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Database: UniProt
Entry: A0A1S3MM53_SALSA
LinkDB: A0A1S3MM53_SALSA
Original site: A0A1S3MM53_SALSA 
ID   A0A1S3MM53_SALSA        Unreviewed;      1624 AA.
AC   A0A1S3MM53;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Low-density lipoprotein receptor-related protein 5-like {ECO:0000313|RefSeq:XP_014004308.1};
GN   Name=LOC106573620 {ECO:0000313|RefSeq:XP_014004308.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014004308.1};
RN   [1] {ECO:0000313|RefSeq:XP_014004308.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014004308.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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_014004308.1; XM_014148833.1.
DR   STRING; 8030.ENSSSAP00000065779; -.
DR   PaxDb; 8030-ENSSSAP00000065779; -.
DR   GeneID; 106573620; -.
DR   KEGG; sasa:106573620; -.
DR   OMA; HECLCPL; -.
DR   OrthoDB; 3107655at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa16.
DR   Bgee; ENSSSAG00000056819; Expressed in actinopterygian pyloric caecum and 13 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd00112; LDLa; 3.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 3.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 4.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
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   PANTHER; PTHR46513:SF16; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 5; 1.
DR   PANTHER; PTHR46513; VITELLOGENIN RECEPTOR-LIKE PROTEIN-RELATED-RELATED; 1.
DR   Pfam; PF14670; FXa_inhibition; 3.
DR   Pfam; PF00057; Ldl_recept_a; 3.
DR   Pfam; PF00058; Ldl_recept_b; 11.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00192; LDLa; 3.
DR   SMART; SM00135; LY; 20.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 3.
DR   SUPFAM; SSF63825; YWTD domain; 4.
DR   PROSITE; PS01209; LDLRA_1; 2.
DR   PROSITE; PS50068; LDLRA_2; 3.
DR   PROSITE; PS51120; LDLRB; 12.
PE   4: Predicted;
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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lipoprotein {ECO:0000313|RefSeq:XP_014004308.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170,
KW   ECO:0000313|RefSeq:XP_014004308.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1395..1415
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REPEAT          125..167
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          168..211
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          212..254
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   DOMAIN          303..342
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|SMART:SM00181"
FT   REPEAT          390..432
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          433..475
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          476..519
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          520..562
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   DOMAIN          609..646
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|SMART:SM00181"
FT   REPEAT          692..734
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          735..777
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          778..820
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          821..862
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   DOMAIN          910..947
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|SMART:SM00181"
FT   REPEAT          1130..1172
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   DOMAIN          1222..1266
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|SMART:SM00181"
FT   REGION          1008..1034
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1487..1514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1575..1624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1009..1034
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1487..1503
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1591..1605
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1610..1624
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        1286..1301
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1304..1316
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1311..1329
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1323..1338
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1342..1354
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1349..1367
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1361..1376
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   1624 AA;  181833 MW;  1C8B580F9EB66AE5 CRC64;
     MELKLRAIEM DVFLVELLFY SSLLSVGNGS PLLLFANRRD VRLVDVEMGR PESAVVVSDL
     EDAAAVDFLY SEGLIFWTDV SEEAIKQTYY NQSTDSLKEA LGTRQTVVVS GLDSPDGLAC
     DWLGRKLYWT DSETNRIEVA NLDGTSRKVL FWLDLDQPRA IALNPAHRYM YWTDWGEEPR
     IERAGMDGSN RKIIVEVDIY WPNGLTVDLD EQKLYWADAK LSFIHRANLD GSSRETVVEG
     TLTHPFALTL SDETLYWTDW QTRSIHACNK HTGDKRREIL SGIYSPMDIQ VLGSDRQPDI
     HTPCSDSNGG CSHLCLLSPM QPFYSCACPT GVKLKEDGKT CRPGAEQVLL LARRTDLRRI
     SLDLPDFTDI VLQVDDIRHA IAIDYDPVDG YVYWTDDEVK AIRRSRIDGT EAQTLVTTEI
     NHPDGIAVDW VARNLYWTDT GTDRIEVTRL NGTSRRILIS ENLDEPRAIV LDPVNGYMYW
     TDWGEKPKIE RANLDGMERL VLLNTSLGWP NGLAIDYEAG KLYWGDAKTD KIEVIDVDGS
     NRMTLLEDKL PHIFGFTLLG DYIYWTDWQR RSIERVHKTN AIREIIIDQL PDLMGLKATR
     VTEVSGTNGC VEDNGGCSHL CFHRPQGLRC DCPMGLELLN DMRTCVVPEA FLLFTNRADI
     RSISLGTNSN DVAIPLTGVK EASALDFDVS ENRIYWTDVS TKTISRAFMN GSSVEHVIEF
     GLDYPEGMAV DWMGRNVYWA DTGTNRIEVA RLDGQYRQVL VCKDLDNPRS LALNPANGYM
     YWTEWGGKPR IARAHMDGSN IMTLVDKVGR ANGLTIDYID QRLYWTDLDT CMIESTNMQG
     LQREIVADDL PHPFGLTQYR DYIYWTDWNL RSIERADKRS GLNRTMVQGH LEYVMDILVF
     HSSRQDGAND CSQNNGNCAH LCLASPAGSQ CRCASHYILD SNSRNCSSPS SFLLFSQKAS
     ISRMVLGEQS PDIILPIHVL RNVRAISYDP LDHLVYWVDG RQNIRRARDD GTQSSVVVST
     TSTHQQQPDK QPHDLSLDTY SRTVYWTCEA TNTINLQRLD GDAVGVVLRD EHDKPRAIVV
     NAEKGYMYFT TMQDRSAKIE GASLDGTERE SLFTTGLIRP VALALDNKLG KLFWVDADLK
     RIESSDLTGA NRIVLQDSNI LQPMGLTVLG EHLYWIDRQQ QMIERVDKLI GEKRTRIQGR
     IAYLTSIHAV EDMDPTEFAS HPCSRDNGGC SHICIAKGDG TPRCSCPMHL VLLPNLLICG
     DPPTCSTEQF TCATGDIDCI PMAWRCDGVA ECDDNSDEEN CPMCSAIQFQ CDKGQCVDAQ
     LRCNGEPDCA DNSDEQDCDT ICLPNQFRCN NKQCILKKQQ CDSYNDCADN SDELFCEFLT
     PPSSDVQSPS HTSTIGPVIG IILSVFVMGG MYFVCQRVVC RRYKGPNGAF PHDYISGTSH
     VPLNFISPSS SQHGTFTGIS CGKSMMSSVS LMGSSCSGAP LYDRNHVTGA SSSSSSSTKG
     AFYPQMLNPP PSPATDRSLY NAEIFYSSNS PSTTRSYRPY LMHGVAPPTT PCSTDVCDSD
     YATSRWKSNK YYMDLNSDSD PYPPPPTPRS QYLSAEESCP PSPSTERSYF HLCPPPPSPC
     TDSS
//
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