ID A0A090L4H9_STRRB Unreviewed; 331 AA.
AC A0A090L4H9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Bax inhibitor 1-related family and ATPase inhibitor, IATP, mitochondria family-containing protein {ECO:0000313|EMBL:CEF62399.1, ECO:0000313|WBParaSite:SRAE_1000067200.1};
GN ORFNames=SRAE_1000067200 {ECO:0000313|EMBL:CEF62399.1,
GN ECO:0000313|WBParaSite:SRAE_1000067200.1,
GN ECO:0000313|WormBase:SRAE_1000067200};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF62399.1};
RN [1] {ECO:0000313|EMBL:CEF62399.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_1000067200.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF62399.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_1000067200.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the ATPase inhibitor family.
CC {ECO:0000256|ARBA:ARBA00010901}.
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DR EMBL; LN609528; CEF62399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090L4H9; -.
DR STRING; 34506.A0A090L4H9; -.
DR EnsemblMetazoa; SRAE_1000067200.1; SRAE_1000067200.1; WBGene00257269.
DR WBParaSite; SRAE_1000067200.1; SRAE_1000067200.1; WBGene00257269.
DR WormBase; SRAE_1000067200; SRP07764; WBGene00257269; -.
DR eggNOG; ENOG502S4JP; Eukaryota.
DR OrthoDB; 2916243at2759; -.
DR Proteomes; UP000035682; Chromosome X.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0042030; F:ATPase inhibitor activity; IEA:InterPro.
DR Gene3D; 1.20.5.500; Single helix bin; 1.
DR InterPro; IPR007648; ATPase_inhibitor_mt.
DR InterPro; IPR006214; Bax_inhibitor_1-related.
DR PANTHER; PTHR48329; FI01416P; 1.
DR PANTHER; PTHR48329:SF1; FI01416P; 1.
DR Pfam; PF01027; Bax1-I; 1.
DR Pfam; PF04568; IATP; 1.
DR SUPFAM; SSF64602; F1 ATPase inhibitor, IF1, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000035682};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT COILED 284..325
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 331 AA; 38280 MW; 7FE054B6C6650663 CRC64;
MTSSQEFLFL YKNERNIIYS FQSRKRFFMK TTYHTLVFLI FTIITTLLIT MNKKWKIILN
QQHQLFSLIS LVIFLTIYGV IITLEQIRFM RGINYIAAFL LAISLGFLIA VEASWYTLET
NINSIFISCI VAIVISGIAF NMKHDVTIYM NQLIMLTFTF MIMACLLFFL SQKIDTTFLR
HLYALGGFLL SCAYIAIDTQ SISIKNRYNQ LATNEYVLGG VQIYFPKQVK MFGNSTRTAA
RMTTVRMCSN KPKTGGTGTI REAGGAFADM GKAKEDQFFY NLQKEQLKKM HQHLEEEIKN
HKKQAEEHQA AIKRHEEKLK ELRAAAGEYK E
//
