ID A0A452FGN5_CAPHI Unreviewed; 2211 AA.
AC A0A452FGN5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 28.
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|Ensembl:ENSCHIP00000023441.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000023441.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000023441.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000023441.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 EMBL; LWLT01000015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_017915129.1; XM_018059640.1.
DR STRING; 9925.ENSCHIP00000023288; -.
DR Ensembl; ENSCHIT00000031148.1; ENSCHIP00000023288.1; ENSCHIG00000020653.1.
DR Ensembl; ENSCHIT00000031301.1; ENSCHIP00000023441.1; ENSCHIG00000020653.1.
DR GeneID; 102187336; -.
DR CTD; 6653; -.
DR GeneTree; ENSGT01030000234563; -.
DR OMA; LCPDGME; -.
DR OrthoDB; 5840at2759; -.
DR Proteomes; UP000291000; Chromosome 15.
DR Bgee; ENSCHIG00000020653; Expressed in ileum and 17 other cell types or tissues.
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; 10.
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; 4.
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; 2.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS01209; LDLRA_1; 5.
DR PROSITE; PS50068; LDLRA_2; 11.
DR PROSITE; PS51120; LDLRB; 3.
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 Reference proteome {ECO:0000313|Proteomes:UP000291000};
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..2211
FT /note="Sortilin-related receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040596373"
FT TRANSMEM 2133..2156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 797..840
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 841..884
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 885..929
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 1554..1646
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1650..1742
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1746..1841
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1931..2026
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DISULFID 1075..1087
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1082..1100
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1094..1109
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1135..1150
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1155..1167
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1162..1180
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1174..1189
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1196..1208
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1203..1221
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1241..1259
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1253..1268
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1322..1334
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1329..1347
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1341..1356
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1373..1391
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1385..1400
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1416..1428
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1423..1441
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1435..1450
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1488..1503
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1531..1546
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 2211 AA; 247750 MW; 92F4966FA94762D5 CRC64;
MATRSSRRES RLPFLFVLIA LLPPGAVGQI WPQTLPGGRA PGPQDRGFLV VRGDPFELRL
GARGAPRGAD EKPLRRRRSA ALQQEPIQVY GQVSLNDSHN QMVVHWAGEK SNVIVALARD
SLALAKPKSS DVYVSYDYGR SFKRISEKLN FGEGNSSEAV IAQFYHSPAD NKRYIFTDAY
AQYLWTTFDF CNTIQGFSIP FRAADLLLHS KASNLLLGFD RSHPNKQLWK SDDFGQTWIM
IQEHVKSVSW GIDPYDKPNT IYVERHEPSG YSTVFRSTDF FQSRENLEVI LEEVRDFQLR
DKYMFATKVV HLFGSPQPSS VQLWVSFGRK PMRAAQFVTR HPINEYYIAD ASEDQVFVCV
SHSNNRTNLY ISEADGLKFS LSLENVLYYS PAGAGSDTLV RYFANEPFAD FHRVEGLQGV
YIATLISGSM NEENMRSVIT FDKGGTWEFL QAPAFTEYGE KINCELSQGC SLHLAQRLSQ
LLSLQLRRMP ILSKESAPGL IIATGSVGKN LASKTNVYIS SSAGARWREA LPGPHYYTWG
DHGGIIMAIA QGMETNELKY STNEGETWKT FIFSEKPVFV YGLLTEPGEK STVFTIFGSN
KENIHSWLIL QVNATNALGV PCTENDYKLW SPSDERGNEC LLGHKTVFKR RTPHATCFNG
EDFDRPVVVS NCSCTREDYE CDFGFKMSED LSLEVCVPDP EFSGNSYAPP VPCPVGSTYR
RTRGYRKISG DTCSGGDVEM RLEGELVPCP LAEENEFILY AMRKSIHRYD LASGATEQLP
LTGLRSAVAL DFDYERNCLY WSDLALDVIQ RLCLNGSTGQ EVIISSGLET VEALAFEPLS
QLLYWVDSGF KKIEVGHPDG DFRLTIVNSS VLDRPRALVL VPQDGVMFWT DWGDLRPGIY
RSNMDGSAAY RLVSEDVKWP NGIAVDEQWI YWTDAYLDCI ERITFSGQQR SVILDNLPHP
YAIAVFKNEI YWDDWSQLSI FRASKYSGSD MAILASRLTG PMDLKIFYRG KTTGSNACAS
RPCSLLCLPK ADGSRSCRCP DGVSSSVLPS GDLMCECPHG YQQKNRTCVK EEDTCLRNQY
RCSNGKCINS IWWCDFDNDC GDMSDERNCP TTVCDLDTQF RCHESGTCIP LSYKCDLEDD
CGDNSDESHC EMHQCRSDEY GCSSGMCIRS SWVCDGDNDC RDWSDEANCT AIYHTCEASN
FQCRNGHCIP QRWACDGDMD CQDGSDEDPV NCEKKCNGFR CPNGTCIPSS KHCDGLHDCS
DGSDEQHCEP LCTRFMDFVC KNRQQCLFQS MVCDGIIQCR DGSDEDPEFA GCSRDPEFHK
VCDEFSFQCQ NGVCISLIWK CDGMDDCGDD SDEANCENPT EAPSCSRYFQ FRCENGRCIP
SRWKCDREND CGDWSDEKDC GDSHVLPSPT PGPSTCLPNY YRCSSGACVM DSWVCDGYRD
CMDGSDEEAC PSPANVTAAS TPTQLGRCDR FEFECRQPKK CIPNWRRCDG HQDCQDGQDE
ANCPTHSTLT CTALEFQCQD GEACIMLSER CDGFLDCSDE SDELACSEEL NVYKIQNLQW
TADFSGDVTL TWIRPKKMPS ASCVYNIYYR VVGESIWNTL ETHSNKTSTV LKVLKPDTTY
QVKVQVQCLS KVHSTNDVVT LRTPEGLPDA PQNLQLLLHR EVEGVIMGHW APPVHTHGLI
REYIVEYSRS GSKTWASQRA LSNFTEIRNL LVNTQYTVRV AAVTSRGIGN WSDSKSITTI
KGQVIPPPDI RIDSFGENFL SFTLSMDTDI KVNGYVVTLF WSFDAHRQEK RTLNFRGTVL
SQKVGNLTAH TPYEISAWAK TDLGDSPLAF KRVTTRGVRP PAPSLKAKAI NQTAVECTWT
GPRNVVYGIF YATSFLDLYR NPKSLTTSQH NRTVLVSGDE QYLFLVRVVV PYQGPSSDYV
VVRMIPDSRL PPRHLHVVCM GKTSAVIKWE SPYDSPDQDL LYAIAVKDLI RKSERSYKVK
SRNSTVEYTL NKLEPGGKYH IIVQLGNMSK DSSIKITTVS LLAPDALKII TENDHVLLFW
KSLALKEKYF NESRGYEIHM FDSVMNISAY LGNTTDNFFK ISNLKLGHNY TFTVQARCLF
GSQICGEPAV LLYDELGSGG DASVIQAARS TDVAAVVVPI LFLILLSLGV GFAILYTKHR
RLQSSFTAFA NSHYSSRLGS AIFSSGDDLG EDDEDAPMIT GFSDDVPMVI A
//
