LMBD1_HUMAN
ID LMBD1_HUMAN Reviewed; 540 AA.
AC Q9NUN5; A8K204; E1P531; Q5VUN6; Q86Y70; Q96FW4; Q9BY56; Q9NZD6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Lysosomal cobalamin transport escort protein LMBD1 {ECO:0000303|PubMed:27456980};
DE Short=LMBD1 {ECO:0000303|PubMed:19136951};
DE AltName: Full=HDAg-L-interacting protein NESI;
DE AltName: Full=LMBR1 domain-containing protein 1;
DE AltName: Full=Nuclear export signal-interacting protein;
GN Name=LMBRD1 {ECO:0000312|HGNC:HGNC:23038}; Synonyms=C6orf209, NESI;
GN ORFNames=BM-021, CD001, MSTP044;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION (MICROBIAL INFECTION),
RP TISSUE SPECIFICITY, AND INTERACTION WITH HEPATITIS DELTA VIRUS HDAG-L
RP (MICROBIAL INFECTION).
RX PubMed=15956556; DOI=10.1128/jvi.79.13.8113-8120.2005;
RA Wang Y.-H., Chang S.C., Huang C., Li Y.-P., Lee C.-H., Chang M.-F.;
RT "Novel nuclear export signal-interacting protein, NESI, critical for the
RT assembly of hepatitis delta virus.";
RL J. Virol. 79:8113-8120(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Heart;
RA Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y.,
RA Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y.,
RA Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C.,
RA Zhao M.S., Hui R.T.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Bone marrow;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Placenta, and Substantia nigra;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
RP VAL-395.
RC 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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 130-540 (ISOFORMS 1/3).
RC TISSUE=Pheochromocytoma;
RA Li N., Song H., Peng Y., Xiao H., Han Z., Chen Z.;
RT "A novel gene expressed in human pheochromocytoma.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-531, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP INVOLVEMENT IN MAHCF, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY,
RP GLYCOSYLATION, AND MUTAGENESIS OF ASN-78; ASN-88; ASN-448 AND ASN-457.
RX PubMed=19136951; DOI=10.1038/ng.294;
RA Rutsch F., Gailus S., Miousse I.R., Suormala T., Sagne C., Toliat M.R.,
RA Nuernberg G., Wittkampf T., Buers I., Sharifi A., Stucki M., Becker C.,
RA Baumgartner M., Robenek H., Marquardt T., Hoehne W., Gasnier B.,
RA Rosenblatt D.S., Fowler B., Nuernberg P.;
RT "Identification of a putative lysosomal cobalamin exporter altered in the
RT cblF defect of vitamin B12 metabolism.";
RL Nat. Genet. 41:234-239(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-531, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP FUNCTION, AND INTERACTION WITH ABCD4 AND MMACHC.
RX PubMed=25535791; DOI=10.3109/09687688.2014.990998;
RA Deme J.C., Hancock M.A., Xia X., Shintre C.A., Plesa M., Kim J.C.,
RA Carpenter E.P., Rosenblatt D.S., Coulton J.W.;
RT "Purification and interaction analyses of two human lysosomal vitamin B12
RT transporters: LMBD1 and ABCD4.";
RL Mol. Membr. Biol. 31:250-261(2014).
RN [14]
RP FUNCTION, INTERACTION WITH ABCD4, AND SUBCELLULAR LOCATION.
RX PubMed=27456980; DOI=10.1038/srep30183;
RA Kawaguchi K., Okamoto T., Morita M., Imanaka T.;
RT "Translocation of the ABC transporter ABCD4 from the endoplasmic reticulum
RT to lysosomes requires the escort protein LMBD1.";
RL Sci. Rep. 6:30183-30183(2016).
RN [15]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ABCD4.
RX PubMed=28572511; DOI=10.1074/jbc.m117.784819;
RA Fettelschoss V., Burda P., Sagne C., Coelho D., De Laet C., Lutz S.,
RA Suormala T., Fowler B., Pietrancosta N., Gasnier B., Bornhauser B.,
RA Froese D.S., Baumgartner M.R.;
RT "Clinical or ATPase domain mutations in ABCD4 disrupt the interaction
RT between the vitamin B12-trafficking proteins ABCD4 and LMBD1.";
RL J. Biol. Chem. 292:11980-11991(2017).
RN [16]
RP INTERACTION WITH ABCD4, AND SUBCELLULAR LOCATION.
RX PubMed=33845046; DOI=10.1016/j.jbc.2021.100654;
RA Kitai K., Kawaguchi K., Tomohiro T., Morita M., So T., Imanaka T.;
RT "The lysosomal protein ABCD4 can transport vitamin B12 across liposomal
RT membranes in vitro.";
RL J. Biol. Chem. 296:100654-100654(2021).
CC -!- FUNCTION: Lysosomal membrane chaperone required to export cobalamin
CC (vitamin B12) from the lysosome to the cytosol, allowing its conversion
CC to cofactors (PubMed:19136951). Targets ABCD4 transporter from the
CC endoplasmic reticulum to the lysosome (PubMed:27456980). Then forms a
CC complex with lysosomal ABCD4 and cytoplasmic MMACHC to transport
CC cobalamin across the lysosomal membrane (PubMed:25535791). Acts as an
CC adapter protein which plays an important role in mediating and
CC regulating the internalization of the insulin receptor (INSR) (By
CC similarity). Involved in clathrin-mediated endocytosis of INSR via its
CC interaction with adapter protein complex 2 (By similarity). Essential
CC for the initiation of gastrulation and early formation of mesoderm
CC structures during embryogenesis (By similarity).
CC {ECO:0000250|UniProtKB:Q8K0B2, ECO:0000269|PubMed:19136951,
CC ECO:0000269|PubMed:27456980, ECO:0000303|PubMed:25535791}.
CC -!- FUNCTION: [Isoform 3]: (Microbial infection) May play a role in the
CC assembly of hepatitis delta virus (HDV). {ECO:0000269|PubMed:15956556}.
CC -!- SUBUNIT: [Isoform 3]: (Microbial infection) Interacts with hepatitis
CC delta virus NES (HDAg-L). {ECO:0000269|PubMed:15956556}.
CC -!- SUBUNIT: Interacts with ABCD4; this interaction induces the
CC translocation of ABCD4 from the endoplasmic reticulum to the lysosome
CC (PubMed:27456980,PubMed:28572511,PubMed:33845046). Interacts with ABCD4
CC and MMACHC; this interaction ensures the transport of cobalamin from
CC the lysosome to the cytoplasm (PubMed:25535791). Interacts with INSR,
CC adapter protein complex 2 and clathrin heavy chain (By similarity).
CC {ECO:0000250|UniProtKB:Q8K0B2, ECO:0000269|PubMed:25535791,
CC ECO:0000269|PubMed:27456980, ECO:0000269|PubMed:28572511,
CC ECO:0000269|PubMed:33845046}.
CC -!- INTERACTION:
CC Q9NUN5; O14678: ABCD4; NbExp=7; IntAct=EBI-2805231, EBI-714396;
CC Q9NUN5-4; Q8WWU5-7: TCP11; NbExp=3; IntAct=EBI-17721490, EBI-17721485;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:27456980}. Lysosome membrane
CC {ECO:0000269|PubMed:19136951, ECO:0000269|PubMed:27456980,
CC ECO:0000269|PubMed:28572511, ECO:0000269|PubMed:33845046}; Multi-pass
CC membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000250|UniProtKB:Q8K0B2}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, clathrin-coated vesicle
CC {ECO:0000250|UniProtKB:Q8K0B2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NUN5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NUN5-2; Sequence=VSP_021630, VSP_036540;
CC Name=3; Synonyms=NESI;
CC IsoId=Q9NUN5-3; Sequence=VSP_021629;
CC Name=4;
CC IsoId=Q9NUN5-4; Sequence=VSP_036539, VSP_021630, VSP_036540;
CC -!- TISSUE SPECIFICITY: Isoform 3 is expressed in liver.
CC {ECO:0000269|PubMed:15956556}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19136951}.
CC -!- DISEASE: Methylmalonic aciduria and homocystinuria, cblF type (MAHCF)
CC [MIM:277380]: An autosomal recessive disorder of cobalamin metabolism
CC characterized by decreased levels of the coenzymes adenosylcobalamin
CC (AdoCbl) and methylcobalamin (MeCbl). It is due to accumulation of free
CC cobalamin in lysosomes, thus hindering its conversion to cofactors.
CC Clinical features include developmental delay, stomatitis, glossitis,
CC seizures and methylmalonic aciduria responsive to vitamin B12.
CC {ECO:0000269|PubMed:19136951}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the LIMR family. LMBRD1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK26247.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY136817; AAN11301.1; -; mRNA.
DR EMBL; AF113224; AAG39295.1; -; mRNA.
DR EMBL; AF208863; AAF64277.1; -; mRNA.
DR EMBL; AK002102; BAA92087.1; -; mRNA.
DR EMBL; AK290069; BAF82758.1; -; mRNA.
DR EMBL; AL358133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL583831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48832.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48833.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48835.1; -; Genomic_DNA.
DR EMBL; BC010360; AAH10360.1; -; mRNA.
DR EMBL; BC047073; AAH47073.1; -; mRNA.
DR EMBL; AF211480; AAK26247.1; ALT_FRAME; mRNA.
DR CCDS; CCDS4969.1; -. [Q9NUN5-1]
DR CCDS; CCDS87415.1; -. [Q9NUN5-3]
DR RefSeq; NP_060838.3; NM_018368.3. [Q9NUN5-1]
DR RefSeq; XP_011534243.1; XM_011535941.1.
DR AlphaFoldDB; Q9NUN5; -.
DR SMR; Q9NUN5; -.
DR BioGRID; 120902; 5.
DR IntAct; Q9NUN5; 6.
DR STRING; 9606.ENSP00000359609; -.
DR TCDB; 9.A.54.1.1; the lysosomal cobalamin (b12) transporter (l-b12t) family.
DR GlyConnect; 1628; 11 N-Linked glycans (1 site).
DR GlyGen; Q9NUN5; 7 sites, 11 N-linked glycans (1 site).
DR iPTMnet; Q9NUN5; -.
DR PhosphoSitePlus; Q9NUN5; -.
DR SwissPalm; Q9NUN5; -.
DR BioMuta; LMBRD1; -.
DR DMDM; 74752981; -.
DR EPD; Q9NUN5; -.
DR jPOST; Q9NUN5; -.
DR MassIVE; Q9NUN5; -.
DR MaxQB; Q9NUN5; -.
DR PaxDb; Q9NUN5; -.
DR PeptideAtlas; Q9NUN5; -.
DR PRIDE; Q9NUN5; -.
DR ProteomicsDB; 82696; -. [Q9NUN5-1]
DR ProteomicsDB; 82697; -. [Q9NUN5-2]
DR ProteomicsDB; 82698; -. [Q9NUN5-3]
DR ProteomicsDB; 82699; -. [Q9NUN5-4]
DR Antibodypedia; 17627; 91 antibodies from 24 providers.
DR DNASU; 55788; -.
DR Ensembl; ENST00000370570.6; ENSP00000359602.1; ENSG00000168216.13. [Q9NUN5-3]
DR Ensembl; ENST00000647964.1; ENSP00000496784.1; ENSG00000168216.13. [Q9NUN5-3]
DR Ensembl; ENST00000648168.1; ENSP00000498178.1; ENSG00000168216.13. [Q9NUN5-3]
DR Ensembl; ENST00000648394.1; ENSP00000497302.1; ENSG00000168216.13. [Q9NUN5-3]
DR Ensembl; ENST00000648743.1; ENSP00000497135.1; ENSG00000168216.13. [Q9NUN5-3]
DR Ensembl; ENST00000649028.1; ENSP00000498034.1; ENSG00000168216.13. [Q9NUN5-3]
DR Ensembl; ENST00000649679.1; ENSP00000497387.1; ENSG00000168216.13. [Q9NUN5-3]
DR Ensembl; ENST00000649918.1; ENSP00000497487.1; ENSG00000168216.13. [Q9NUN5-3]
DR Ensembl; ENST00000649934.3; ENSP00000497690.1; ENSG00000168216.13. [Q9NUN5-1]
DR Ensembl; ENST00000650035.1; ENSP00000497703.1; ENSG00000168216.13. [Q9NUN5-3]
DR Ensembl; ENST00000650107.1; ENSP00000497124.1; ENSG00000168216.13. [Q9NUN5-3]
DR GeneID; 55788; -.
DR KEGG; hsa:55788; -.
DR MANE-Select; ENST00000649934.3; ENSP00000497690.1; NM_018368.4; NP_060838.3.
DR UCSC; uc003pez.4; human. [Q9NUN5-1]
DR CTD; 55788; -.
DR DisGeNET; 55788; -.
DR GeneCards; LMBRD1; -.
DR GeneReviews; LMBRD1; -.
DR HGNC; HGNC:23038; LMBRD1.
DR HPA; ENSG00000168216; Low tissue specificity.
DR MalaCards; LMBRD1; -.
DR MIM; 277380; phenotype.
DR MIM; 612625; gene.
DR neXtProt; NX_Q9NUN5; -.
DR OpenTargets; ENSG00000168216; -.
DR Orphanet; 79284; Methylmalonic acidemia with homocystinuria type cblF.
DR PharmGKB; PA134948847; -.
DR VEuPathDB; HostDB:ENSG00000168216; -.
DR eggNOG; ENOG502QQ2T; Eukaryota.
DR GeneTree; ENSGT00390000002581; -.
DR HOGENOM; CLU_028341_1_0_1; -.
DR InParanoid; Q9NUN5; -.
DR OrthoDB; 744771at2759; -.
DR PhylomeDB; Q9NUN5; -.
DR TreeFam; TF329170; -.
DR PathwayCommons; Q9NUN5; -.
DR Reactome; R-HSA-5683329; Defective ABCD4 causes MAHCJ.
DR Reactome; R-HSA-9758881; Uptake of dietary cobalamins into enterocytes.
DR Reactome; R-HSA-9758890; Transport of RCbl within the body.
DR SignaLink; Q9NUN5; -.
DR BioGRID-ORCS; 55788; 11 hits in 1080 CRISPR screens.
DR ChiTaRS; LMBRD1; human.
DR GeneWiki; LMBRD1; -.
DR GenomeRNAi; 55788; -.
DR Pharos; Q9NUN5; Tbio.
DR PRO; PR:Q9NUN5; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9NUN5; protein.
DR Bgee; ENSG00000168216; Expressed in secondary oocyte and 205 other tissues.
DR ExpressionAtlas; Q9NUN5; baseline and differential.
DR Genevisible; Q9NUN5; HS.
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; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
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; IEA:Ensembl.
DR GO; GO:0140318; F:protein transporter activity; IDA:MGI.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISS:UniProtKB.
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; IDA: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 Alternative splicing; Cell membrane; Cobalamin; Cobalt;
KW Cytoplasmic vesicle; Developmental protein; Endocytosis;
KW Endoplasmic reticulum; Gastrulation; Glycoprotein; Host-virus interaction;
KW Lysosome; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..540
FT /note="Lysosomal cobalamin transport escort protein LMBD1"
FT /id="PRO_0000260515"
FT TOPO_DOM 1..10
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..100
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..188
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..364
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..408
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..486
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..507
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..540
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 232..235
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 294..297
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 238
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8K0B2"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:19136951"
FT VAR_SEQ 1..204
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036539"
FT VAR_SEQ 1..73
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11042152,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15956556,
FT ECO:0000303|Ref.2"
FT /id="VSP_021629"
FT VAR_SEQ 362..392
FT /note="VFPLDYILITIIIMYFIFTSMAGIRNIGIWF -> EFEILAYGSFGLDYIKS
FT EEVEPGPKHSFFSA (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021630"
FT VAR_SEQ 393..540
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036540"
FT VARIANT 144
FT /note="T -> A (in dbSNP:rs12214456)"
FT /id="VAR_029047"
FT VARIANT 395
FT /note="I -> V (in dbSNP:rs17854411)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_029048"
FT VARIANT 469
FT /note="D -> E (in dbSNP:rs12648)"
FT /id="VAR_029049"
FT MUTAGEN 78
FT /note="N->Q: Does not affect glycosylation status; when
FT associated with Q-88."
FT /evidence="ECO:0000269|PubMed:19136951"
FT MUTAGEN 88
FT /note="N->Q: Does not affect glycosylation status; when
FT associated with Q-78."
FT /evidence="ECO:0000269|PubMed:19136951"
FT MUTAGEN 448
FT /note="N->Q: Affects glycosylation status; when associated
FT with Q-457."
FT /evidence="ECO:0000269|PubMed:19136951"
FT MUTAGEN 457
FT /note="N->Q: Affects glycosylation status. Affects
FT glycosylation status; when associated with Q-448."
FT /evidence="ECO:0000269|PubMed:19136951"
SQ SEQUENCE 540 AA; 61389 MW; CC7578B0F5FD7BA6 CRC64;
MATSGAASAE LVIGWCIFGL LLLAILAFCW IYVRKYQSRR ESEVVSTITA IFSLAIALIT
SALLPVDIFL VSYMKNQNGT FKDWANANVS RQIEDTVLYG YYTLYSVILF CVFFWIPFVY
FYYEEKDDDD TSKCTQIKTA LKYTLGFVVI CALLLLVGAF VPLNVPNNKN STEWEKVKSL
FEELGSSHGL AALSFSISSL TLIGMLAAIT YTAYGMSALP LNLIKGTRSA AYERLENTED
IEEVEQHIQT IKSKSKDGRP LPARDKRALK QFEERLRTLK KRERHLEFIE NSWWTKFCGA
LRPLKIVWGI FFILVALLFV ISLFLSNLDK ALHSAGIDSG FIIFGANLSN PLNMLLPLLQ
TVFPLDYILI TIIIMYFIFT SMAGIRNIGI WFFWIRLYKI RRGRTRPQAL LFLCMILLLI
VLHTSYMIYS LAPQYVMYGS QNYLIETNIT SDNHKGNSTL SVPKRCDADA PEDQCTVTRT
YLFLHKFWFF SAAYYFGNWA FLGVFLIGLI VSCCKGKKSV IEGVDEDSDI SDDEPSVYSA
