LRP12_MOUSE
ID LRP12_MOUSE Reviewed; 858 AA.
AC Q8BUJ9; Q8BWM9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Low-density lipoprotein receptor-related protein 12;
DE Short=LRP-12;
DE Flags: Precursor;
GN Name=Lrp12;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Heart, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Probable receptor, which may be involved in the
CC internalization of lipophilic molecules and/or signal transduction. May
CC act as a tumor suppressor (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: May interact with RACK1, ZFYVE9 and NMRK2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Membrane, coated pit {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BUJ9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BUJ9-2; Sequence=VSP_009821;
CC -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39247.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK050512; BAC34299.1; -; mRNA.
DR EMBL; AK084675; BAC39247.1; ALT_SEQ; mRNA.
DR EMBL; BC058345; AAH58345.1; -; mRNA.
DR CCDS; CCDS27446.1; -. [Q8BUJ9-1]
DR CCDS; CCDS84168.1; -. [Q8BUJ9-2]
DR RefSeq; NP_001333965.1; NM_001347036.1. [Q8BUJ9-2]
DR RefSeq; NP_766402.1; NM_172814.3. [Q8BUJ9-1]
DR AlphaFoldDB; Q8BUJ9; -.
DR BioGRID; 232078; 1.
DR STRING; 10090.ENSMUSP00000022916; -.
DR GlyGen; Q8BUJ9; 5 sites.
DR iPTMnet; Q8BUJ9; -.
DR PhosphoSitePlus; Q8BUJ9; -.
DR SwissPalm; Q8BUJ9; -.
DR EPD; Q8BUJ9; -.
DR MaxQB; Q8BUJ9; -.
DR PaxDb; Q8BUJ9; -.
DR PRIDE; Q8BUJ9; -.
DR ProteomicsDB; 292112; -. [Q8BUJ9-1]
DR ProteomicsDB; 292113; -. [Q8BUJ9-2]
DR Antibodypedia; 2508; 192 antibodies from 31 providers.
DR DNASU; 239393; -.
DR Ensembl; ENSMUST00000022916; ENSMUSP00000022916; ENSMUSG00000022305. [Q8BUJ9-1]
DR Ensembl; ENSMUST00000110305; ENSMUSP00000105934; ENSMUSG00000022305. [Q8BUJ9-2]
DR GeneID; 239393; -.
DR KEGG; mmu:239393; -.
DR UCSC; uc007vom.1; mouse. [Q8BUJ9-1]
DR UCSC; uc007von.1; mouse. [Q8BUJ9-2]
DR CTD; 29967; -.
DR MGI; MGI:2443132; Lrp12.
DR VEuPathDB; HostDB:ENSMUSG00000022305; -.
DR eggNOG; KOG1215; Eukaryota.
DR GeneTree; ENSGT00940000158307; -.
DR HOGENOM; CLU_013747_0_0_1; -.
DR InParanoid; Q8BUJ9; -.
DR OMA; DQFHCGN; -.
DR OrthoDB; 135036at2759; -.
DR PhylomeDB; Q8BUJ9; -.
DR TreeFam; TF332149; -.
DR Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR BioGRID-ORCS; 239393; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q8BUJ9; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8BUJ9; protein.
DR Bgee; ENSMUSG00000022305; Expressed in manus and 234 other tissues.
DR ExpressionAtlas; Q8BUJ9; baseline and differential.
DR Genevisible; Q8BUJ9; MM.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0040011; P:locomotion; IBA:GO_Central.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IMP:MGI.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00112; LDLa; 5.
DR Gene3D; 2.60.120.290; -; 2.
DR Gene3D; 4.10.400.10; -; 5.
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 Pfam; PF00431; CUB; 2.
DR Pfam; PF00057; Ldl_recept_a; 4.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00192; LDLa; 5.
DR SUPFAM; SSF49854; SSF49854; 2.
DR SUPFAM; SSF57424; SSF57424; 5.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 5.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coated pit; Disulfide bond; Endocytosis;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..858
FT /note="Low-density lipoprotein receptor-related protein 12"
FT /id="PRO_0000017340"
FT TOPO_DOM 33..492
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..858
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 47..159
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 165..201
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 214..255
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 259..372
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 374..411
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 412..449
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 450..486
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT REGION 619..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..76
FT /evidence="ECO:0000250"
FT DISULFID 103..122
FT /evidence="ECO:0000250"
FT DISULFID 166..178
FT /evidence="ECO:0000250"
FT DISULFID 173..191
FT /evidence="ECO:0000250"
FT DISULFID 185..200
FT /evidence="ECO:0000250"
FT DISULFID 215..232
FT /evidence="ECO:0000250"
FT DISULFID 222..245
FT /evidence="ECO:0000250"
FT DISULFID 239..254
FT /evidence="ECO:0000250"
FT DISULFID 259..285
FT /evidence="ECO:0000250"
FT DISULFID 375..388
FT /evidence="ECO:0000250"
FT DISULFID 382..401
FT /evidence="ECO:0000250"
FT DISULFID 395..410
FT /evidence="ECO:0000250"
FT DISULFID 413..426
FT /evidence="ECO:0000250"
FT DISULFID 420..439
FT /evidence="ECO:0000250"
FT DISULFID 433..448
FT /evidence="ECO:0000250"
FT DISULFID 451..463
FT /evidence="ECO:0000250"
FT DISULFID 458..476
FT /evidence="ECO:0000250"
FT DISULFID 470..485
FT /evidence="ECO:0000250"
FT VAR_SEQ 27..45
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009821"
SQ SEQUENCE 858 AA; 94551 MW; B6E4AC8C2B69798C CRC64;
MARRWSTKES QRRGSAWLLL FLAGVYGNGA LAELSENVHI SGVSTACGES PEQIRAPSGI
ITSPGWPSDY PAQVNCSWLI RANPGEIITI SFQDFDIQGS RRCTLDWLTI ETYKNIESYR
ACGSTIPPPY ISSQDHVWIR FHSDDSVSRK GFRLAYFSGK SEQPDCACDQ FRCGNGKCIP
EAWKCNSMDE CGDSSDEEVC ASDAHPPTTT AFQPCAYNQF QCLSRFTKVY TCLPESLKCD
GNIDCLDLGD EIDCDMPTCG QWLKYFYGTF NSPNYPDFYP PGSNCTWLID TGDHRKVILR
FTDFKLDGTG YGDYVKIYDG LEENPRKLLR VLTAFDSHAP LTVVSSSGQI RVHFCADKVN
AARGFNATYQ VDGFCLPWEI PCGGNWGCYT EQQRCDGYWH CPNGRDEINC TMCQKEEFPC
SRNGVCYPRS DRCNYQNHCP NGSDEKNCFF CQPGNFHCKN NRCVFESWVC DSQDDCGDGS
DEENCPVIVP TRVITAAVIG SLICGLLLVI ALGCTCKLYS LRMFERRSFE TQLSRVEAEL
LRREAPPSYG QLIAQGLIPP VEDFPVCSPN QASVLENLRL AVRSQLGFTS IRLPMTGRSS
NIWNRIFNFA RSRHSGSLAL VSGDGDEVVP SQSSSRETER SRPHRSLFSV ESDDTDTENE
RRDTAGASGG VAAPLPQKVP PTTAVEATVG SGGNSSAQST RGGHADGREV SSVEAPSVSP
ARHQLTSALS RMTQGLRWVR FTLGRSSSTT QNRSPLRQLD TAVSGREDDD DVEMLIPVSD
GASDIDANDC SRPLLDLASD QVQGFRQPHS AGNPGVRTSN RDGPCERCGI VHTAQIPDTC
LEATVKTETS DDEALLLC
