HAX1_BOVIN
ID HAX1_BOVIN Reviewed; 279 AA.
AC Q2KIE2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=HCLS1-associated protein X-1;
DE AltName: Full=HS1-associating protein X-1;
DE Short=HAX-1;
GN Name=HAX1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Recruits the Arp2/3 complex to the cell cortex and regulates
CC reorganization of the cortical actin cytoskeleton via its interaction
CC with KCNC3 and the Arp2/3 complex. Slows down the rate of inactivation
CC of KCNC3 channels. Promotes GNA13-mediated cell migration. Involved in
CC the clathrin-mediated endocytosis pathway. May be involved in
CC internalization of ABC transporters such as ABCB11. May inhibit CASP9
CC and CASP3. Promotes cell survival. May regulate intracellular calcium
CC pools. {ECO:0000250|UniProtKB:O00165}.
CC -!- SUBUNIT: Interacts with ABCB1, ABCB4 and ABCB11 (By similarity).
CC Directly associates with HCLS1/HS1, through binding to its N-terminal
CC region (By similarity). Interacts with CTTN (By similarity). Interacts
CC with PKD2. Interacts with GNA13. Interacts with CASP9. Interacts with
CC ITGB6. Interacts with PLN and ATP2A2; these interactions are inhibited
CC by calcium. Interacts with GRB7. Interacts (via C-terminus) with
CC XIAP/BIRC4 (via BIR 2 domain and BIR 3 domain) and this interaction
CC blocks ubiquitination of XIAP/BIRC4. Interacts with TPC2. Interacts
CC with KCNC3. Interacts with XPO1 (By similarity). Interacts with RNF217
CC (By similarity). {ECO:0000250|UniProtKB:O00165,
CC ECO:0000250|UniProtKB:Q7TSE9}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O00165}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:O00165}. Nucleus membrane
CC {ECO:0000250|UniProtKB:O00165}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:O35387}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:O00165}. Cell membrane
CC {ECO:0000250|UniProtKB:O00165}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O00165}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O00165}. Sarcoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q7TSE9}. Cytoplasm, P-body
CC {ECO:0000250|UniProtKB:O00165}. Cytoplasm
CC {ECO:0000250|UniProtKB:O00165}. Nucleus {ECO:0000250|UniProtKB:O00165}.
CC Note=Predominantly cytoplasmic. Also detected in the nucleus when
CC nuclear export is inhibited (in vitro). {ECO:0000250|UniProtKB:O00165}.
CC -!- SIMILARITY: Belongs to the HAX1 family. {ECO:0000305}.
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DR EMBL; BC112670; AAI12671.1; -; mRNA.
DR RefSeq; NP_001039418.2; NM_001045953.2.
DR AlphaFoldDB; Q2KIE2; -.
DR STRING; 9913.ENSBTAP00000017314; -.
DR PaxDb; Q2KIE2; -.
DR PRIDE; Q2KIE2; -.
DR GeneID; 506895; -.
DR KEGG; bta:506895; -.
DR CTD; 10456; -.
DR eggNOG; ENOG502S0AE; Eukaryota.
DR InParanoid; Q2KIE2; -.
DR OrthoDB; 1567048at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
DR InterPro; IPR017248; HAX-1.
DR PANTHER; PTHR14938; PTHR14938; 1.
DR PIRSF; PIRSF037634; HS1-associating_X-1; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Cytoplasm; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Membrane; Mitochondrion; Nucleus; Phosphoprotein;
KW Reference proteome; Sarcoplasmic reticulum.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O00165"
FT CHAIN 2..279
FT /note="HCLS1-associated protein X-1"
FT /id="PRO_0000313800"
FT REGION 2..42
FT /note="Required for localization in mitochondria"
FT /evidence="ECO:0000250"
FT REGION 16..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..279
FT /note="Involved in HCLS1 binding"
FT /evidence="ECO:0000250"
FT REGION 175..206
FT /note="Involved in CASP9 binding"
FT /evidence="ECO:0000250"
FT REGION 176..247
FT /note="Involved in GNA13 binding"
FT /evidence="ECO:0000250"
FT REGION 183..279
FT /note="Required for localization in sarcoplasmic reticulum"
FT /evidence="ECO:0000250"
FT REGION 184..279
FT /note="Involved in PKD2 binding"
FT /evidence="ECO:0000250"
FT REGION 203..245
FT /note="Involved in ATP2A2 binding"
FT /evidence="ECO:0000250"
FT REGION 203..225
FT /note="Involved in PLN binding"
FT /evidence="ECO:0000250"
FT REGION 270..279
FT /note="Required for ITGB6 binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 28..42
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 127..128
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O00165"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00165"
SQ SEQUENCE 279 AA; 31415 MW; 0C18E670200C6D9B CRC64;
MSLFDLFRGF FGFSGPRSHR DPFFGGMTRD EDEDDEEEEE EGVTWGRGNS RFEGPQSPEE
FSFGFSFSPG GGMRFHDNFG FDDLVRDFNN IFSEMGAWTL PSRPPELPGP ESETPGERRQ
EGQTLRDSML KYPDSHQPKI FGGGLESDAR SESSKPAPDW GPQRPFHRFD DTWPVTPHSR
AREDNDLDTQ VSQEGLGPVL QPQPKSYFKS VSVTKITKPD GTVEERRTVV DSEGRKETTV
THQEAGSSPR DGPESPTPPS LDDSSSILDL FLGRWFRSR
