ID A0A2T7PB37_POMCA Unreviewed; 530 AA.
AC A0A2T7PB37;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Lipase maturation factor {ECO:0000256|RuleBase:RU361229};
GN ORFNames=C0Q70_09900 {ECO:0000313|EMBL:PVD30627.1};
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD30627.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD30627.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD30627.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD30627.1};
RA Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA Zhang G., Qian W., Fan W.;
RT "The genome of golden apple snail Pomacea canaliculata provides insight
RT into stress tolerance and invasive adaptation.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the maturation of specific proteins in the
CC endoplasmic reticulum. {ECO:0000256|RuleBase:RU361229}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU361229}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU361229}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the lipase maturation factor family.
CC {ECO:0000256|ARBA:ARBA00005512, ECO:0000256|RuleBase:RU361229}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PVD30627.1}.
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DR EMBL; PZQS01000005; PVD30627.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7PB37; -.
DR STRING; 400727.A0A2T7PB37; -.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg5.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051604; P:protein maturation; IEA:InterPro.
DR InterPro; IPR009613; LMF.
DR PANTHER; PTHR14463; LIPASE MATURATION FACTOR; 1.
DR PANTHER; PTHR14463:SF10; LIPASE MATURATION FACTOR 1; 1.
DR Pfam; PF06762; LMF1; 2.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU361229};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361229};
KW Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361229};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361229}.
FT TRANSMEM 58..75
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 95..116
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 248..271
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 327..348
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
SQ SEQUENCE 530 AA; 60722 MW; A516D7726EB9A742 CRC64;
MSEHAGGTQS AVRKRTTAKP FEDIVAFLVA LHQNKQLIGP NGLLPANLFL DSIKKRMGGL
NFNTIFNVPT IIWMFDYEHN LSTLLDRIAL TGLALSGLVI VLGAANWFIM LTLWVLYHSL
VNVGQRCLFG FAGWESQLLE TGFLATFLCP VWSLRQMPRK TPTSFIIIMG YRWLIFRIML
GAGLIKIRGD KCWRDLTCMN YHYETQPVPN PMSTYMHQAP EAWHKFETLS NHFIELVAPF
LLLMPRPFCL LGGAFQILFQ VVLIISGNLS FLNWLTILPN LACYDDASYS WMFSKRVLKQ
VAELQKSNMN NSTSAPSIDI GMYIRRVFNI GVGLLVAYLS IPVVQNLLSS RQAMNTSFDP
LRLVNTYGAF GSVTKKRTEV IFQGTYSNDP YSPNAVWEEY EFKCKPGNVM RRPCLISPYH
YRLDWLMWFA AFQSFNQNPW LVHLAIKLLA NDEDAVSLIA YNPFAGKQPP KFIRAEHYKY
RYTKLGTNET VGGAWWKRKY IKNYLPPLSM QSAKPILEQM GWKKPKIKQN
//
