ID A0A3Q4HYS6_NEOBR Unreviewed; 581 AA.
AC A0A3Q4HYS6;
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};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000029235.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000029235.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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|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 AlphaFoldDB; A0A3Q4HYS6; -.
DR STRING; 32507.ENSNBRP00000029235; -.
DR Ensembl; ENSNBRT00000029991.1; ENSNBRP00000029235.1; ENSNBRG00000022258.1.
DR GeneTree; ENSGT00530000063702; -.
DR OMA; LGTYHQN; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000022258; Expressed in zone of skin and 6 other cell types or tissues.
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 Reference proteome {ECO:0000313|Proteomes:UP000261580};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 78..97
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 104..125
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 131..148
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 253..280
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 300..321
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 341..363
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
FT TRANSMEM 383..406
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361229"
SQ SEQUENCE 581 AA; 66877 MW; B40DF4E939F694E2 CRC64;
SKMGEVVLPR RMFLWCMAVI YLTAFVSLYV QIPGLYGNEG LLPARWQLRY SGKPLVEQLL
SSPTLLWLGP RLGLDTHTAM ELLCLIGAAL SLAATLVEAF RDSVVFFCLW VLYLSMYEVG
QVFLYFQWDN LLLETGFLCI LVAPLTLIRG SRGVREHDRV TFWLTRWLLF RLMFASGVVK
LTSRCPTWWG LTALTYHYET QCIPTPLAWF AHQLPVCWQK LSMVGAFVIE IAVPFLFFSP
LRRLRLGAFY LQVLLQVFII LSGNYNFFNL LTVTLCLSLL DDRHVYFWLH SKLWSWLCYL
LELVVWALLI VGTIICFDLQ LDTAKKGISS RTAFTYHQFN LFLKTVTIPC IWIGVLSLTW
EMVTSLFRCA CVSGFFKRFW GTVQWTVFAG AAASMFAVSL VPFTFIEYDS NSRLWPGVRQ
AYEMVDRYQV VNSYGLFRRM TGVGGRPEVV IEGSSDGVTW TEIEFMYKPG NLSASPPVLT
PHQPRLDWQM WFAALGPNTQ SPWFTSLMYR LLQGKRDVIE LIQSDVSQYP FHQQPPAYLR
AHRYRYWFTE SKADGSVLSG SPRASLCLPA LKKLHWKHFT A
//