ID A0A3Q1DEH6_AMPOC Unreviewed; 584 AA.
AC A0A3Q1DEH6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Lipase maturation factor {ECO:0000256|RuleBase:RU361229};
GN Name=LMF1 {ECO:0000313|Ensembl:ENSAOCP00000029866.1};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000029866.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000029866.1}
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; A0A3Q1DEH6; -.
DR STRING; 80972.ENSAOCP00000029866; -.
DR Ensembl; ENSAOCT00000031946.1; ENSAOCP00000029866.1; ENSAOCG00000020432.1.
DR GeneTree; ENSGT00530000063702; -.
DR OMA; NFAWLNW; -.
DR Proteomes; UP000257160; 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:UP000257160};
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 63..85
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 111..130
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 142..170
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 301..317
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 379..400
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 66832 MW; 4EB58C824623FCFB CRC64;
MTVTSGNMAT SGEAPDSSVR RRRVGSRRTE TDSVLTGKED EADTSRDSEK QKQLLSLQPG
TYWLTRIVLL RSVAFIYFVA FSVAYNQNKQ LIGEHGLMPC KNYLNSVKRY VGGKIGMAAL
AYTPSLLWFM DWSDMDANLD GIALVGMALS GFVLVTGMAN MIIMVTLWVL YHSLVNVGQL
WYSFGWESQL LETGFLAIFL CPVWTLSQVP RRCPPSLICI WTFRWLIVRI MLGAGLIKIR
GDKCWRDLTC MDYHYETQPV PNPMSYYMHR SPWWFHRFET LSNHFIELIV PFFTFLGRRM
CMVNGALQIL FQVVLIISGN LSFLNWLTIV PSLACFDDAS LGFLFRSGAG PKKMVLEIQN
EDAAGRTLKP NKGMLIRRVV NISLGVLIGF LSVPVVMNLL SSRQVMNTSF DPLRIVNTYG
AFGSITKERT EVIFQGTLSP DPKDPEAVWE EYQFLCKPGD IYRRPCLISP YHYRLDWLMW
FAAFQTYEQS EWVIHIAGCL LSNDSTVLSL LDHNPFHGRD PPRWVRGEHF RYKFSQPGSP
SAAQGKWWLR KRIGPYFPAV DLEGLRGYFQ SRNWPHPHIP TQRS
//
