ID A0A286ZJ24_PIG Unreviewed; 2143 AA.
AC A0A286ZJ24;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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:ENSSSCP00000031576.1,
GN ECO:0000313|VGNC:VGNC:108617};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000031576.1, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000031576.1, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000031576.1,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000031576.1}
RP IDENTIFICATION.
RG Ensembl;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSSSCT00000065854.3; ENSSSCP00000031576.1; ENSSSCG00000015135.5.
DR VGNC; VGNC:108617; SORL1.
DR GeneTree; ENSGT01030000234563; -.
DR Proteomes; UP000008227; Chromosome 9.
DR Bgee; ENSSSCG00000015135; Expressed in omentum and 41 other cell types or tissues.
DR ExpressionAtlas; A0A286ZJ24; baseline and differential.
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; 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; 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; 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; 6.
DR PROSITE; PS50068; LDLRA_2; 11.
DR PROSITE; PS51120; LDLRB; 3.
PE 1: Evidence at protein level;
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};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A286ZJ24};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..2143
FT /note="Sortilin-related receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013307375"
FT REPEAT 798..841
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 842..885
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 886..930
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 1555..1647
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1651..1743
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1748..1843
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1933..2028
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DISULFID 1076..1088
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1083..1101
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1095..1110
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1136..1151
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1156..1168
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1163..1181
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1175..1190
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1197..1209
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1204..1222
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1242..1260
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1254..1269
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1323..1335
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1330..1348
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1342..1357
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1374..1392
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1386..1401
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1417..1429
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1424..1442
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1436..1451
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1489..1504
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1532..1547
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 2143 AA; 240628 MW; 62DC1323CA007BA9 CRC64;
MATRSSRRES RLPFLFILMA LLPPGAVGEV WPYTLPGGRA PGPQDRGFLV VRGDPRELRL
GAHGAPRGAD EKPLRRKRSA ALQPEPIQVY GQVSLNDSHN QMVVHWAGEK SNVIVALARD
SLSLARPRSS DVYVSYDYGR SFKRISEKLN FGTGNSSEAV IAQFYHSPAD NKRYIFADAY
AQYLWTTFDF CNTIQGFSIP FRAADLLLHS KASNLLLGFD RSHPNKQLWK SDDFGQTWIM
IQEHVKSFSW GVDPYDKPNT IYVERHEPSG YSTVFRSTDF FQSRENLEVI LEEVRDFQLR
DKYMFATKVV QHLFGSQQPS SVQLWVSFGR KPMRAAQFVT RHPINEYYIA DASEDQVFVC
VSHSNNRTNL YISEAEGLKF SLSLENVLYY SPGGAGSDTL VRYFANEPFA DFHRVEGLQG
VYIATLINGS MNEENMRSVI TFDKGGTWEF LQAPAFTEYG EKINCELSQG CSLHLAQRLS
QLLSLQLRRT PILSKESAPG LIIATGSVGK NLASKTNVYV SSSAGARWRE ALPGPHYYTW
GDHGGIIVAI AQGMETNELK YSTNEGETWK TFVFSEKPMF VYGLLTEPGE KSTVFTIFGS
NKENIHSWLI LQVNTTDALG VPCTENDYKL WSPSDERGNE CLLGHKTVFK RRTPHATCFN
GEDFDRPVVV SNCSCTREDY ECDFGFKMSE DLFLEVCVPD PEFSGKSFSP PVPCPVGSTY
RRTRGYRKIS GDTCSGGDVE VRLEGELVPC PLAEENEFIL YAMRKSIHRY DLASGTTEQL
PLTGLRAAVA LDFDYEHNCL YWSDLALDII QRLCLNGNTG QEVIINSGLE TVEALAFEPL
SQLLYWVDSG FKKIEVGNPD GDFRLTIVNS SVLDRPRALV LVPQDGVMFW TDWGDLRPGI
YRSNMDGSAA YRLVSEDVKW PNGIAVDAQW VYWTDAYLDC IERVTFSGQQ RSIILDNLPH
PYAIAVFKNE IYWDDWSELS IFRASKHSKS DMAILASQLT GPMDLKIFYR GKTTGSNACV
SRPCSLLCLP KANNTRTCRC PDGVSGSVLP SGDLMCECPQ GYQLKNHTCV KEENTCLRNQ
YRCSNGNCIN SIWWCDFDND CGDMSDERNC PTTVCDLDTQ FRCQESGTCI PLSYKCDLED
DCGDNSDESH CELHQCRSNE YSCSSGMCIR SSWVCDGDND CRDWSDEANC TAIYHTCEAS
NFQCHNGHCI PQRWACDGDM DCQDGSDEDP VTCEKKCNGF RCPNGTCIPS SKHCDGLHDC
GDGSDEQHCE PLCTRFMDFV CKNRQQCLFQ SMVCDGIVQC RDGSDEDAAF AGCSHDPEFH
KVCDELSFQC QNGVCISLIW KCDGMDDCGD DSDEANCENP TEAPNCSRYF QFQCENGHCI
PNRWKCDREN DCGDWSDEKD CGDLHILPSP TPGPSTCLPN YYRCSSGACV MDSWVCDGYR
DCADGSDEEA CPSPANVTAA STPTQLGRCD RFEFECRQPK KCIPNWRRCD GHQDCQDGQD
EANCPTRSSL TCTSWEFKCE DGETCIVLSE RCDGFLDCSD ESDERNCSEE LNVYKIQNLQ
WTADFSGDIT LTWLKPKKMP SASCVYNVYY RVVGESMWKI LETHSNKTST VLKVLKPDTT
YQVKVQVQCL SKVHSTNDFV TLRTPEGLPD APQNLQLSLH REVEGVIVGH WTPPIHTHGL
IREYIVEYSR SGSKMWASQR SAGNSTEIRN LLLNAPYTVR VAAVTSRGIG NWSDSKSITT
TNKGKVIPQP DIHIDSYDEN SLSFTLSMDS DIKVNGYVVN LFWAFDTHAQ EQRTLNFQGS
MLSHRVGNLT AHTPYEISAW AKTDLGDSPL AFEHVTTRGV RPPAPSLKAK AINQTAVECT
WTGPRNVVYG IFYATSFLDL YRNPKSVTTS QHNKTVLVSR DEQYLFLVRV VVPYQGPSSD
YVVVRMIPDS RLPPRHLHVV HTGKTSAVIK WESPYDSPDQ DLLYAIAVKD LIRKSDRSYK
VKSRNSTVEY TLNKLEPGGK YHVIVQLGNM SKDSSIKITT VSLSAPDALK IITENDHVLL
FWKSLALKEK HFNESRGYEI HMFDSAMNIT AYLGNTTDNF FKISNLKLGH NYTFTVQAQC
LFGSQICGEP AVLLYDELGS GKLLLLPVSV FSSGEIYQER STV
//
