ID   LMF2_XENTR              Reviewed;         707 AA.
AC   Q0P4Y8; Q569N7;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Lipase maturation factor 2;
GN   Name=lmf2;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) 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. {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; BC092370; AAH92370.1; -; mRNA.
DR   EMBL; BC121839; AAI21840.1; -; mRNA.
DR   RefSeq; NP_001072170.1; NM_001078702.1.
DR   AlphaFoldDB; Q0P4Y8; -.
DR   PaxDb; Q0P4Y8; -.
DR   DNASU; 594899; -.
DR   GeneID; 594899; -.
DR   KEGG; xtr:594899; -.
DR   CTD; 91289; -.
DR   Xenbase; XB-GENE-974438; lmf2.
DR   eggNOG; ENOG502QTN6; Eukaryota.
DR   InParanoid; Q0P4Y8; -.
DR   OrthoDB; 759759at2759; -.
DR   Reactome; R-XTR-8963889; Assembly of active LPL and LIPC lipase complexes.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; 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   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_0000324515"
FT   TRANSMEM        11..31
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        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        256..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        306..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        358..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        398..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        634..654
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          659..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        483
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        80
FT                   /note="M -> L (in Ref. 1; AAH92370)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        143
FT                   /note="V -> L (in Ref. 1; AAH92370)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148
FT                   /note="W -> C (in Ref. 1; AAH92370)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   707 AA;  81968 MW;  99EACFCAA84524B8 CRC64;
     MGEQRLARSS FLWGLSGIYL VAFVSLYAQI PGLYGREGIL PAWKMMRFTG KGFWEQLKDS
     PSLLWFGPRL GLDTEMTMEM ICLLGALLSL GALLFSFLRD SLVFLLLWIF YLSLYQVGQV
     FLYFQWDSLL LETGFLAVLV APVHALRWKT SVWSSHDGVT FWLTRWLLFR LMFASGIVKL
     TSRCPTWWGL TALTYHYETQ CIPNPAAWFA HQLPVWFQKF SVVATYFIEI GVPLLFFLPF
     RRLRLFSFYS QVVLQILIIM TGNYNFFNLL TVVLCCSLLD DQHITFFQRH KKPQHKGGRV
     TSAFSLYSLI SLLDVPIFGL LVFWTVKYFD LQINWEKHSV ESRTAFTYHD FQQWLRTITF
     PTIWIAAASL GWEILKGMYR SASVRGIFWK LWSTLQWVIF SCAAVAMFTI SLVPYTYIDF
     ESNGHLWPEV HRMFNAVDRY QLVNSYGLFR RMTGVGGRPE VIVEGSYDRE TWTEIEFMYK
     PGNISTTPSV IIPHQPRLDW QMWFAALAHN SHSPWFASFV YRLLQGNKDV IHLVQNDESL
     YPFHAYPPTY IRAQLYKYWF TEVDQSGQMP KSWWRRRHVE EFFPAVFLGD PFLDNLLTQH
     GLKDKPPARR SLDAPIPSAL RLIRAFLHPL PAPLLLHSFI FGIFTIYFLQ AMFGGVSKPG
     VAKQRHSKPP NEKKKQKSNS GQGESAAAKS SGHGADTVRR NKKNEKS