ID A0A077ZHQ6_TRITR Unreviewed; 543 AA.
AC A0A077ZHQ6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Lipase maturation factor {ECO:0000256|RuleBase:RU361229};
GN ORFNames=TTRE_0000827401 {ECO:0000313|EMBL:CDW59927.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW59927.1};
RN [1] {ECO:0000313|EMBL:CDW59927.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW59927.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT "The whipworm genome and dual-species transcriptomics of an intimate host-
RT pathogen interaction.";
RL Submitted (MAR-2014) 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|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU361229}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
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}.
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DR EMBL; HG806789; CDW59927.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077ZHQ6; -.
DR STRING; 36087.A0A077ZHQ6; -.
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:SF5; LIPASE MATURATION FACTOR 2; 1.
DR Pfam; PF06762; LMF1; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU361229};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361229};
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 24..42
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 49..67
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 73..91
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 103..126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 196..224
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 244..266
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 287..308
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
SQ SEQUENCE 543 AA; 62679 MW; EB6BD888CA8CCBE5 CRC64;
MGNLPTILHL SEMVSLSPSE AMEAGLLVGM LVAGLSFTFV LLRNTFSYLV LWYLYLSFVQ
VGGDFLYFQW DTLLLEAGFL AVLLAPVRIL RRPSTKWLPQ DNVTLFLFRW LGFRLMFASG
VVKLLIQDQT WWTLTALHYH FNSQCIPTPL AWYAHQLPGF VKQFSVAATF VILIFLSLFM
LSPSKHLRYV AFGGQTLLMV LIALTGNYNF FNFLCVVICS SALVDSSFSR TDIELAKFHP
NVTRYLPWVM LLGITMFFSE VIAAMLRLRS DFKKEKIFKR IWYGFQCTLI CIMATAVFSV
SLVPLTFIDR FTWDHIPQQL KDAHEATEKY HIAHSYGLFA SMTGVGGRPE IVLEGANKIN
GTWKEYNFLY KPGAPYRRPP IVEPHQPRLD WQMWFASLTN SFREMPWFLS MTHKLLKQSK
PVMKLIDKSP FEKPPKYIRA TLYTYNFTNW DDLRNDWWTR KAKKEFMPPT SVDNGDLLQY
LKENNLIVEK TVKRPQNSMA SRFLQAARQF SDHFSGVQFV YGITCTVLAP VLVPKVISKK
AHV
//
