LMF1_BOVIN
ID LMF1_BOVIN Reviewed; 561 AA.
AC Q0P5C0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Lipase maturation factor 1;
DE AltName: Full=Transmembrane protein 112;
GN Name=LMF1; Synonyms=TMEM112;
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=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the maturation of specific proteins in the
CC endoplasmic reticulum. Required for maturation and transport of active
CC lipoprotein lipase (LPL) through the secretory pathway. Each LMF1
CC molecule chaperones 50 or more molecules of LPL (By similarity).
CC {ECO:0000250|UniProtKB:Q3U3R4, ECO:0000250|UniProtKB:Q96S06}.
CC -!- SUBUNIT: Interacts with LPL and SEL1L. {ECO:0000250|UniProtKB:Q3U3R4}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q3U3R4}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q3U3R4}.
CC -!- SIMILARITY: Belongs to the lipase maturation factor family.
CC {ECO:0000305}.
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DR EMBL; BC120253; AAI20254.1; -; mRNA.
DR RefSeq; NP_001068658.1; NM_001075190.2.
DR AlphaFoldDB; Q0P5C0; -.
DR STRING; 9913.ENSBTAP00000004206; -.
DR PaxDb; Q0P5C0; -.
DR GeneID; 505124; -.
DR KEGG; bta:505124; -.
DR CTD; 64788; -.
DR eggNOG; ENOG502QT4H; Eukaryota.
DR HOGENOM; CLU_020557_2_0_1; -.
DR InParanoid; Q0P5C0; -.
DR OrthoDB; 759759at2759; -.
DR TreeFam; TF314339; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051604; P:protein maturation; IBA:GO_Central.
DR GO; GO:0006641; P:triglyceride metabolic process; ISS:UniProtKB.
DR InterPro; IPR009613; LMF.
DR PANTHER; PTHR14463; PTHR14463; 1.
DR Pfam; PF06762; LMF1; 2.
PE 2: Evidence at transcript level;
KW Chaperone; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..561
FT /note="Lipase maturation factor 1"
FT /id="PRO_0000276738"
FT TOPO_DOM 1..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..120
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..285
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..561
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 561 AA; 64022 MW; 763BD4CF7C2A473D CRC64;
MAAPRESLRR RKAGAGDPEP EAPPGQGRDL KGRPARLRAG TFWLTRIVLL RALAFVYFVA
FLVAFHQNKQ LIGDRGLLPC RAYLQSVQRH FGGRVSWDAL SYAPTILWLL DWSHMDANLD
ALALLGLGIS SFILVSGCAN MVLMAALWVL YMSLVNVGQI WYSFGWESQL LETGFLGIFL
CPLWTLSALP RGTPTSWVVM WGFRWLIFRI MLGAGLIKIR GDRCWRDLTC MDFHYETQPV
PNPVAYFLHR SPWWFHRFET LSNHFLELVV PFFIFLGRRM CIVHGALQVL FQVVLIISGN
LSFLNWLTIV PSLACFDDAT LGGLFPSGPG RLKDQVLKIQ EEETRGARAP RTRGSVARGT
VNLALGILVA WLSIPVVLNL LSPRQVMNSS FNPLRIVNTY GAFGSITRER TEVILQGTAS
ANASAPDSAW EDYEFKCKPG DPRRRPCLIS PYHHRLDWLM WFAAFQTYEH NEWIIHLAGK
LLANDAQALS LLARNPFEGR DPPRWVRGEH YRYKFSRPGG RHAAEGKWWI RRRLGPYFPP
LSRQDLRGYF TSRQWPYPEP E