ID   LMBD1_DANRE             Reviewed;         541 AA.
AC   Q5PR61;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
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; ORFNames=wu:fc08a03, zgc:103471;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (DEC-2004) 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}.
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DR   EMBL; BC086815; AAH86815.1; -; mRNA.
DR   RefSeq; NP_001008612.1; NM_001008612.1.
DR   AlphaFoldDB; Q5PR61; -.
DR   SMR; Q5PR61; -.
DR   STRING; 7955.ENSDARP00000068620; -.
DR   PaxDb; Q5PR61; -.
DR   GeneID; 323720; -.
DR   KEGG; dre:323720; -.
DR   CTD; 55788; -.
DR   ZFIN; ZDB-GENE-041212-36; lmbrd1.
DR   eggNOG; ENOG502QQ2T; Eukaryota.
DR   InParanoid; Q5PR61; -.
DR   OrthoDB; 744771at2759; -.
DR   PhylomeDB; Q5PR61; -.
DR   Reactome; R-DRE-9758881; Uptake of dietary cobalamins into enterocytes.
DR   Reactome; R-DRE-9758890; Transport of RCbl within the body.
DR   PRO; PR:Q5PR61; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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:0005774; C:vacuolar membrane; IBA:GO_Central.
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   GO; GO:0072665; P:protein localization to vacuole; IBA:GO_Central.
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..541
FT                   /note="Lysosomal cobalamin transport escort protein LMBD1"
FT                   /id="PRO_0000365818"
FT   TOPO_DOM        1..11
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..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..101
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..122
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        123..145
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        167..189
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        190..210
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        211..306
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        307..327
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        328..365
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        366..386
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        387..409
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        410..430
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        431..488
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        489..509
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        510..541
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
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        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        348
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        459
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   541 AA;  61565 MW;  7A15444ABC6DD931 CRC64;
     MATPVALLSE SVLGWSIFTV VLLVILAFCW VYIRKYQSRQ ESEVISTITA ICALAIALIT
     SALLPVDIFL VSFMKHPNGT YKEWAANNET RVQIEDTVLY GYYTLYSIIL FCVFLWIPFV
     YFYYEEKDED NNNKCLQVKN ALKYTIGFVI VCSALLLIGT FVPLASPPNQ NSTQWQKVQY
     LFEELGSSHG LAALSFSISS LTLIGMLAVI TYTAYGMSVL PLNLIKGTRS VLYERLENTE
     DTEEVERQID KLKAKCADGR PLSMRDRRNL QDLEDKLQLL HRRGRHLEIA ERNCCNKVGS
     ALRPMKILLG VFFILVALLF FVTLFISNLD KALHSAGIST GFIIFGTNLT NPLNELLLAL
     QPVFPLDYVL ITVITMYFVF TSMAGIRNMG IWFFWIRLYK IRPQRTRPQA LLFLCMILLL
     IVLHTSYMIY SLAPQYVMYG SQKYLLQTPL PTAVPSQSNR SATITKICDA DAPEDQCTVT
     RSYLFLHKFW FFSTIYYFGN WAFLGVFLIG LVVSCCKGKK SVIEGEVDAD DSDFSDDEYV
     H