ID A0A3Q3EZ38_KRYMA Unreviewed; 558 AA.
AC A0A3Q3EZ38;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Lipase maturation factor {ECO:0000256|RuleBase:RU361229};
GN Name=LMF1 {ECO:0000313|Ensembl:ENSKMAP00000006842.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000006842.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000006842.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A3Q3EZ38; -.
DR STRING; 37003.ENSKMAP00000006842; -.
DR Ensembl; ENSKMAT00000006954.1; ENSKMAP00000006842.1; ENSKMAG00000005158.1.
DR GeneTree; ENSGT00530000063702; -.
DR OMA; NFAWLNW; -.
DR Proteomes; UP000264800; Unplaced.
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:UP000264800};
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 48..70
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 96..115
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 127..155
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 167..186
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 192..214
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 283..304
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 356..377
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 558 AA; 63700 MW; D9B92F9EAE4D586E CRC64;
MAASSGCSES SVRKRHVDSR RTETERVPSS RDRETGQQRV SFRPGTYWLT RIVLLRSVSF
IYFVAFGVAY NQNKQLIGEN GLTPCKNYLN SVKRYVGGKI GMAALAYTPS VLWFLDWSQM
DANLDGMALV GMALSGFVLV TGTANMLIMV TLWVLYHSLV NVGQLQLLET GFLAIFLCPV
WTLSLVPRHC PPSLICIWTF RWLIVRIMLG AGLIKIRGDK CWTDLTCMDY HYETQPVPNP
MSYYMHRSPW WFHRFETLSN HFIELIAPFF TFLGRRMCMV NGALQIVFQV VLIVSGNLSF
LNWLTIVPSL SCFDDAALGF LFGRGSVAEK AVLEMQKEHA AGRSPKPTKG MLIRRVMNVS
LAVVIGYLSI PVVMNLWSSR QMMNTSFDPL RIVNTYGAFG SITKERTEVI LQGSLSPDPK
APEAVWEEYQ FKCKPGDISR QPCLISPYHY RLDWLMWFAA FQTYEQSEWV IHIAGRLLAN
DTTVLSLLDH NPFQGREPPR WVRGEHFRYK FSQPGSASAA QGKWWIRKRI GAYFPPVDLE
GLRGYFQSRN WPHPHIKS
//
