Q8SQ43 (Q8SQ43_FELCA) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Bax-protein EMBL BAB85810.1

Gene names

Name:

bax EMBL BAB85810.1

Organism

Felis catus (Cat) (Felis silvestris catus) EMBL BAB85810.1

Taxonomic identifier

9685 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Carnivora › Feliformia › Felidae › Felinae › Felis

Protein attributes

Sequence length	192 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

Ontologies

Gene Ontology (GO)
Biological_process	B cell apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c Inferred from sequence or structural similarity. Source: UniProtKB apoptotic DNA fragmentation Inferred from sequence or structural similarity. Source: UniProtKB cleavage of lamin involved in execution phase of apoptosis Inferred from sequence or structural similarity. Source: UniProtKB establishment or maintenance of transmembrane electrochemical gradient Inferred from sequence or structural similarity. Source: UniProtKB induction of apoptosis Inferred from sequence or structural similarity. Source: HGNC intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial fragmentation involved in apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial fusion Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of protein binding Inferred from sequence or structural similarity. Source: UniProtKB nuclear fragmentation involved in apoptotic nuclear change Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of endoplasmic reticulum unfolded protein response Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of intrinsic apoptotic signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of neuron apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of protein oligomerization Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of release of cytochrome c from mitochondria Inferred from sequence or structural similarity. Source: UniProtKB protein homooligomerization Inferred from sequence or structural similarity. Source: HGNC regulation of mitochondrial membrane potential Inferred from sequence or structural similarity. Source: UniProtKB regulation of protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB release of cytochrome c from mitochondria Inferred from sequence or structural similarity. Source: UniProtKB release of matrix enzymes from mitochondria Inferred from sequence or structural similarity. Source: UniProtKB response to toxin Inferred from sequence or structural similarity. Source: UniProtKB retinal cell apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB transformed cell apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	BAX complex Inferred from sequence or structural similarity. Source: UniProtKB cytosol Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial permeability transition pore complex Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	BH3 domain binding Inferred from sequence or structural similarity. Source: UniProtKB channel activity Inferred from sequence or structural similarity. Source: UniProtKB lipid binding Inferred from sequence or structural similarity. Source: UniProtKB protein homodimerization activity Inferred from sequence or structural similarity. Source: HGNC
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q8SQ43 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 852D271AE86923FB	FASTA	192	21,284
	10 20 30 40 50 60 MDGSGEQPRG GGHTSSEQIM KTGALLLQGF IQDRAGRMGG ETPELALEQV PQDASTKKLS 70 80 90 100 110 120 ECLKRIGDEL DSNMELQRMI AAVDTDSPRE VFFRVAAEMF SDGNFNWGRV VALFYFASKL 130 140 150 160 170 180 VLKALCTKVP ELIRTIMGWT LDFLRERLLG WIQDQGGWDG LLSYFGTPTW QTVTIFVAGV 190 LTASLAIWKK MG

References

[1]	"molecular cloning of feline bcl-2 family." Yamazaki J., Oguma K., Kano R., Hasegawa A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB080724 mRNA. Translation: BAB85810.1.
RefSeq	NP_001009282.1. NM_001009282.1.
3D structure databases
HSSP	HSSP built from PDB template 1F16 based on UniProtKB Q07812.
ProteinModelPortal	Q8SQ43.
SMR	Q8SQ43. Positions 1-192.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	493837.
KEGG	fca:493837.
Organism-specific databases
CTD	581.
Phylogenomic databases
HOGENOM	HOG000095178.
HOVERGEN	HBG003606.
KO	K02159.
Family and domain databases
InterPro	IPR026304. BAX. IPR002475. Bcl2-like. IPR020717. Bcl2_BH1_motif_CS. IPR020726. Bcl2_BH2_motif_CS. IPR020728. Bcl2_BH3_motif_CS. IPR026298. Blc2_fam. [Graphical view]
PANTHER	PTHR11256. PTHR11256. 1 hit. PTHR11256:SF9. PTHR11256:SF9. 1 hit.
Pfam	PF00452. Bcl-2. 1 hit. [Graphical view]
PRINTS	PR01862. BCL2FAMILY.
PROSITE	PS50062. BCL2_FAMILY. 1 hit. PS01080. BH1. 1 hit. PS01258. BH2. 1 hit. PS01259. BH3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q8SQ43_FELCA

Accession

Primary (citable) accession number: Q8SQ43

Entry history

Integrated into UniProtKB/TrEMBL:	June 1, 2002
Last sequence update:	June 1, 2002
Last modified:	April 3, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)