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

 HAX1_MOUSE              Reviewed;         280 AA.
O35387; Q542F8;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
07-NOV-2018, entry version 149.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Watanabe T., Takeshita H.;
"Mouse HAX-1 short form (HAX-1s).";
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH PKD2 AND CTTN, AND SUBCELLULAR LOCATION.
PubMed=10760273; DOI=10.1073/pnas.97.8.4017;
Gallagher A.R., Cedzich A., Gretz N., Somlo S., Witzgall R.;
"The polycystic kidney disease protein PKD2 interacts with Hax-1, a
protein associated with the actin cytoskeleton.";
Proc. Natl. Acad. Sci. U.S.A. 97:4017-4022(2000).
[5]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16814492; DOI=10.1016/j.gene.2006.04.027;
Hippe A., Bylaite M., Chen M., von Mikecz A., Wolf R., Ruzicka T.,
Walz M.;
"Expression and tissue distribution of mouse Hax1.";
Gene 379:116-126(2006).
[6]
DISRUPTION PHENOTYPE.
PubMed=18288109; DOI=10.1038/nature06604;
Chao J.R., Parganas E., Boyd K., Hong C.Y., Opferman J.T., Ihle J.N.;
"Hax1-mediated processing of HtrA2 by Parl allows survival of
lymphocytes and neurons.";
Nature 452:98-102(2008).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
INTERACTION WITH KCNC3.
PubMed=26997484; DOI=10.1016/j.cell.2016.02.009;
Zhang Y., Zhang X.F., Fleming M.R., Amiri A., El-Hassar L.,
Surguchev A.A., Hyland C., Jenkins D.P., Desai R., Brown M.R.,
Gazula V.R., Waters M.F., Large C.H., Horvath T.L., Navaratnam D.,
Vaccarino F.M., Forscher P., Kaczmarek L.K.;
"Kv3.3 channels bind Hax-1 and Arp2/3 to assemble a stable local actin
network that regulates channel gating.";
Cell 165:434-448(2016).
-!- 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}.
-!- SUBUNIT: Interacts with ABCB1, ABCB4 and ABCB11 (By similarity).
Directly associates with HCLS1/HS1, through binding to its N-
terminal region (By similarity). Interacts with CTTN
(PubMed:10760273). Interacts with PKD2(PubMed:10760273). 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 (PubMed:26997484). Interacts with XPO1 (By similarity).
{ECO:0000250|UniProtKB:O00165, ECO:0000250|UniProtKB:Q7TSE9,
ECO:0000269|PubMed:10760273}.
-!- INTERACTION:
Q8BWG8:Arrb1; NbExp=6; IntAct=EBI-642449, EBI-641778;
Q9JIY5:Htra2; NbExp=3; IntAct=EBI-642449, EBI-2365838;
Q13563:PKD2 (xeno); NbExp=3; IntAct=EBI-642449, EBI-7813714;
P42227:Stat3; NbExp=11; IntAct=EBI-642449, EBI-602878;
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16814492}.
Endoplasmic reticulum {ECO:0000269|PubMed:10760273}. Nucleus
membrane {ECO:0000305|PubMed:16814492}. Cytoplasmic vesicle
{ECO:0000269|PubMed:10760273, ECO:0000269|PubMed:16814492}.
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:0000250|UniProtKB:Q7TSE9}. Cytoplasm, P-body
{ECO:0000250|UniProtKB:O00165}. Cytoplasm
{ECO:0000250|UniProtKB:O00165}. Nucleus
{ECO:0000250|UniProtKB:O00165}. Note=Predominantly cytoplasmic.
Also detected in the nucleus when nuclear export is inhibited (in
vitro). {ECO:0000250|UniProtKB:O00165}.
-!- TISSUE SPECIFICITY: Ubiquitous, with highest levels in kidney and
liver (at protein level). {ECO:0000269|PubMed:16814492}.
-!- DISRUPTION PHENOTYPE: Mice lacking Hax1 fail to survive longer
than 14 weeks, due to a loss of motor coordination and activity,
leading to failure to eat and drink. They display extensive
apoptosis of neurons in the striatum and cerebellum, and a loss of
lymphocytes in spleen, bone marrow and thymus.
{ECO:0000269|PubMed:18288109}.
-!- SIMILARITY: Belongs to the HAX1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF023482; AAB81081.1; -; mRNA.
EMBL; AK002256; BAB21969.1; -; mRNA.
EMBL; AK010633; BAB27077.1; -; mRNA.
EMBL; AK088746; BAC40544.1; -; mRNA.
EMBL; BC006688; AAH06688.1; -; mRNA.
EMBL; BC098225; AAH98225.1; -; mRNA.
CCDS; CCDS17519.1; -.
RefSeq; NP_035956.1; NM_011826.4.
UniGene; Mm.256035; -.
UniGene; Mm.416677; -.
ProteinModelPortal; O35387; -.
BioGrid; 204783; 16.
CORUM; O35387; -.
DIP; DIP-49445N; -.
IntAct; O35387; 21.
STRING; 10090.ENSMUSP00000078661; -.
iPTMnet; O35387; -.
PhosphoSitePlus; O35387; -.
EPD; O35387; -.
MaxQB; O35387; -.
PaxDb; O35387; -.
PRIDE; O35387; -.
Ensembl; ENSMUST00000079724; ENSMUSP00000078661; ENSMUSG00000027944.
GeneID; 23897; -.
KEGG; mmu:23897; -.
UCSC; uc008qaj.2; mouse.
CTD; 10456; -.
MGI; MGI:1346319; Hax1.
eggNOG; ENOG410IJQ0; Eukaryota.
eggNOG; ENOG411211U; LUCA.
GeneTree; ENSGT00390000018324; -.
HOGENOM; HOG000090247; -.
HOVERGEN; HBG002991; -.
InParanoid; O35387; -.
KO; K16220; -.
OMA; GSQRPFH; -.
OrthoDB; EOG091G0MK9; -.
PhylomeDB; O35387; -.
TreeFam; TF328619; -.
PRO; PR:O35387; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000027944; Expressed in 21 organ(s), highest expression level in female gonad.
CleanEx; MM_HAX1; -.
ExpressionAtlas; O35387; baseline and differential.
Genevisible; O35387; MM.
GO; GO:0015629; C:actin cytoskeleton; IDA:BHF-UCL.
GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0030027; C:lamellipodium; IDA:BHF-UCL.
GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
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.
GO; GO:0005667; C:transcription factor complex; ISO:MGI.
GO; GO:0019966; F:interleukin-1 binding; ISO:MGI.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:MGI.
GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; ISO:MGI.
GO; GO:0030854; P:positive regulation of granulocyte differentiation; ISO:MGI.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0030833; P:regulation of actin filament polymerization; ISO:MGI.
InterPro; IPR017248; HAX-1.
PANTHER; PTHR14938; PTHR14938; 1.
PIRSF; PIRSF037634; HS1-associating_X-1; 1.
1: Evidence at protein level;
Acetylation; 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 2 280 HCLS1-associated protein X-1.
/FTId=PRO_0000083907.
REGION 2 45 Required for localization in
mitochondria. {ECO:0000250}.
REGION 115 280 Involved in HCLS1 binding. {ECO:0000250}.
REGION 176 207 Involved in CASP9 binding. {ECO:0000250}.
REGION 177 248 Involved in GNA13 binding. {ECO:0000250}.
REGION 184 280 Required for localization in sarcoplasmic
reticulum. {ECO:0000250}.
REGION 185 280 Involved in PKD2 binding.
REGION 204 246 Involved in ATP2A2 binding.
{ECO:0000250}.
REGION 204 226 Involved in PLN binding. {ECO:0000250}.
REGION 271 280 Required for ITGB6 binding.
{ECO:0000250}.
COMPBIAS 30 44 Asp/Glu-rich (highly acidic).
SITE 128 129 Cleavage; by caspase-3. {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:O00165}.
MOD_RES 190 190 Phosphoserine.
{ECO:0000250|UniProtKB:O00165}.
MOD_RES 193 193 Phosphoserine.
{ECO:0000250|UniProtKB:O00165}.
SEQUENCE 280 AA; 31654 MW; 3123979BA10B45D1 CRC64;
MSVFDLFRGF FGFPGPRSHR DPFFGGMTRD DDDDDDDDDE AEEDRGAWGR ESYAFDGSQP
PEEFGFSFSP RGGMRFHGNF GFDDLVRDFN SIFSEMGAWT LPSHSPELPG PESETPGERL
REGQTLRDSM LKYPDSHQPR IFEGVLESHA KPESPKPAPD WGSQGPFHRL DDTWPVSPHS
RAKEDKDLDS QVSQEGLGPL LQPQPKSYFK SISVTKITKP DGTVEERRTV VDSEGRRETT
VTHQEAHDSS RSDPDSQRSS ALDDPFSILD LLLGRWFRSR


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