ID A0A1S3PT70_SALSA Unreviewed; 1901 AA.
AC A0A1S3PT70;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Low-density lipoprotein receptor-related protein 4-like isoform X4 {ECO:0000313|RefSeq:XP_014030414.1};
GN Name=LOC106587054 {ECO:0000313|RefSeq:XP_014030414.1};
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_014030414.1};
RN [1] {ECO:0000313|RefSeq:XP_014030414.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014030414.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the LDLR family.
CC {ECO:0000256|ARBA:ARBA00009939}.
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_014030414.1; XM_014174939.1.
DR STRING; 8030.ENSSSAP00000077350; -.
DR PaxDb; 8030-ENSSSAP00000077350; -.
DR GeneID; 106587054; -.
DR OrthoDB; 3107655at2759; -.
DR Proteomes; UP000087266; Chromosome ssa26.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; cd00054; EGF_CA; 1.
DR CDD; cd00112; LDLa; 7.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 8.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 4.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
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; PTHR22722; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 2-RELATED; 1.
DR PANTHER; PTHR22722:SF14; MEGALIN, ISOFORM A; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF14670; FXa_inhibition; 3.
DR Pfam; PF00057; Ldl_recept_a; 8.
DR Pfam; PF00058; Ldl_recept_b; 14.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00192; LDLa; 8.
DR SMART; SM00135; LY; 20.
DR SUPFAM; SSF57196; EGF/Laminin; 5.
DR SUPFAM; SSF57424; LDL receptor-like module; 8.
DR SUPFAM; SSF63825; YWTD domain; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 5.
DR PROSITE; PS50068; LDLRA_2; 8.
DR PROSITE; PS51120; LDLRB; 16.
PE 3: Inferred from homology;
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_014030414.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170,
KW ECO:0000313|RefSeq:XP_014030414.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1901
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010342712"
FT TRANSMEM 1717..1740
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 419..434
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT REPEAT 481..523
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 524..566
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 567..610
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 611..653
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 787..829
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 830..872
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 873..916
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 917..959
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1095..1137
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1138..1180
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1181..1224
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1225..1266
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1399..1441
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1442..1484
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1485..1528
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1529..1570
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 1655..1687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1856..1901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 52..67
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 72..84
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 79..97
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 91..106
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 111..123
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 118..136
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 149..161
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 156..174
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 168..183
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 192..204
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 199..217
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 211..226
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 232..244
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 239..257
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 251..266
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 271..283
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 278..296
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 290..305
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 313..325
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 320..338
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1901 AA; 211991 MW; 0BDFFA322C6D2FA3 CRC64;
MQVSVVLCSM ITFFLRSQGV LGSAECSCGR NHFTCAVSVF GECTCIPAQW QCDGDNDCGD
HSDEDGCMLP TCSPLDFHCD NGKCIRRSWV CDGDNDCEDD SDEQDCPPRE CEEDEFHCQN
GYCIRSLWHC DGDNDCGDNS DELCDMRKCS DKEFRCTDGS CIAEHWYCDG DTDCKDGSDE
ENCPSDVMTA TCSVEEFQCA YGRCILDIYH CDGDDDCGDW SDESDCSSHQ PCRSVEFMCS
SGMCINAGWR CDGEFDCDDQ SDEKNCTTSM CTADQFRCAS GRCVRLSWRC DGEDDCSDGS
DEDDCEKTDT PPCAPDQFLC GNGRCIGQRK VCNEVSDCGD GTDEHPHQDC RPRSSDGNCN
LNNGGCSQKC QMARGLVQCT CHTGYRLMED GRACQDVDEC AEEGYCSQGC TNTEGGFQCW
CVQGYELRPD KRSCKALGPE PVLLFANRID IRQVLPHRSE YTLLLNNLEN AIALDFHHNQ
ELVFWSDVTL DRIMKANLNG SNVEEVVSTG LESPGGLAID WIHDKLYWTD SGTSRIEVAN
LDGTHRKVLL WQSMEKPRAI ALHPIEGKIY WTDWGNTPRI EYANMDGSNR RVIADTHLFW
PNGLTIDYAG HRMYWVDAKH HVIERADLDG RNRKAVISQG LPHPFAITVF EDSLYWTDWH
TKSINSANKF TGKNQEIIRN KLHFPMDIHT LHPQRQPAGG RNRCGTNNGG CSHLCLPGNK
TYTCDCPTGF KKVDQHNCAL SLDKFLLFAR RTDIRRISFD TEDMSDDVIP LADVRNAVAL
DWHAEEGFIY WTDVTTDSIN RAQWDGSRQE VVVDTSLESP AGLAIDWVTN KLYWTDAGTD
RIEVSNADGS MRTVLIWENL DRPRDIVVDP IGGYMYWTDW GVSPKIEQAG MDASSRIVII
SSNLTWPNGL AIDYQTQRLY WADAGMKTIE FGNFDGSDRQ VLIGSQLPHP FGLTLHEEKL
YWTDWQSKSI QCANKMTGLG RQTLAENLEN LMDIHMFHRY RTTVRTPCAV NNGGCSHLCL
LAPPTKGSSC TCPTGINLQL DGKTCTHGMS SFLIFARRTD IRMVSLDIPY FADVVLAVNR
SMKNTIAIGV DPKEGKVYWS DSTLKKVSRA NINGTAHEDI IATGLMTTDG LAVDAVGRKI
YWTDTGTNRI EVANLDGSMR KVLIWQNLDS PRAIALYHEM GYMYWTDWGE HAKLERSAMD
GSDRLVLISN NLGWPNGLAV DSAGSQLLWA DAHTERIEAA DLNGQNRHTL VSPVQHPYGL
TLLGPHIYWT DWQSRSIQRA DKTTGANTIT VRSNLPGLMD IQAVDREKPL SFNKCGRRNG
GCSHLCLPRP NGTSCACPTG ILLKGDARSC DDSPETYLLF SNRVSVRRIS LDTNDHTDVH
VPVPELHNVI SLDYDSVDGK LYYTDVSLDV IRRVNLDGTG METVISQGLK TTDGLAVDWV
TRNMYWTDTG RNTIEVARLD GTSRKVLVNN SLDEPRAIAV FPSKGYLFWT DWGHIAKIER
AHLDGSDRKV LINTDLGWPN GLTLDYDTRR IFWVDAHLDR IESSDLNGKL RQILVSPVSH
PFALTQQDRW IYWTDWQTKS IQRVDKHTGR SKETVLANVE GLMDIIIVSP QRQSGTNHCG
VNNGGCTHLC FANTNSFVCA CPDEPDSRPC STISGYVPTS PDRETTSTPA PNKIPKAPTD
TPQQGPPLIN CTDKSLSVEG CVESNVVTAP HGEGLHISYG IGGALTILAI LIIITAFIIY
RHKKSKFADP GVSNLTYSNP SYRTSTQEVK IETSQKPPIY NQLRYKKEGG GDSGYTKEKI
RIVEGVCLLS SEELYWEDLK QLKPSRGGLH TCMRTDTVSL QASSASLDDG ETEQLLQEET
SECSSINTLT PVTVTPQRHP QHSLPDTGWT PARKPSTESE V
//
