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HCLS1-associated protein X-1 (HS1-associating protein X-1) (HAX-1) (HS1-binding protein 1) (HSP1BP-1)

 HAX1_RAT                Reviewed;         278 AA.
Q7TSE9; Q5D1N3; Q5D1N4; Q7TSE7; Q7TSE8;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
23-MAY-2018, entry version 81.
RecName: Full=HCLS1-associated protein X-1;
AltName: Full=HS1-associating protein X-1;
Short=HAX-1;
AltName: Full=HS1-binding protein 1;
Short=HSP1BP-1;
Name=Hax1; Synonyms=Hs1bp1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3; 5 AND 6).
STRAIN=Lewis; TISSUE=Testis;
PubMed=16516414; DOI=10.1016/j.gene.2005.11.035;
Grzybowska E.A., Sarnowska E., Konopinski R., Wilczynska A.,
Sarnowski T.J., Siedlecki J.A.;
"Identification and expression analysis of alternative splice variants
of the rat Hax-1 gene.";
Gene 371:84-92(2006).
[2]
INTERACTION WITH ABCB1; ABCB4; ABCB11 AND CTTN, SUBCELLULAR LOCATION,
AND FUNCTION.
PubMed=15159385; DOI=10.1074/jbc.M404337200;
Ortiz D.F., Moseley J., Calderon G., Swift A.L., Li S., Arias I.M.;
"Identification of HAX-1 as a protein that binds bile salt export
protein and regulates its abundance in the apical membrane of Madin-
Darby canine kidney cells.";
J. Biol. Chem. 279:32761-32770(2004).
[3]
SUBCELLULAR LOCATION, FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE
SPECIFICITY.
PubMed=19913549; DOI=10.1016/j.yjmcc.2009.10.028;
Yap S.V., Vafiadaki E., Strong J., Kontrogianni-Konstantopoulos A.;
"HAX-1: a multifaceted antiapoptotic protein localizing in the
mitochondria and the sarcoplasmic reticulum of striated muscle
cells.";
J. Mol. Cell. Cardiol. 48:1266-1279(2010).
[4]
ALTERNATIVE SPLICING, AND SUBCELLULAR LOCATION (ISOFORM 1).
PubMed=23164465; DOI=10.1111/febs.12066;
Grzybowska E.A., Zayat V., Konopinski R., Trebinska A., Szwarc M.,
Sarnowska E., Macech E., Korczynski J., Knapp A., Siedlecki J.A.;
"HAX-1 is a nucleocytoplasmic shuttling protein with a possible role
in mRNA processing.";
FEBS J. 280:256-272(2013).
-!- FUNCTION: Recruits the Arp2/3 complex to the cell cortex and
regulates reorganization of the cortical actin cytoskeleton via
its interaction with KCNC3 and the Arp2/3 complex. Slows down the
rate of inactivation of KCNC3 channels. Promotes GNA13-mediated
cell migration. Involved in the clathrin-mediated endocytosis
pathway. May be involved in internalization of ABC transporters
such as ABCB11. May inhibit CASP9 and CASP3. Promotes cell
survival. May regulate intracellular calcium pools.
{ECO:0000250|UniProtKB:O00165, ECO:0000269|PubMed:15159385,
ECO:0000269|PubMed:19913549}.
-!- SUBUNIT: Interacts with ABCB1, ABCB4 and ABCB11 (PubMed:15159385).
Directly associates with HCLS1/HS1, through binding to its N-
terminal region (By similarity). Interacts with CTTN
(PubMed:15159385). Interacts with PKD2. Interacts with GNA13.
Interacts with CASP9. Interacts with ITGB6. Interacts with PLN and
ATP2A2; these interactions are inhibited by calcium. Interacts
with GRB7. Interacts (via C-terminus) with XIAP/BIRC4 (via BIR 2
domain and BIR 3 domain) and this interaction blocks
ubiquitination of XIAP/BIRC4. Interacts with TPC2. Interacts with
KCNC3. Interacts with XPO1 (By similarity).
{ECO:0000250|UniProtKB:O00165, ECO:0000269|PubMed:15159385}.
-!- INTERACTION:
O70127:Abcb11; NbExp=5; IntAct=EBI-930005, EBI-930036;
Q08201:Abcb4; NbExp=3; IntAct=EBI-930005, EBI-929988;
Q6PSM0:Mdr1a; NbExp=2; IntAct=EBI-930005, EBI-930055;
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19913549}.
Endoplasmic reticulum {ECO:0000250|UniProtKB:O00165}. Nucleus
membrane {ECO:0000250|UniProtKB:O00165}. Cytoplasmic vesicle
{ECO:0000269|PubMed:15159385}. Cytoplasm, cell cortex
{ECO:0000250|UniProtKB:O00165}. Cell membrane
{ECO:0000250|UniProtKB:O00165}; Peripheral membrane protein
{ECO:0000250|UniProtKB:O00165}; Cytoplasmic side
{ECO:0000250|UniProtKB:O00165}. Sarcoplasmic reticulum
{ECO:0000269|PubMed:19913549}. Cytoplasm, P-body
{ECO:0000250|UniProtKB:O00165}. Cytoplasm
{ECO:0000269|PubMed:23164465}. Nucleus
{ECO:0000250|UniProtKB:O00165}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm
{ECO:0000269|PubMed:23164465}. Nucleus
{ECO:0000250|UniProtKB:O00165}. Note=Predominantly cytoplasmic.
Also detected in the nucleus when nuclear export is inhibited, and
in response to cellular stress caused by arsenite (in vitro).
{ECO:0000250|UniProtKB:O00165}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q7TSE9-1; Sequence=Displayed;
Name=2;
IsoId=Q7TSE9-2; Sequence=VSP_030139;
Name=3;
IsoId=Q7TSE9-3; Sequence=VSP_030137;
Name=5;
IsoId=Q7TSE9-5; Sequence=VSP_030138;
Name=6;
IsoId=Q7TSE9-6; Sequence=VSP_030138, VSP_030139;
-!- TISSUE SPECIFICITY: Present in striated muscles (at protein
level). {ECO:0000269|PubMed:19913549}.
-!- DEVELOPMENTAL STAGE: Abundant in hindlimb and cardiac muscles
throughout embryogenesis (at protein level).
{ECO:0000269|PubMed:19913549}.
-!- SIMILARITY: Belongs to the HAX1 family. {ECO:0000305}.
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EMBL; AY291062; AAP44974.1; -; mRNA.
EMBL; AY291063; AAP44975.1; -; mRNA.
EMBL; AY291064; AAP44976.1; -; mRNA.
EMBL; AY919342; AAX18866.1; -; mRNA.
EMBL; AY919343; AAX18867.1; -; mRNA.
EMBL; DQ286293; ABB91376.1; -; Genomic_DNA.
RefSeq; NP_853658.1; NM_181627.2. [Q7TSE9-1]
UniGene; Rn.185269; -.
IntAct; Q7TSE9; 4.
STRING; 10116.ENSRNOP00000067159; -.
PaxDb; Q7TSE9; -.
PRIDE; Q7TSE9; -.
DNASU; 291202; -.
GeneID; 291202; -.
KEGG; rno:291202; -.
CTD; 10456; -.
RGD; 727960; Hax1.
HOVERGEN; HBG002991; -.
InParanoid; Q7TSE9; -.
KO; K16220; -.
PhylomeDB; Q7TSE9; -.
PRO; PR:Q7TSE9; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0030136; C:clathrin-coated vesicle; IDA:RGD.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
GO; GO:0016529; C:sarcoplasmic reticulum; IDA:CACAO.
InterPro; IPR017248; HAX-1.
PIRSF; PIRSF037634; HS1-associating_X-1; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell membrane; Complete proteome;
Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum; Membrane;
Mitochondrion; Nucleus; Phosphoprotein; Reference proteome;
Sarcoplasmic reticulum.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O00165}.
CHAIN 2 278 HCLS1-associated protein X-1.
/FTId=PRO_0000313801.
REGION 2 43 Required for localization in
mitochondria.
REGION 113 278 Involved in HCLS1 binding. {ECO:0000250}.
REGION 174 205 Involved in CASP9 binding. {ECO:0000250}.
REGION 175 246 Involved in GNA13 binding. {ECO:0000250}.
REGION 182 278 Required for localization in sarcoplasmic
reticulum.
REGION 183 278 Involved in PKD2 binding. {ECO:0000250}.
REGION 202 244 Involved in ATP2A2 binding.
{ECO:0000250}.
REGION 202 224 Involved in PLN binding. {ECO:0000250}.
REGION 269 278 Required for ITGB6 binding.
{ECO:0000250}.
COMPBIAS 30 42 Asp/Glu-rich (highly acidic).
SITE 126 127 Cleavage; by caspase-3. {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:O00165}.
MOD_RES 188 188 Phosphoserine.
{ECO:0000250|UniProtKB:O00165}.
MOD_RES 191 191 Phosphoserine.
{ECO:0000250|UniProtKB:O00165}.
VAR_SEQ 1 26 Missing (in isoform 5 and isoform 6).
{ECO:0000303|PubMed:16516414}.
/FTId=VSP_030138.
VAR_SEQ 1 18 MSVFDLFRGFFGFPGPRS -> MQQGPERRKQWGSGKEDRE
QVIG (in isoform 3).
{ECO:0000303|PubMed:16516414}.
/FTId=VSP_030137.
VAR_SEQ 44 104 Missing (in isoform 2 and isoform 6).
{ECO:0000303|PubMed:16516414}.
/FTId=VSP_030139.
SEQUENCE 278 AA; 31448 MW; 0B49E32FF89CD975 CRC64;
MSVFDLFRGF FGFPGPRSHR DPFFGGMTRD DDDDEDDEEE EDSGAWGRES YAFDGFHPTE
EFGFSFSPRG GMRFHGNFGF DDLVRDFNSI FSEMGAWTLP SHSPELPGPE SETPGVRLRE
GQTLRDSMLK YPDSHQPRIF EGVLESHAKP ESSKPAPDWG SQGPFHRLDD TWPVSPHSRA
REDKDLDSQV SQEGLGPLLQ PQPKSYFKSI SVTKITKPDG TVEEHRTVVD SEGRRETTVT
HQEAHDSSRS DPDPPRSSAL DDPFSILDLL LGRWFRSR


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