LMBRL_PONAB
ID LMBRL_PONAB Reviewed; 490 AA.
AC Q5RBY7;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Protein LMBR1L;
DE AltName: Full=Lipocalin-1-interacting membrane receptor {ECO:0000250|UniProtKB:Q6UX01};
DE Short=LIMR {ECO:0000250|UniProtKB:Q6UX01};
GN Name=LMBR1L;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an essential role in lymphocyte development by
CC negatively regulating the canonical Wnt signaling pathway (By
CC similarity). In association with UBAC2 and E3 ubiquitin-protein ligase
CC AMFR, promotes the ubiquitin-mediated degradation of CTNNB1 and Wnt
CC receptors FZD6 and LRP6 (By similarity). LMBR1L stabilizes the beta-
CC catenin destruction complex that is required for regulating CTNNB1
CC levels (By similarity). Acts as a LCN1 receptor and can mediate its
CC endocytosis (By similarity). {ECO:0000250|UniProtKB:Q6UX01,
CC ECO:0000250|UniProtKB:Q9D1E5}.
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, GSK3A, GSK3B, FZD6, DVL2 and RNF43 (By
CC similarity). Interaction with LGB and SCGB1A1 is controversial (By
CC similarity). {ECO:0000250|UniProtKB:Q6UX01,
CC ECO:0000250|UniProtKB:Q9D1E5}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6UX01};
CC Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:Q6UX01}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the LIMR family. {ECO:0000305}.
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DR EMBL; CR858495; CAH90723.1; -; mRNA.
DR RefSeq; NP_001125402.1; NM_001131930.1.
DR AlphaFoldDB; Q5RBY7; -.
DR STRING; 9601.ENSPPYP00000005104; -.
DR GeneID; 100172307; -.
DR KEGG; pon:100172307; -.
DR CTD; 55716; -.
DR eggNOG; KOG3722; Eukaryota.
DR InParanoid; Q5RBY7; -.
DR OrthoDB; 768229at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0070231; P:T cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
DR GO; GO:0042098; P:T cell proliferation; ISS: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; PTHR12625; 1.
DR Pfam; PF04791; LMBR1; 2.
DR PRINTS; PR01692; LIPOCALINIMR.
PE 2: Evidence at transcript level;
KW Cell membrane; Endocytosis; Endoplasmic reticulum; Membrane; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix;
KW Wnt signaling pathway.
FT CHAIN 1..490
FT /note="Protein LMBR1L"
FT /id="PRO_0000053913"
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..490
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"
SQ SEQUENCE 490 AA; 55347 MW; D05DE5C2D943EA82 CRC64;
MEAPDYEVLS VREQLFHERI RECIISTLLF ATLYILCHIF LTRFKKPAEF TTVDDEDATV
NKIALELCTF TLAIALGAVL LLPFSIISNE VLLSLPRNYY IQWLNGSLIH GLWNLVFLFS
NLSLIFLMPF AYFFTESEGF AGSRRGVLGR VYETVVMLML LTLLVLGMVW VASAILDNNK
ASRESLYDFW EYYLPYLYSC ISFLGVLLLL VCTPLGLARM FSVTGKLLVK PRLLEDLEEQ
LYCSAFEEAA PTRRICNPTS CWLPLDMELL HRQVLALQTQ RVLLEKRRKA SAWQRNLGYP
LAMLCLLVLT GLSVLIVAIH ILELLIDEAA MPRGMQDASL GQVSFSRLGS FGAVIQVALI
FYLMVSSVVG FYSSPLFRSL RPRWHDTAMT QIIGNCVCLL VLSSALPVFS RTLGLTRFDL
LGDFGRFNWL GNFYIVFLYN AAFAGLTTLC LVKTFTAAVR AELIRAFGLD RLPLPVSGFP
PRASRKTQHQ
