LMBD1_BOVIN
ID LMBD1_BOVIN Reviewed; 543 AA.
AC Q3SYY9;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 72.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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). 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; BC103324; AAI03325.1; -; mRNA.
DR RefSeq; NP_001030264.1; NM_001035092.2.
DR AlphaFoldDB; Q3SYY9; -.
DR SMR; Q3SYY9; -.
DR STRING; 9913.ENSBTAP00000021518; -.
DR PaxDb; Q3SYY9; -.
DR PRIDE; Q3SYY9; -.
DR GeneID; 510495; -.
DR KEGG; bta:510495; -.
DR CTD; 55788; -.
DR eggNOG; ENOG502QQ2T; Eukaryota.
DR InParanoid; Q3SYY9; -.
DR OrthoDB; 744771at2759; -.
DR Proteomes; UP000009136; Unplaced.
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:0005886; C:plasma membrane; ISS:UniProtKB.
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: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; 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; Cytoplasmic vesicle;
KW Developmental protein; Endocytosis; Endoplasmic reticulum; Gastrulation;
KW Glycoprotein; Lysosome; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..543
FT /note="Lysosomal cobalamin transport escort protein LMBD1"
FT /id="PRO_0000260514"
FT TOPO_DOM 1..12
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..102
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..190
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..366
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..410
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 432..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..543
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 234..237
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 296..299
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 240
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8K0B2"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN5"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUN5"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
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 543 AA; 62022 MW; B8741D7E11A63691 CRC64;
MAAAAAGAAS AELVIGWCIF GLLLLAILAF CWIYVRKYQS QRESEVVSTI TAIFSLAIAL
ITSALLPVDI FLVSYMKNQN GTFKDWANGN VSRQIEDTVL YGYYTLYSVI LFCVFFWIPF
VYFYYEEKDD DDTGKCTQVK MALKYTLGFV VICALLLLVG AFVPLNLPDN KNSTEWEKVK
FLFEELGSSH GLAALSFSIS SLTLVGMLAA IIYTAYGMSA LPLNLIKGTR NAAYERLENT
EDIEEVEQHI QTIKSKSKDG RPLPARDRRA LKQFEERLRT LRKRERRLEF IENSWWTKFC
GALRPLKIIW GIFFIFVALL FVISLFLSNL DKALHSAGID SGFIIFGANL SNPLNMLLPL
LQTVFPLDYI LITIIIMYFI FTSMAGIRNI GIWFFWIRLY KIRRGRTRPQ ALLFLCMILL
LIVLHTSYMI YSLAPQYVMY GSQNYLIESN MTYNDHRGNS SLSVPKRCDA DAPEDQCTVT
RTYLFLHKFW FFSAAYYFGN WAFLGVFIVG FIVSCCKGKK SVLERVDEDD SDLSDDEPSL
YSV
