LRP11_MOUSE
ID LRP11_MOUSE Reviewed; 483 AA.
AC Q8CB67; Q8C7Y7;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Low-density lipoprotein receptor-related protein 11;
DE Short=LRP-11;
DE Flags: Precursor;
GN Name=Lrp11;
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].
RC STRAIN=C57BL/6J; TISSUE=Bone, and Cerebellum;
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].
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
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DR EMBL; AK036676; BAC29532.1; -; mRNA.
DR EMBL; AK048919; BAC33492.1; -; mRNA.
DR EMBL; BC059874; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS23686.1; -.
DR RefSeq; NP_766372.1; NM_172784.3.
DR AlphaFoldDB; Q8CB67; -.
DR STRING; 10090.ENSMUSP00000019931; -.
DR GlyGen; Q8CB67; 3 sites.
DR iPTMnet; Q8CB67; -.
DR PhosphoSitePlus; Q8CB67; -.
DR MaxQB; Q8CB67; -.
DR PaxDb; Q8CB67; -.
DR PRIDE; Q8CB67; -.
DR ProteomicsDB; 292111; -.
DR Antibodypedia; 33293; 86 antibodies from 25 providers.
DR DNASU; 237253; -.
DR Ensembl; ENSMUST00000019931; ENSMUSP00000019931; ENSMUSG00000019796.
DR GeneID; 237253; -.
DR KEGG; mmu:237253; -.
DR UCSC; uc007ehw.2; mouse.
DR CTD; 84918; -.
DR MGI; MGI:2442989; Lrp11.
DR VEuPathDB; HostDB:ENSMUSG00000019796; -.
DR eggNOG; ENOG502QW7V; Eukaryota.
DR GeneTree; ENSGT00940000161275; -.
DR HOGENOM; CLU_042674_1_0_1; -.
DR InParanoid; Q8CB67; -.
DR OMA; AINMKST; -.
DR OrthoDB; 993497at2759; -.
DR PhylomeDB; Q8CB67; -.
DR TreeFam; TF325867; -.
DR BioGRID-ORCS; 237253; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Lrp11; mouse.
DR PRO; PR:Q8CB67; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8CB67; protein.
DR Bgee; ENSMUSG00000019796; Expressed in dentate gyrus of hippocampal formation granule cell and 90 other tissues.
DR ExpressionAtlas; Q8CB67; baseline and differential.
DR Genevisible; Q8CB67; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0033555; P:multicellular organismal response to stress; IEP:AgBase.
DR GO; GO:0009409; P:response to cold; IEP:AgBase.
DR GO; GO:0009408; P:response to heat; IEP:AgBase.
DR GO; GO:0035902; P:response to immobilization stress; IEP:AgBase.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:AgBase.
DR GO; GO:0042594; P:response to starvation; IEP:AgBase.
DR GO; GO:0009414; P:response to water deprivation; IEP:AgBase.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 4.10.400.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR042484; LRP11.
DR InterPro; IPR013980; MANSC_dom.
DR InterPro; IPR011106; MANSC_N.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR46876; PTHR46876; 2.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF07502; MANEC; 1.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00765; MANEC; 1.
DR SUPFAM; SSF49299; SSF49299; 1.
DR SUPFAM; SSF57424; SSF57424; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50986; MANSC; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endocytosis; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..483
FT /note="Low-density lipoprotein receptor-related protein 11"
FT /id="PRO_0000017338"
FT TOPO_DOM 33..433
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..483
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 85..172
FT /note="MANSC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00341"
FT DOMAIN 193..287
FT /note="PKD"
FT DOMAIN 293..329
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT REGION 346..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 294..306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 301..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 313..328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT CONFLICT 25
FT /note="L -> H (in Ref. 1; BAC33492)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="K -> KLFVWQ (in Ref. 1; BAC33492)"
FT /evidence="ECO:0000305"
FT CONFLICT 401..483
FT /note="DSNSSGKNQEEGNYDLKSKSGQAGGEHPAPEAGAVLPLALGLAITVLLLLMV
FT TCRLRLVKQKLKKARPITSEESDYLINGMYL -> AIPQERTKKKEIMISSPRVAKQEG
FT STRPRKQVRCYLWH (in Ref. 2; BC059874)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 51814 MW; 7AC8F124DD30CC82 CRC64;
MATRGGGPGP GFRHRALRGL LLLCLWLPGS RPGEPAAPSS GVDRLLQDFR RQLQRARPRE
ELEPELLGGP REDCPGAGGT AVYRAVPDTI IRTQDSIAAG ASFLRAPGSV RGWRQCVTAC
CSEPSCSVAV VQLPRGPSVP APMPAPRCYL FNCTARGRSV CKFAPLRGYR TYTLSRAEDA
AGIPPRPDED KPPVSKAGKD VVLHLPTDGV VLDGRESSDD HAIVLYEWTL QQGDPSSVDM
KVPQPGTLRL SRLKEGAYIF QLTVTDSVGQ RSSDNVSVTV LPRPYSTGGC SSACSRYHFF
CDSGCCIDIA LACDGVRQCP DGSDEDFCQN LALDRKLVTH TVATSAQPGA MGLNEGEGDP
KLEKSQRATT HNQPATVSHP ETRIHSTQKA PESQINPVQP DSNSSGKNQE EGNYDLKSKS
GQAGGEHPAP EAGAVLPLAL GLAITVLLLL MVTCRLRLVK QKLKKARPIT SEESDYLING
MYL
