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
RC   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   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.
DR   Genevisible; Q9D1E5; MM.
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
//