ID LMBRL_MOUSE Reviewed; 489 AA.
AC Q9D1E5; Q3TD82; Q69ZP7;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Protein LMBR1L;
DE AltName: Full=Lipocalin-1-interacting membrane receptor {ECO:0000250|UniProtKB:Q6UX01};
DE Short=LIMR {ECO:0000250|UniProtKB:Q6UX01};
DE AltName: Full=Uteroglobin receptor;
GN Name=Lmbr1l; Synonyms=D15Ertd735e, Kiaa1174;
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 [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RA Mukherjee A.B., Zhang Z., Chowdhury B.;
RT "Mouse uteroglobin receptor.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Cerebellum, Dendritic cell, Embryo, Kidney, Pituitary, and Spleen;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INTERACTION WITH
RP UBAC2; FAF2; VCP; AMFR; ZNRF3; CTNNB1; LRP6; GSK3B; FZD6; DVL2 AND RNF43,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF 212-CYS--GLN-489.
RX PubMed=31073040; DOI=10.1126/science.aau0812;
RA Choi J.H., Zhong X., McAlpine W., Liao T.C., Zhang D., Fang B., Russell J.,
RA Ludwig S., Nair-Gill E., Zhang Z., Wang K.W., Misawa T., Zhan X., Choi M.,
RA Wang T., Li X., Tang M., Sun Q., Yu L., Murray A.R., Moresco E.M.Y.,
RA Beutler B.;
RT "LMBR1L regulates lymphopoiesis through Wnt/beta-catenin signaling.";
RL Science 364:0-0(2019).
CC -!- FUNCTION: Plays an essential role in lymphocyte development by
CC negatively regulating the canonical Wnt signaling pathway
CC (PubMed:31073040). In association with UBAC2 and E3 ubiquitin-protein
CC ligase AMFR, promotes the ubiquitin-mediated degradation of CTNNB1 and
CC Wnt receptors FZD6 and LRP6 (PubMed:31073040). LMBR1L stabilizes the
CC beta-catenin destruction complex that is required for regulating CTNNB1
CC levels (PubMed:31073040). Acts as a LCN1 receptor and can mediate its
CC endocytosis (By similarity). {ECO:0000250|UniProtKB:Q6UX01,
CC ECO:0000269|PubMed:31073040}.
CC -!- SUBUNIT: Dimer (By similarity). Can also form higher oligomers (By
CC similarity). Interacts with LCN1; this interaction mediates the
CC endocytosis of LCN1 (By similarity). Interacts with UBAC2, FAF2, VCP,
CC AMFR, ZNRF3, CTNNB1, LRP6, GSK3B, FZD6, DVL2 and RNF43
CC (PubMed:31073040). Interacts with GSK3A (By similarity). Interaction
CC with LGB and SCGB1A1 is controversial (By similarity).
CC {ECO:0000250|UniProtKB:Q6UX01, ECO:0000269|PubMed:31073040}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31073040};
CC Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000269|PubMed:31073040}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D1E5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D1E5-2; Sequence=VSP_016897;
CC -!- TISSUE SPECIFICITY: Highly expressed in the bone marrow, thymus, spleen
CC and lymphocytes. {ECO:0000269|PubMed:31073040}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit severely impaired development of all
CC lymphoid lineages, compromised antibody responses to immunization,
CC reduced cytotoxic T-cell killing activity and natural killer (NK) cell
CC function, and resistance to cytomegalovirus infection
CC (PubMed:31073040). T-cells are predisposed to apoptosis and die in
CC response to antigen-specific or homeostatic expansion signals
CC (PubMed:31073040). Impaired differentiation of hematopoietic stem cells
CC into the lymphoid primed multipotent progenitor (LMPP) and common
CC lymphoid progenitor populations that give rise to T-cells, B-cells, and
CC NK cells (PubMed:31073040). {ECO:0000269|PubMed:31073040}.
CC -!- SIMILARITY: Belongs to the LIMR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32399.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY052398; AAL13076.1; -; mRNA.
DR EMBL; AK173121; BAD32399.1; ALT_INIT; mRNA.
DR EMBL; AK003656; BAB22919.1; -; mRNA.
DR EMBL; AK030589; BAC27033.1; -; mRNA.
DR EMBL; AK049110; BAC33547.1; -; mRNA.
DR EMBL; AK143891; BAE25586.1; -; mRNA.
DR EMBL; AK154968; BAE32960.1; -; mRNA.
DR EMBL; AK170328; BAE41722.1; -; mRNA.
DR EMBL; BC023397; AAH23397.1; -; mRNA.
DR CCDS; CCDS27811.1; -. [Q9D1E5-1]
DR RefSeq; NP_083374.1; NM_029098.3. [Q9D1E5-1]
DR AlphaFoldDB; Q9D1E5; -.
DR STRING; 10090.ENSMUSP00000023736; -.
DR PhosphoSitePlus; Q9D1E5; -.
DR EPD; Q9D1E5; -.
DR PaxDb; 10090-ENSMUSP00000023736; -.
DR ProteomicsDB; 290047; -. [Q9D1E5-1]
DR ProteomicsDB; 290048; -. [Q9D1E5-2]
DR Antibodypedia; 42857; 93 antibodies from 18 providers.
DR DNASU; 74775; -.
DR Ensembl; ENSMUST00000023736.10; ENSMUSP00000023736.9; ENSMUSG00000022999.16. [Q9D1E5-1]
DR GeneID; 74775; -.
DR KEGG; mmu:74775; -.
DR UCSC; uc007xoi.1; mouse. [Q9D1E5-1]
DR AGR; MGI:1289247; -.
DR CTD; 55716; -.
DR MGI; MGI:1289247; Lmbr1l.
DR VEuPathDB; HostDB:ENSMUSG00000022999; -.
DR eggNOG; KOG3722; Eukaryota.
DR GeneTree; ENSGT00390000007809; -.
DR HOGENOM; CLU_029445_1_0_1; -.
DR InParanoid; Q9D1E5; -.
DR OMA; QQRRTWW; -.
DR OrthoDB; 2878909at2759; -.
DR PhylomeDB; Q9D1E5; -.
DR TreeFam; TF313485; -.
DR BioGRID-ORCS; 74775; 6 hits in 77 CRISPR screens.
DR PRO; PR:Q9D1E5; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9D1E5; Protein.
DR Bgee; ENSMUSG00000022999; Expressed in retinal neural layer and 136 other cell types or tissues.
DR Genevisible; Q9D1E5; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISO:MGI.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; IMP:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR GO; GO:0070231; P:T cell apoptotic process; IMP:UniProtKB.
DR GO; GO:0030217; P:T cell differentiation; IMP:UniProtKB.
DR GO; GO:0042098; P:T cell proliferation; IMP:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR008075; LIMR.
DR InterPro; IPR006876; LMBR1-like_membr_prot.
DR PANTHER; PTHR12625; LIPOCALIN-1 INTERACTING MEMBRANE RECEPTOR LIMR; 1.
DR PANTHER; PTHR12625:SF2; PROTEIN LMBR1L; 1.
DR Pfam; PF04791; LMBR1; 2.
DR PRINTS; PR01692; LIPOCALINIMR.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Endocytosis; Endoplasmic reticulum;
KW Membrane; Receptor; Reference proteome; Transmembrane; Transmembrane helix;
KW Wnt signaling pathway.
FT CHAIN 1..489
FT /note="Protein LMBR1L"
FT /id="PRO_0000053912"
FT TOPO_DOM 1..21
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..114
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..196
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..350
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..431
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..76
FT /note="LCN1-binding"
FT /evidence="ECO:0000250|UniProtKB:Q6UX01"
FT REGION 1..59
FT /note="Interaction with LGB"
FT /evidence="ECO:0000250|UniProtKB:Q6UX01"
FT VAR_SEQ 1..127
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_016897"
FT MUTAGEN 212..489
FT /note="Missing: In st (strawberry phenotype); affected mice
FT exhibit severe lymphopenia, failure of lymphocyte
FT development, reduced natural killer (NK) cell function and
FT impaired B-cell development."
FT /evidence="ECO:0000269|PubMed:31073040"
FT CONFLICT 88
FT /note="S -> G (in Ref. 3; BAE41722)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="M -> V (in Ref. 3; BAE41722)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="V -> A (in Ref. 3; BAE41722)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 54958 MW; 50AA85EF2C58B79A CRC64;
MEAADYEVLS VREQLFHDRV RECIISILLF ATLYILCHIF LTRFKKPAEF TTVDDEDATV
NKIALELCTF TLAVALGAVL LLPFSIISNE VLLSLPRNYY IQWLNGSLIH GLWNLVFLFS
NLSLVFLMPF AYFFTESEGF AGSRKGVLGR VYETVVMLIL LTLLVLGMVW VASAIVDNDK
ASRESLYDFW EYYLPYLYSC ISFLGVLLLL VCTPLGLARM FSVTGKLLVK PRLLEDLEEQ
LNCSAFEEAA LTRRICNPTS CWLPLDMELL HRQVLALQAQ RVLLEKRRKA SAWQRNLGYP
LAMLCLLVLT GLSVLIVAVH ILELLIDEAA MPRGMQDAAL GQASFSKLGS FGAIIQVVLI
FYLMVSSVVG FYSSPLFGSL RPRWHDTSMT QIIGNCVCLL VLSSALPVFS RTLGLTRFDL
LGDFGRFNWL GNFYIVFLYN AAFAGLTTLC LVKTFTAAVR AELIRAFGLD RLPLPVSGFP
RASRKKQHQ
//
