ID A0A2Y9K7C8_ENHLU Unreviewed; 2211 AA.
AC A0A2Y9K7C8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=LOC111153957 {ECO:0000313|RefSeq:XP_022369018.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022369018.1};
RN [1] {ECO:0000313|RefSeq:XP_022369018.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022369018.1};
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_022369018.1; XM_022513310.1.
DR Proteomes; UP000248482; Unplaced.
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:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
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; 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; 11.
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; 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; 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_022369018.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
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_5016170614"
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..926
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 928..969
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; 247633 MW; 5469CA749EBBBC8A CRC64;
MATRSSRRES RLPFLFTLVA LLPPGALCEV WTQTLPGGRT PLPQNRGFRV VQGEPRELRL
WARGGPRGAD EKPLRRRRSA ALQPEPIKVY GQVSLNDSHN QMVVHWAGEK SNVIVALARD
SLALARPRSS DVYVSYDYGK SFKRISEKLS FGVGNSSEAV IAQFYHSPAD NKRYIFADAY
AQYLWITFDF CNTIHGFSIP FRAADLLLHS KASNLLLGFD RSHPNKQLWK SDDFGQTWIL
IQEHVKSFSW GIDPYDKPNT IYVERHEPSG YSTVFRSTDF FQSRENQEVI LEEVKDFQLR
DKYMFATKVV HLRGSLYPSS VQLWVSCGRK PMRPAQFVTR HPINEYYIAD ASEDQVFVCV
SHSNNRTNLY ISEAEGLKFS LSLENVLYYS PGGAGGDTLV RYFANEPFAD FHRVEGLQGV
YIATLINGSM NEENMRSVIT FDKGGTWEFL QAPAFTEYGE KINCELAQGC SLHLAQRLSQ
LLNLQLRRMP ILSKESAPGL IIATGSVGKN LASKTNVYVS SSAGARWREA LPGPHYYTWG
DHGGIIMAIA QGMETNELKY STNEGETWKT FIFSERPVFV YGLLTEPGEK STVFTIFGSN
KESAHSWLIL QVNATNALGV PCTENDYKLW SPSDERGNEC LLGHKTVFKR RTPHATCFNG
EDFDRPVVVS NCSCTREDYE CDFGFKMSED LSLEVCVPDP EFSGKSYSPP VPCPVGSTYR
RTRGYRKISG DTCSGGDVET RLEGELVPCP LAEENEFILY AMRKSIHRYD LASGATEQLP
LTGLRAAVAL DFDYERNCLY WSDLALDTIQ RLCLNGNTGQ EVIINSGLET VEALAFEPLS
QLLYWVDSGF KKIEVANPDG DFRLTIVNAS VLDRPRALVL LPQDGVMFWT DWGDLKPGIY
RSNMDGSAVH RLVSEDVKWP NGISVDDQWV YWTDAYLDCI ERITFDGQQR SIILDNLPHP
YAIAVFKNEI YWDDWSQLSI FRASKYSGSQ MAVLASQLTG LMDMKIFYKG KTTGSNACVS
RPCSLLCLPK ANNSKSCRCP EGVASSVLPS GDLMCECPQG YQRENDTCLK EENTCLRNQY
RCSNGNCINS IWWCDFDNDC GDMSDERNCP TTVCDLDTQF RCQESGTCIP LSYKCDLEDD
CGDNSDESHC EMHQCQSDEY SCSSGMCIRS SWVCDGDNDC RDWSDEANCT AIYHTCEASN
FQCHNGHCIP QRWACDGDMD CQDGSDEDPV NCEKKCNGFR CPNGTCIPSS KHCDGLRDCS
DGADEQHCEP LCTRFMDFVC KNRQQCLFHS MVCDGIVQCR DGSDEDAAFA GCSQDPEFHK
VCDEFSFQCQ NGVCISLIWK CDGMDDCGDY SDEASCENPT EAPNCSRYFQ FQCENGHCIP
NRWKCDREND CGDWSDERDC GDSHILPSPT PGPSTCLPNY YRCSSGACVM DSWVCDGYRD
CADGSDEEAC PSPANVTAAS VPTHHGHCDR FEFECRQPKK CIPNWKRCDG HQDCQDGQDE
ANCPTHSTLT CMSREFKCED GEACIVLSER CDGFLDCSDE SDERACSDEL TVYKVQNLQW
TADFSGDVTL TWTRPKKMPS AACVYNIYYR MVGEGIWKTV ETHSNKTNTI LKVLKPDTTY
QVKVQVQCLS KVHNTNDFVT LRTPEGLPDA PQNLQLSLHR EEEGVIVAHW IPPTHSHGLI
REYIVEYSRS GSKMWASQRA ASNFTEIKNL LVNAPYTVRV AAVTSRGVGN WSGSKSITTV
KGKVIPPPDI HIDSYGENFL SFTLTMENDI KVNGYVVNLF WAFDTHKQEK RTLNFRGSIL
SHKVANLTAH TSYEISAWAK TDLGDSPLAF EHVTTKGVRP PAPSLKAKAI NQTAVECTWT
GPRNVVYGIF YATSFLDLYR SPQSLTTSLH NKTIIVSRDE QYLFLVRVVV PYQGPSSDYV
VVKMIPDSRL PPRHLHVVHT GKTSAVIKWE SPYDSPDQDL LYAVAVKDLI RKSDRSYKIK
SHNSTVEYTL TKLEPGGKYH IIVQLGNMSK DSSIKITTVS LSAPDALKII TENDHVLLFW
KSLALKEKHF NESRGYEIHM FDSAMNISAY LGNTTDNFFK ISNLKLGHNY TFTVQARCLF
GSQICGEPAV LLYDELGSSG GASASQATRS TDVAAVAVPI LFLVLLSLGV GFAVLYTKHR
RLQSSFTAFA NSHYSSRLGS AIFSSGDDLG EDDEDAPMIT GFSDDVPMVI A
//
