LMBD1_XENLA
ID LMBD1_XENLA Reviewed; 537 AA.
AC Q7SYR6; Q7ZY17;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 59.
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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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). May play a role in mediating and regulating the
CC internalization of the insulin receptor (By similarity).
CC {ECO:0000250|UniProtKB:Q8K0B2, 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}.
CC -!- SIMILARITY: Belongs to the LIMR family. LMBRD1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH44020.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC044020; AAH44020.1; ALT_FRAME; mRNA.
DR EMBL; BC054294; AAH54294.1; -; mRNA.
DR RefSeq; NP_001082436.1; NM_001088967.2.
DR AlphaFoldDB; Q7SYR6; -.
DR SMR; Q7SYR6; -.
DR DNASU; 398468; -.
DR GeneID; 398468; -.
DR KEGG; xla:398468; -.
DR CTD; 398468; -.
DR Xenbase; XB-GENE-1015713; lmbrd1.L.
DR OMA; IITTFTW; -.
DR OrthoDB; 744771at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 398468; Expressed in muscle tissue and 19 other tissues.
DR GO; GO:0045334; C:clathrin-coated endocytic 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:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0038016; P:insulin receptor internalization; ISS:UniProtKB.
DR GO; GO:0061462; P:protein localization to lysosome; ISS:UniProtKB.
DR InterPro; IPR006876; LMBR1-like_membr_prot.
DR Pfam; PF04791; LMBR1; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cobalamin; Cobalt; Endoplasmic reticulum; Glycoprotein;
KW Lysosome; Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..537
FT /note="Lysosomal cobalamin transport escort protein LMBD1"
FT /id="PRO_0000365819"
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..98
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..186
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..362
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..484
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..537
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
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 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 537 AA; 61110 MW; 8A5D10E5C7EFB7EA CRC64;
MATGSTELLI GWCIFGVLLL AILAFCWVYV RKYQSHQESE VISTITAISS LAIALITSAL
LPVDIFLVSF MKNHNGTFKD WAENNDTRIQ IENTVLIGYY TLYSIILFCV FLWIPFVYFY
YEEKDDTDGS HCSQIGSALK YTSGFVLVCS CLLLIGAFAP LDIPSKANAT ELDKIKLLFQ
NLGSSNGLAA LSFSISSLTL IGMLAAITYT AYGMSALPLN LIKGKRNAHY ERLENSEDIE
EVEQQVENIK SKCKDGRPLS SKDRQALYKL QEKLRTLKRK DRHLEHHENN CWTKCCLVMR
PFKIVWGILF ILVALLFIVS LFLSNLDKAL HSAGINTGFI IFGTNLTNPL NILLPVLQTV
FPLDYIFITT ITMYFIFTSM AGIRNMGIWF FWIRLYKIRR RRTRPQALLF LCMILLLIVL
HTSYMIYSLA PQYVMYGSQK YLWENNSTQE TAIGNSSALV LKDCDASAPE DQCTVTRTYL
FLHKFWFFSS IYYFGNWAFI VVFVIGLIVS CCKGKKSVIE GEVEDDDSDL SDDEDHP
