ID A0A3Q2KZZ6_HORSE Unreviewed; 2172 AA.
AC A0A3Q2KZZ6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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|VGNC:VGNC:23452};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000030460.1, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000030460.1, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000030460.1,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000030460.1}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000030460.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: 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}. Recycling endosome membrane
CC {ECO:0000256|ARBA:ARBA00004480}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004480}.
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 Ensembl; ENSECAT00000042498.3; ENSECAP00000030460.1; ENSECAG00000019083.4.
DR VGNC; VGNC:23452; SORL1.
DR GeneTree; ENSGT01030000234563; -.
DR Proteomes; UP000002281; Chromosome 7.
DR Bgee; ENSECAG00000019083; Expressed in blood and 23 other cell types or tissues.
DR ExpressionAtlas; A0A3Q2KZZ6; baseline.
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-KW.
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; 4.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 11.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 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 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; 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; 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:UP000002281};
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..2172
FT /note="Sortilin-related receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018706499"
FT TRANSMEM 2094..2117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 758..801
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 802..845
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 846..890
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 1515..1607
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1611..1703
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1707..1802
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1892..1987
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DISULFID 1036..1048
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1043..1061
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1055..1070
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1096..1111
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1116..1128
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1123..1141
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1135..1150
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1157..1169
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1164..1182
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1202..1220
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1214..1229
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1283..1295
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1290..1308
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1302..1317
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1334..1352
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1346..1361
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1377..1389
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1384..1402
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1396..1411
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1449..1464
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1492..1507
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 2172 AA; 243989 MW; A949C0E3F27004C5 CRC64;
MATRSSRRES RLPFLFALVA LLPPGALCEV WTQTLHGGRA PLPQDQGFLV VRGDPRELRL
WAREAARGAD EKPLRRRRSA ALQPEPIKVY GQVYVSYDYG KSFKKISEKL NFGVGNNSEA
VISQFYHSPA DNKRYIFADA YAQYLWITFD FCNTIQGFPI PFRAGDLLLH SKAADLLLGF
DRSHPNKQLW KSDDFGQTWV LIQEHVKSFS WGIDPYDEPT TIYIERHEPF GFSTVFRSTD
FFQSLENQEV ILEEVKDFQL RDKYMFATRV LPFWESPEPS SVQLWVSFDR KPMQAAQFVT
RHPINEYYIA DASEDQVFVC VSHSNNRTNL YISEAEGLKF SLSLENVLYY SPGGAGSDTL
VRYFANEPFA DFHRVEGLQG VYIATLINGS MSEENMRSVI TFDKGGTWEF LQAPAFTGYG
EKINCELSQG CSLHLAQRLS QLLNLQLRRM PILSKESAPG LIIATGSVGK NLASKTNVYI
SSSAGARWRE ALPGPHYYTW GDHGGIIMAI AQGMETNELK YSTNEGETWK TFIFSEKPVF
VYGLLTEPGE KSTVFTIFGS NKENVHSWLI LQVNATDALG VPCTENDYKL WSPSDERGNE
CLLGHKTVFK RRTPHATCFN GEDFDRPVVV SNCSCTREDY ECDFGFKMSE DLLLEVCVPD
PEFPGRAYSP PVPCPEGSTY RRTRGYRKIS GDTCSGGDVE ARLEGELVPC PLAEENEFML
YALRKSIYRY DLASGATEQL PLTGLRAAVA LDFDYERNCL YWSDLALDII QRLCLNGSTG
QEVIINSGLE TVEALAFDPL SQLLYWVDAG FKKIEVANPD GDFRLTIVNS SVLDRPRALV
LMSQKGLMFW TDWGDLKPGI YRSNMDGSAV HRLVSEDVKW PNGIAVDDQW IYWTDAYLDC
IERITFSGQQ RSIILDNLPH PYAIAVFKNE IYWDDWSQLS IFRASKYSGS QMAILASQLT
GLMDMKIFYK GKTTGSNACV PQPCSLLCLP KANNSKSCRC PEGVASSVLP SGDLMCECPH
GYQLRNNTCV KEENTCLRNQ YRCSNGKCIN SIWWCDFDND CGDMSDERNC PTTICDLDTQ
FRCQESGSCI PLSYKCDLED DCGDNSDESH CEMHQCRSDE YNCSSGMCIR SSWVCDGDND
CRDWSDEANC TAIYHTCEAS NFQCHNGHCI PQRWACDGDT DCQDGSDEDP VNCEKKCNGF
RCPNGTCIPS SKHCDGLRDC SDGSDEQHCE PLCTRFMDFV CKNRQQCLFH SMVCDGIVQC
RDGSDEDPEF AGCSHDPEFR KVCDEFSFQC LNGVCISLIW KCDGMDDCGD YSDEANCEYP
TEAPNCSRYF QFQCENGHCV PNRWKCDREN DCGDWSDERD CGDSYLLPSP TPEPSTCLPN
YYRCSNGACV MDSWVCDGYR DCADGSDEEV CPSPANVTPA STPTQFGRCD RFEFECHQPK
KCIPNWKRCD GHQDCQDGQD EANCPTHSTL TCMSSEFKCE DGEACIVLSE RCDGFLDCSD
ESDEKACSDE LTVYKVQNLQ WTADFSGDVT LTWTRPKKMP SASCVYNVYY RVVGESMWKT
LETHSNKTNM ILKVLKPDTT YQVKVQVQCL SKVHNTNDFV TLRTPEGLPD APQNLQLSLH
REVEGVIVGQ WTPPAHTHGL IREYIVEYSR SGSKMWASQR AASNFTEIKN LLVSAQYTVR
VAAVTSRGIG NWSDSKSITT IKGKVIPPPD IHIDSYSENS LSFTLSMDND IKVNGYVVNL
FWAFDSHKQE KRTLNFQGSM LSHKVGNLTA HTAYEISAWA KTDLGDSPLA FEHVTTKGVR
PPAPSLKAKA INQTAVECTW TGPRNVVYGI FYATSFLDLY RNPKSLTTSL HNKTVIVSRD
EQYLFLVRVV VPYEGPSSDY VVVKMIPDSR LPPRHLHAVH ITKTSAVLKW ESPYDSPDQD
LLYAIAVKDL IRKSDRSYKV KSCNSTVEYT LNKLEPGGKY HIIVQLGNMS KDSNIKITTV
SLSAPDALKI ITENDHVLLF WKSLALKEKY FNESRGYEIH MFDSAMNITA YLGNTTDNFF
KISNLKLGHN YTFTVQARCL FGSQICGEPA VLLYDDLGSG GDASAFQAAR STDVAAVVVP
ILFLILLSLG VGFAILYTKH RRLQSSFTAF ANSHYSSRLG SAIFSSGDDL GEDDEDAPMI
TGFSDDVPMV IA
//
