LMBD1_CHICK
ID LMBD1_CHICK Reviewed; 539 AA.
AC Q5ZI05;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=RCJMB04_31k18;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720979; CAG32638.1; -; mRNA.
DR RefSeq; NP_001006413.1; NM_001006413.1.
DR AlphaFoldDB; Q5ZI05; -.
DR SMR; Q5ZI05; -.
DR STRING; 9031.ENSGALP00000031013; -.
DR PaxDb; Q5ZI05; -.
DR GeneID; 421874; -.
DR KEGG; gga:421874; -.
DR CTD; 55788; -.
DR VEuPathDB; HostDB:geneid_421874; -.
DR eggNOG; ENOG502QQ2T; Eukaryota.
DR InParanoid; Q5ZI05; -.
DR OrthoDB; 744771at2759; -.
DR PhylomeDB; Q5ZI05; -.
DR PRO; PR:Q5ZI05; -.
DR Proteomes; UP000000539; 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..539
FT /note="Lysosomal cobalamin transport escort protein LMBD1"
FT /id="PRO_0000260519"
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..539
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 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"
SQ SEQUENCE 539 AA; 61675 MW; 2389568E3C8A3FAD CRC64;
MAAAASELLT GWFLFGLALL AILIFSWVYV RKYQSRRESE VISTVTAIFA LAVALISSAL
LPVDIFLVSY MKNQNGTFKD WADANVSRQI EDTVLYGYYT LYSIILFCVF LWIPFVYFYY
EEKEEDDGNT CSQVKTALKY TLGFITVCAV LLLIGAFVPL DIPNKKNSTE WEKVKLLFEE
FGSSHGLTAL SFSISSLTVI GMLAAITYTA YGMSALPLNL IKGTTSAAYE RLENTEDIEE
VEQRILRIKS KCRDGRPLSS RDRRAVQQLE ERLRTLRRRE RHLETIEKSW WLKFCEAIRP
LKIVWGVFFI IVALLFTVSL FLSNLDKALH SAGFDSGFII LGTNLTNPLN MLLPVLQTVF
PLDYILITTI VMYFIFTSMA GIRNMGIWFF WIRLYKIRRG KTRPQALLFL CMILLLIVLH
TSYMIYSLAP QYVMYGSQKY LVQSNKTIDG QPKNVTTFVA KDCDADAPED QCIVTRTYLF
LHKFWFFSAV YYFGNWAFIA VFLIGLIVSC CKGKKSVIEG EVDEDDSDMS DDELSAYYC
