LMF2_XENLA
ID LMF2_XENLA Reviewed; 707 AA.
AC Q7ZWN0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Lipase maturation factor 2;
GN Name=lmf2;
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 (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the maturation of specific proteins in the
CC endoplasmic reticulum. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the lipase maturation factor family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC046869; AAH46869.1; -; mRNA.
DR RefSeq; NP_001079679.1; NM_001086210.1.
DR AlphaFoldDB; Q7ZWN0; -.
DR DNASU; 379366; -.
DR GeneID; 379366; -.
DR KEGG; xla:379366; -.
DR CTD; 379366; -.
DR Xenbase; XB-GENE-974445; lmf2.L.
DR OrthoDB; 759759at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 379366; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051604; P:protein maturation; IEA:InterPro.
DR InterPro; IPR009613; LMF.
DR PANTHER; PTHR14463; PTHR14463; 1.
DR Pfam; PF06762; LMF1; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..707
FT /note="Lipase maturation factor 2"
FT /id="PRO_0000324514"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 634..654
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 661..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 707 AA; 82267 MW; B37A31482CF5CB92 CRC64;
MGEHRLARSA FLWGLSGIYL FAFVSLYVQI PGLYGREGIL PAWKMLRFTG KGFWEQMKDS
PSLLWFGPRL GLDTEMTMEL ICLLGALLSL GALLFSCLRD SLVFLLLWVF YLSLYQVGQV
FLYFQWDSLL LETGFLAILV APLHAMRWKT SVWSAHDGVT FWLTRWLLFR LMFASGVVKL
TSRCPTWWGL TALTYHYETQ CIPNPAAWYA HQLPVWLQKF SVVATFFIEI GVPWLFFLPF
RRLRLFSFYS QVLLQILIII TGNYNFFNLL TIVLCCSMLD DQHIAFFQRH KKTQHKGGIA
TSAFSLRSLV SLLEIPIFGL LVFWTVKYFD LQINWDKHSL ESRTAFTYHD FQQWLRTITF
PSIWIAAASL GWEILKGMYR SASVRGFFWK LWSTLQWLMF SCAAAAMFTI SLVPYTYMDF
ESNGQLWPEV HQMFNTVDRY QLVNSYGLFR RMTGVGGRPE VVVEGSFDRE TWTEIEFMYK
PGNISTIPTV IVPHQPRLDW QMWFAALSHH SHSPWFASFV YRLLQGNKDV IHLVQNDESL
YPFHANPPTY IRAQQYKYWF TEVDQSGHMP KSWWRRRHVE EFFPAVFLDD PFLDNLLSQH
GLKDKPPARR SLDAPIPFVL KLIRDFLHPL PAPLLLHSFI FGIFTIYFLQ AMFGGVSRPS
VAKQRHSMPP NEKKKQKPNS GQGESASSKS SGHGTDTVRR NKKNEKS