LMBD1_RAT
ID LMBD1_RAT Reviewed; 537 AA.
AC Q6AZ61; Q8R3Z8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Lysosomal cobalamin transport escort protein LMBD1 {ECO:0000250|UniProtKB:Q9NUN5};
DE Short=LMBD1;
DE AltName: Full=LMBR1 domain-containing protein 1;
GN Name=Lmbrd1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lee Y., Xu C., Lee W.;
RT "Cloning and analysis of p53-related gene from cDNA library following short
RT interval successive partial hepatectomy in rat liver regeneration.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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-525 AND SER-528, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Lysosomal membrane chaperone required to export cobalamin
CC (vitamin B12) from the lysosome to the cytosol, allowing its conversion
CC to cofactors. Targets ABCD4 transporter from the endoplasmic reticulum
CC to the lysosome. Then forms a complex with lysosomal ABCD4 and
CC cytoplasmic MMACHC to transport cobalamin across the lysosomal membrane
CC (By similarity). Acts as an adapter protein which plays an important
CC role in mediating and regulating the internalization of the insulin
CC receptor (INSR) (By similarity). Involved in clathrin-mediated
CC endocytosis of INSR via its interaction with adapter protein complex 2
CC (By similarity). Essential for the initiation of gastrulation and early
CC formation of mesoderm structures during embryogenesis (By similarity).
CC {ECO:0000250|UniProtKB:Q8K0B2, ECO:0000250|UniProtKB:Q9NUN5}.
CC -!- SUBUNIT: Interacts with ABCD4; this interaction induces the
CC translocation of ABCD4 from the endoplasmic reticulum to the lysosome.
CC Interacts with ABCD4 and MMACHC; this interaction ensures the transport
CC of cobalamin from the lysosome to the cytoplasm (By similarity).
CC Interacts with INSR, adapter protein complex 2 and clathrin heavy chain
CC (By similarity). {ECO:0000250|UniProtKB:Q8K0B2,
CC ECO:0000250|UniProtKB:Q9NUN5}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9NUN5}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q9NUN5}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q8K0B2}; Multi-pass
CC membrane protein {ECO:0000255}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000250|UniProtKB:Q8K0B2}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9NUN5}.
CC -!- SIMILARITY: Belongs to the LIMR family. LMBRD1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AY093598; AAM18793.1; -; mRNA.
DR EMBL; BC078723; AAH78723.1; -; mRNA.
DR RefSeq; NP_631928.2; NM_139189.2.
DR AlphaFoldDB; Q6AZ61; -.
DR SMR; Q6AZ61; -.
DR STRING; 10116.ENSRNOP00000016887; -.
DR GlyGen; Q6AZ61; 7 sites.
DR iPTMnet; Q6AZ61; -.
DR PhosphoSitePlus; Q6AZ61; -.
DR jPOST; Q6AZ61; -.
DR PaxDb; Q6AZ61; -.
DR PRIDE; Q6AZ61; -.
DR Ensembl; ENSRNOT00000016887; ENSRNOP00000016887; ENSRNOG00000012178.
DR GeneID; 246046; -.
DR KEGG; rno:246046; -.
DR UCSC; RGD:708471; rat.
DR CTD; 55788; -.
DR RGD; 708471; Lmbrd1.
DR eggNOG; ENOG502QQ2T; Eukaryota.
DR GeneTree; ENSGT00390000002581; -.
DR HOGENOM; CLU_028341_1_0_1; -.
DR InParanoid; Q6AZ61; -.
DR OMA; IITTFTW; -.
DR OrthoDB; 744771at2759; -.
DR PhylomeDB; Q6AZ61; -.
DR Reactome; R-RNO-9758881; Uptake of dietary cobalamins into enterocytes.
DR Reactome; R-RNO-9758890; Transport of RCbl within the body.
DR PRO; PR:Q6AZ61; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000012178; Expressed in Ammon's horn and 20 other tissues.
DR Genevisible; Q6AZ61; RN.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; ISS:UniProtKB.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISS:UniProtKB.
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:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR GO; GO:0035612; F:AP-2 adaptor complex binding; ISS:UniProtKB.
DR GO; GO:0032050; F:clathrin heavy chain binding; ISS:UniProtKB.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0005158; F:insulin receptor binding; ISO:RGD.
DR GO; GO:0140318; F:protein transporter activity; IEA:Ensembl.
DR GO; GO:0043495; F:protein-membrane adaptor activity; ISO:RGD.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISS:UniProtKB.
DR GO; GO:0009235; P:cobalamin metabolic process; ISO:RGD.
DR GO; GO:0007369; P:gastrulation; ISS:UniProtKB.
DR GO; GO:0038016; P:insulin receptor internalization; ISS:UniProtKB.
DR GO; GO:0061462; P:protein localization to lysosome; ISS:UniProtKB.
DR GO; GO:0072665; P:protein localization to vacuole; IBA:GO_Central.
DR InterPro; IPR006876; LMBR1-like_membr_prot.
DR Pfam; PF04791; LMBR1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cobalamin; Cobalt; Cytoplasmic vesicle;
KW Developmental protein; Endocytosis; Endoplasmic reticulum; Gastrulation;
KW Glycoprotein; Lysosome; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..537
FT /note="Lysosomal cobalamin transport escort protein LMBD1"
FT /id="PRO_0000260518"
FT TOPO_DOM 1..7
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..97
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..185
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..361
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..483
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..504
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 505..537
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 229..232
FT /note="YERL motif; mediates interaction with adapter
FT protein complex 2 and is essential for its function in
FT clathrin-mediated endocytosis of INSR"
FT /evidence="ECO:0000250|UniProtKB:Q8K0B2"
FT MOTIF 291..294
FT /note="WTKF motif; mediates interaction with adapter
FT protein complex 2 and is essential for its function in
FT clathrin-mediated endocytosis of INSR"
FT /evidence="ECO:0000250|UniProtKB:Q8K0B2"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8K0B2"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 132
FT /note="T -> A (in Ref. 1; AAM18793)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="I -> T (in Ref. 1; AAM18793)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 537 AA; 61018 MW; 8048BC2561BBD72E CRC64;
MAAAAADLVI GWCIFGLLLL AILAFCWVYV RKYQSQRESE VVSTVTAIFS LAVALITSAL
LPVDIFLVSY MKNQNGTFKD WANANVTVQI ENTVLYGYYT LYSVILFCVF FWIPFVYFYY
EEKDDDDTSK CTQVKTALKY TLGFVVICAL LLLVGAFVPL NLPNNNNSTE WEKVKLLFED
LGTGQGLAAL SFSISSLTLI GMLAAITYTA YGMSALPLNL IKGTRSTAYE RLENTEDIEE
VEQHIQTIRS KSKDGRPLSA RDRRTLKQCE ERLRTLRKRE RHLEFIENSW WTKFCGALRP
LKIIWGIFFI LVALLFVISL FLSNLDKALH SAGIDSGFIV FGTNLSNPLN MLLPLLQTVF
PLDYILITII IMYFIFTSMA GIRNIGIWFF WIRLYKIRRG RTRPQALLFL CMILLLIVLH
TSYMIYSLAP QYVMYGSQNY LIESNITSDA HKGNSTLAVP KRCDADAPKD QCTVTRTYVF
LHKFWFFSAA YYFGNWAFLV VFLIGLIVSC CKGKKSVIEG VDEDSDLSDD EPSAYSA
