ID   LMF2_RAT                Reviewed;         702 AA.
AC   A1L1J9; Q5I0G9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Lipase maturation factor 2;
GN   Name=Lmf2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung, and Spleen;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Involved in the maturation of specific proteins in the
CC       endoplasmic reticulum. May be required for maturation and transport of
CC       active lipoprotein lipase (LPL) through the secretory pathway (By
CC       similarity). {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}.
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DR   EMBL; BC088333; AAH88333.1; -; mRNA.
DR   EMBL; BC129102; AAI29103.1; -; mRNA.
DR   RefSeq; NP_001073408.1; NM_001079939.1.
DR   AlphaFoldDB; A1L1J9; -.
DR   STRING; 10116.ENSRNOP00000051363; -.
DR   GlyGen; A1L1J9; 1 site.
DR   jPOST; A1L1J9; -.
DR   PaxDb; A1L1J9; -.
DR   PeptideAtlas; A1L1J9; -.
DR   PRIDE; A1L1J9; -.
DR   GeneID; 315218; -.
DR   KEGG; rno:315218; -.
DR   CTD; 91289; -.
DR   RGD; 1306274; Lmf2.
DR   eggNOG; ENOG502QTN6; Eukaryota.
DR   HOGENOM; CLU_020557_1_0_1; -.
DR   InParanoid; A1L1J9; -.
DR   OMA; FMWFQWD; -.
DR   OrthoDB; 759759at2759; -.
DR   PhylomeDB; A1L1J9; -.
DR   TreeFam; TF314339; -.
DR   Reactome; R-RNO-8963889; Assembly of active LPL and LIPC lipase complexes.
DR   PRO; PR:A1L1J9; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000030633; Expressed in lung and 20 other tissues.
DR   Genevisible; A1L1J9; RN.
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   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..702
FT                   /note="Lipase maturation factor 2"
FT                   /id="PRO_0000324512"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        396..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        628..648
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          660..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..679
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        680..696
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        488
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   702 AA;  80254 MW;  387813E87033960A CRC64;
     MASARVPQQL FLQGVAAVYL FAFASLYTQI PGLYGPEGIL PARRTLRPQG KGRWQQLWET
     PTILWEAPRL GLDTAQGLDL LTLLGTVLAL GALLLNSLRH PFIYLLLWAA YLSACQVGQV
     FLYFQWDSLL LETGFLAILV APLRRPSKHK IPQGGLAGAL PHEDLPFWLV RWLLFRLMFA
     SGVVKLTSRC PAWWGLTALT YHYETQCLPT PAAWFAHHLP VWLHRLSVVA TFLIEIAVPP
     LFFAPIRRLR LSAFYAQALL QILIIITGNY NFFNLLTLVL TTALLDDRHL SAEPELRCHK
     KMPTSWPKTL LTSLSLMLEL TVYGLLAYGT IYYFGLEVDW QQQIVLSKTT FTFHQFSQWL
     KMVTLPTVWL GTASLAWELL IALWRWIQVQ GWSRKFFAGI QLSVLGTATV FLFLISLVPY
     SYVEPGTHGR LWTGAHRLFS SVEHLQLANS YGLFRRMTGL GGRPEVVLEG SHDGHHWTEI
     EFMYKPGNVS RPPPFLIPHQ PRLDWQMWFA ALGPHTHSPW FTSLVLRLLQ GKEPVIRLIQ
     NQVANYPFRE QPPTYLRAQR YKYWFSKPGD QSRWWHRQWV EEFFPSVSLG DPTLETLLQQ
     FGLKDKSPPR ARSSKNALAQ TLNWVRAQLS PLEPSILLWG LLGAVVAIRV VRTLLTPRPL
     QSSKQTREEK RKQAPKKDSR AVSEQTAPNS NSNGSWAPRR KK