ID A0A2Y9DA25_TRIMA Unreviewed; 860 AA.
AC A0A2Y9DA25;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Low-density lipoprotein receptor-related protein 12 isoform X1 {ECO:0000313|RefSeq:XP_004370760.1};
GN Name=LOC101346279 {ECO:0000313|RefSeq:XP_004370760.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004370760.1};
RN [1] {ECO:0000313|RefSeq:XP_004370760.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane, coated pit
CC {ECO:0000256|ARBA:ARBA00037878}.
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_004370760.1; XM_004370703.3.
DR AlphaFoldDB; A0A2Y9DA25; -.
DR STRING; 127582.A0A2Y9DA25; -.
DR GeneID; 101346279; -.
DR KEGG; tmu:101346279; -.
DR InParanoid; A0A2Y9DA25; -.
DR OrthoDB; 2916406at2759; -.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00112; LDLa; 4.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 5.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR PANTHER; PTHR24270:SF47; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 12; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00057; Ldl_recept_a; 3.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00192; LDLa; 5.
DR SUPFAM; SSF57424; LDL receptor-like module; 5.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 5.
PE 4: Predicted;
KW Coated pit {ECO:0000256|ARBA:ARBA00023176};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Lipoprotein {ECO:0000313|RefSeq:XP_004370760.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023176};
KW Receptor {ECO:0000313|RefSeq:XP_004370760.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..860
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015938437"
FT DOMAIN 47..159
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 259..372
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 622..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 166..178
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 173..191
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 185..200
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 239..254
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 395..410
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 433..448
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 451..463
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 458..476
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 470..485
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 860 AA; 94984 MW; 60E26D16DEBFCBB9 CRC64;
MARRWSTKES LRWRSALVLL FLGGVYGNGP LAEHSENVHI SGVSTACGET PEQIRAPSGI
ITSPGWPSEY PAKINCSWFI RANPGEIITI SFQDFDIQGS RRCSLDWLTI ETYKNIESYR
ACGSTIPPPY ISSQDHVWIR FHSDDSISRK GFRLAYFSGK SEEPNCACDQ FRCGNGKCIP
EAWRCNNMDE CGDSSDEEIC SKEANPPTAA AFQPCAYNQL QCLSRFTKVY TCLPESLKCD
GNIDCLDLGD EIDCDVPTCG QSLKYFYGTF NSPNYPDFYP PGSNCTWLID TGDHRKVILR
FTDFKLDGTG FGDYVKIYDG LEENPHKLLR VLTAFDSHAP LTVVSSSGQI RVHFCADKVN
AARGFNATYQ VDGFCLPWEI PCGGNWGCYS EQQRCDGYWH CPNGRDEVNC TMCQKEEFPC
SRNGVCYPRS DRCNYQNHCP NGSDEKNCFF CQPGNFHCKN NRCVFESWVC DSQDDCGDGS
DEENCPVIVP TRVITAAVIG SLICGLLLVI ALGCTCKLYS LRMFERRSFE TQLSRVEAEL
LRREAPPSYG QLIAQGLIPP VEDFPVCSPN QASVLENLRL AVRSQLGFTS IRLPTAGRSS
NIWSRIFNFA RSRHSGSLAL VSAEGDEVVP SQSTSREPER NNTHRSLFSV EPDDTDTENE
RRDTGGASGG VAAPLPQKVP PTTGVEATVG AYGSSSTQST RGGNTDHGRD VTSMEPTSVS
PARHQLTSAL SRMTQRLRWV RFTLGRSSSV NQNQSPLRQL DNGVNGREED DDVEMLIPVS
DAASDFDVND CSRPLLDLAS DQGQVFRQPF SATNPGVRPS NPGDGPCERC GIVHTAQIPD
ACLEATLKNE TSDDEALLLC
//
