBA:ARBA00004393}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004393}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}. Recycling endosome membrane
CC {ECO:0000256|ARBA:ARBA00004480}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004480}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the VPS10-related sortilin family. SORL1
CC subfamily. {ECO:0000256|ARBA:ARBA00007041}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR RefSeq; XP_005069459.1; XM_005069402.3.
DR STRING; 10036.ENSMAUP00000014440; -.
DR GeneID; 101823721; -.
DR KEGG; maua:101823721; -.
DR CTD; 6653; -.
DR eggNOG; KOG1215; Eukaryota.
DR eggNOG; KOG3511; Eukaryota.
DR OrthoDB; 5840at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0031985; C:Golgi cisterna; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005641; C:nuclear envelope lumen; IEA:Ensembl.
DR GO; GO:0097356; C:perinucleolar compartment; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; IEA:Ensembl.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IEA:Ensembl.
DR GO; GO:0042923; F:neuropeptide binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:Ensembl.
DR GO; GO:0002024; P:diet induced thermogenesis; IEA:Ensembl.
DR GO; GO:0099638; P:endosome to plasma membrane protein transport; IEA:Ensembl.
DR GO; GO:0038020; P:insulin receptor recycling; IEA:Ensembl.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; IEA:Ensembl.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IEA:Ensembl.
DR GO; GO:1902997; P:negative regulation of neurofibrillary tangle assembly; IEA:Ensembl.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IEA:Ensembl.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0010897; P:negative regulation of triglyceride catabolic process; IEA:Ensembl.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:Ensembl.
DR GO; GO:1904179; P:positive regulation of adipose tissue development; IEA:Ensembl.
DR GO; GO:1902955; P:positive regulation of early endosome to recycling endosome transport; IEA:Ensembl.
DR GO; GO:2001137; P:positive regulation of endocytic recycling; IEA:Ensembl.
DR GO; GO:1902953; P:positive regulation of ER to Golgi vesicle-mediated transport; IEA:Ensembl.
DR GO; GO:1900168; P:positive regulation of glial cell-derived neurotrophic factor production; IEA:Ensembl.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; IEA:Ensembl.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IEA:Ensembl.
DR GO; GO:0051604; P:protein maturation; IEA:Ensembl.
DR GO; GO:0045053; P:protein retention in Golgi apparatus; IEA:Ensembl.
DR GO; GO:0006622; P:protein targeting to lysosome; IEA:Ensembl.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:Ensembl.
DR GO; GO:0014910; P:regulation of smooth muscle cell migration; IEA:Ensembl.
DR CDD; cd00063; FN3; 5.
DR CDD; cd00112; LDLa; 11.
DR Gene3D; 2.10.70.80; -; 1.
DR Gene3D; 3.30.60.270; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 11.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
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:SF20; SORTILIN-RELATED RECEPTOR; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF00057; Ldl_recept_a; 10.
DR Pfam; PF00058; Ldl_recept_b; 2.
DR Pfam; PF15902; Sortilin-Vps10; 1.
DR Pfam; PF15901; Sortilin_C; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00060; FN3; 6.
DR SMART; SM00192; LDLa; 11.
DR SMART; SM00135; LY; 5.
DR SMART; SM00602; VPS10; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 3.
DR SUPFAM; SSF57424; LDL receptor-like module; 11.
DR SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 1.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS01209; LDLRA_1; 4.
DR PROSITE; PS50068; LDLRA_2; 11.
DR PROSITE; PS51120; LDLRB; 4.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170,
KW ECO:0000313|RefSeq:XP_005069459.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..2214
FT /note="Sortilin-related receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010528127"
FT TRANSMEM 2136..2159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 800..843
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 844..887
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 888..929
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 931..972
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 1557..1649
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1653..1745
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1747..1844
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1934..2029
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 62..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1078..1090
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1085..1103
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1097..1112
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1138..1153
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1158..1170
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1165..1183
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1177..1192
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1199..1211
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1206..1224
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1244..1262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1256..1271
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1325..1337
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1332..1350
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1344..1359
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1376..1394
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1388..1403
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1419..1431
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1426..1444
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1438..1453
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1491..1506
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1534..1549
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 2214 AA; 247502 MW; C093D20FE0A17BD5 CRC64;
MATRSSRRES RLPFLFALVA LLPPGALGGG WTKRLYGGRT PLPQDWGFFV VQGDLQELRL
GTHGDARGAS PAAGKPLRTR RSATVQPQPI QVYGQVSLND SHNQMVVHWA GEKSNVIVAL
ARDSLALARP KSSDVYVSYD YGKSFNRISG KLNFGVGNNS EAVISQFYHS PADNKRYIFV
DAYAQYLWIT FDFCSTIHGF SIPFRAADLL LHSKASNLLL GFDRSHPNKQ LWKSDDFGQT
WIMIQEHVKS FSWGIDPYDQ PNTIYIERHE PFGFSTVFRS TDFFQSRENQ EVILEEVRDF
QLRDKYMFAT KVVHLPGSQQ QSSVQLWVSF GRKPMRAAQF VTKHPINEYY IADASEDQVF
VCVSHSNNST NLYISEAEGL EFSLSLENVL YYSPGGVGSD TLVRYFANEP FADFHRVEGL
QGVYIATLMN GSMNEENMRS VITFDKGGTW EFLQAPAFTG YGEKINCELS QGCSLHLAQR
LSQLLNLQLR RMPILSKESA PGLIIATGSV GKNLASKTNV YISSSAGARW REALPGPHYY
TWGDHGGIIM AIAQGMETNE LKYSTNEGET WKTFVFSEKP VFVYGLLTEP GEKSTVFTIF
GSNKENVHSW LILQVNATDA LGVPCTENDY KLWSPSDERG NECLLGHKTV FKRRTPHATC
FNGEDFDRPV VVSNCSCTRE DYECDFGFKL SEDLSLEVCV PDPEFSGKPY SPPMPCPVGS
TYRRTRGYRK ISGDTCSGGD VEARLEGELV PCPLAEENEF ILYAVRKSIY RYDLASGATE
QLPLSGLRAA VALDFDYERN CLYWSDLALD TIQRLCLNGS TGQEVIINSG LETVEALAFE
PLSQLLYWVD AGFKKIEVAN PDGDFRLTII NSSVLDRPRA LVLVPQEGVM FWTDWGDLKP
GIYRSNMDGS AAYPLVSEDV KWPNGISVDS QWLYWTDAYL DCIERITLSG QQRSVILDNL
PHPYAIAVFK NEIYWDDWSQ LSIFRASKYS GSRMEILASQ LTGLMDMKIF YKGKNAGSNA
CLPQPCSLLC LPKANNSKSC RCPEGVASSV LSTGDLMCDC PQGFQRKNNT CVKEENTCLR
NQYRCSNGNC INSIWWCDFD NDCGDMSDER NCPTTVCDAD TQFRCQESGT CIPLSYKCDL
EDDCGDNSDE SHCEMHQCRS DEFNCSSGMC IRSSWVCDGD NDCRDWSDEA NCTAIYHTCE
ASNFQCHNGH CIPQRWACDG DADCQDGSDE DPVSCEKKCN GFHCPNGTCI PSSKHCDGLR
DCPDGSDEQH CEPFCTRFMD FVCKNRQQCL FHSMVCDGIV QCRDGSDEDA AFAGCSQDPE
FHKECDEFGF QCQNGVCISL IWKCDGMDDC GDYSDEANCE NPTEAPNCSR YFQFRCENGH
CIPNRWKCDR ENDCGDWSDE KDCGESHVFP SPTPGPSTCL PNYFRCSSGA CVMDTWVCDG
YRDCADGSDE EACPSLANTT AASTPAQRGR CDRFEFECHQ PKKCIPNWKR CDGHQDCQDG
QDEANCPTHS TLTCMSREFK CEDGEACIVL SERCDGFLDC SDESDEKACS DELTVYKVQN
LQWTADFSGD VTLTWMRPKK MPSASCVYNV YYRVVGESIW KTLETHSNKT STVLKVLKPD
TTYHVKVQVH CLSKVHNTND FVTLRTPEGL PDAPRNLQLS LNNEEEGVII GHWAPPIHTH
GLIREYIVEY SRSGSKMWAS QRAASNSTEI KNLLLNALYT IRVAAVTSRG IGNWSDSKSI
TTIKGKVIQA PNVHIDSYDE NSLSFTLTMD GDIKVNGYVV NLFWSFDAHK QEKKTLNFQG
SSVSHKVSNL TAHTSYEISA WAKTDLGDSP LAFEHVLTRG IRPPAPSLKA KAINQTAVEC
TWTGPKNVVY GIFYATSFLD LYRNPRSLTT SLHNKTVIVS KDEQYLFLVR VLIPYQGPSS
DYVVVKMIPD SRLPPRHLHA VQIGKTSAII KWESPYDSPD QDLFYAIAVK DLIRKTDRSY
KVKSRNSTVE YSLNKLEPGG KYHVVVQLGN MSKESSIKIT TVSLSAPDAL KIITENDHVL
LFWKSLALKE KQFSETRGYE IHMFDSAMNL TAYLGNTTDN FFKVSNLKLG HNYTFTVQAR
CLFGSQICGE PAVLLYDELS SGGDTTAVQT ARSTDVAAVV VPILFLILLS LGVGFAILYT
KHRRLQSSFT AFANSHYSSR LGSAIFSSGD DLGEDDEDAP MITGFSDDVP MVIA
//
