XIRP1_MOUSE
ID XIRP1_MOUSE Reviewed; 1129 AA.
AC O70373;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Xin actin-binding repeat-containing protein 1;
DE AltName: Full=Cardiomyopathy-associated protein 1;
GN Name=Xirp1; Synonyms=Cmya1, Xin;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Heart muscle;
RX PubMed=10021346; DOI=10.1242/dev.126.6.1281;
RA Wang D.-Z., Reiter R.S., Lin J.L.-C., Wang Q., Williams H.S., Krob S.L.,
RA Schultheiss T.M., Evans S., Lin J.-J.;
RT "Requirement of a novel gene, Xin, in cardiac morphogenesis.";
RL Development 126:1281-1294(1999).
RN [2]
RP SEQUENCE REVISION.
RA Wang D.-Z., Lin J.J.-C.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=12203715; DOI=10.1002/dvdy.10131;
RA Sinn H.W., Balsamo J., Lilien J., Lin J.J.-C.;
RT "Localization of the novel Xin protein to the adherens junction complex in
RT cardiac and skeletal muscle during development.";
RL Dev. Dyn. 225:1-13(2002).
RN [5]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=17766470; DOI=10.1152/ajpheart.00806.2007;
RA Gustafson-Wagner E.A., Sinn H.W., Chen Y.-L., Wang D.-Z., Reiter R.S.,
RA Lin J.L.-C., Yang B., Williamson R.A., Chen J., Lin C.-I., Lin J.J.-C.;
RT "Loss of mXinalpha, an intercalated disk protein, results in cardiac
RT hypertrophy and cardiomyopathy with conduction defects.";
RL Am. J. Physiol. 293:H2680-H2692(2007).
RN [6]
RP INTERACTION WITH CTNNB1 AND ACTIN.
RX PubMed=17925400; DOI=10.1074/jbc.m707639200;
RA Choi S., Gustafson-Wagner E.A., Wang Q., Harlan S.M., Sinn H.W.,
RA Lin J.L.-C., Lin J.J.-C.;
RT "The intercalated disc protein, mXin{alpha}, is capable of interacting with
RT beta-catenin and bundling actin filaments.";
RL J. Biol. Chem. 282:36024-36036(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205; SER-208; SER-213;
RP SER-295; SER-332 AND SER-353, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Protects actin filaments from depolymerization.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with FLNC and VASP (By similarity). Interacts with
CC F-actin and CTNNB1. {ECO:0000250, ECO:0000269|PubMed:17925400}.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000250}. Note=Colocalizes
CC with actin stress fibers. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in heart and skeletal muscle. In heart,
CC present in intercalated disks (at protein level).
CC {ECO:0000269|PubMed:10021346, ECO:0000269|PubMed:17766470}.
CC -!- DEVELOPMENTAL STAGE: At 8 dpc, expression is restricted to cardiogenic
CC cells. At 10 dpc, expressed in heart and rostral somites. At 13.5 dpc,
CC expressed in heart and skeletal muscle (at protein level).
CC {ECO:0000269|PubMed:12203715}.
CC -!- DOMAIN: Xin repeats bind F-actin.
CC -!- DISRUPTION PHENOTYPE: Mice are predisposed to hypertrophic
CC cardiomyopathy, and display abnormal cardiac electrophysiological
CC characteristics, including defects in atrial depolarization and
CC ventricular repolarization. {ECO:0000269|PubMed:17766470}.
CC -!- SIMILARITY: Belongs to the Xin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00721}.
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DR EMBL; AF051945; AAC06023.2; -; mRNA.
DR EMBL; BC117959; AAI17960.1; -; mRNA.
DR EMBL; BC117960; AAI17961.1; -; mRNA.
DR PIR; T14267; T14267.
DR AlphaFoldDB; O70373; -.
DR CORUM; O70373; -.
DR IntAct; O70373; 1.
DR STRING; 10090.ENSMUSP00000107262; -.
DR iPTMnet; O70373; -.
DR PhosphoSitePlus; O70373; -.
DR MaxQB; O70373; -.
DR PaxDb; O70373; -.
DR PeptideAtlas; O70373; -.
DR PRIDE; O70373; -.
DR ProteomicsDB; 297653; -.
DR MGI; MGI:1333878; Xirp1.
DR eggNOG; ENOG502QTAC; Eukaryota.
DR InParanoid; O70373; -.
DR PhylomeDB; O70373; -.
DR PRO; PR:O70373; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O70373; protein.
DR GO; GO:0005912; C:adherens junction; IDA:MGI.
DR GO; GO:0005916; C:fascia adherens; IDA:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0014704; C:intercalated disc; IDA:MGI.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0031005; F:filamin binding; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; ISO:MGI.
DR GO; GO:0055013; P:cardiac muscle cell development; IMP:MGI.
DR GO; GO:0003007; P:heart morphogenesis; ISA:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR GO; GO:0045214; P:sarcomere organization; IMP:MGI.
DR InterPro; IPR012510; Actin-binding_Xin_repeat.
DR InterPro; IPR030072; XIRP1/XIRP2.
DR PANTHER; PTHR22591; PTHR22591; 2.
DR Pfam; PF08043; Xin; 10.
DR PROSITE; PS51389; XIN; 17.
PE 1: Evidence at protein level;
KW Actin-binding; Cell junction; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1129
FT /note="Xin actin-binding repeat-containing protein 1"
FT /id="PRO_0000316984"
FT REPEAT 89..104
FT /note="Xin 1"
FT REPEAT 121..136
FT /note="Xin 2"
FT REPEAT 151..166
FT /note="Xin 3"
FT REPEAT 186..201
FT /note="Xin 4"
FT REPEAT 226..241
FT /note="Xin 5"
FT REPEAT 264..279
FT /note="Xin 6"
FT REPEAT 302..317
FT /note="Xin 7"
FT REPEAT 340..355
FT /note="Xin 8"
FT REPEAT 376..391
FT /note="Xin 9"
FT REPEAT 440..455
FT /note="Xin 10"
FT REPEAT 511..526
FT /note="Xin 11"
FT REPEAT 549..564
FT /note="Xin 12"
FT REPEAT 593..608
FT /note="Xin 13"
FT REPEAT 625..640
FT /note="Xin 14"
FT REPEAT 658..673
FT /note="Xin 15"
FT REPEAT 695..710
FT /note="Xin 16"
FT REPEAT 727..742
FT /note="Xin 17"
FT REGION 1..54
FT /note="Interaction with VASP"
FT /evidence="ECO:0000250"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..636
FT /note="Interaction with CTNNB1"
FT /evidence="ECO:0000269|PubMed:17925400"
FT REGION 567..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1018..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..973
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1129 AA; 123431 MW; FF6CBB5D91409E16 CRC64;
MADAQMQVAP TPTIQMRTEE DLSLPHPSAP EGLPPPPPKE TFSKFQQQRQ ASELRRLYKH
IHPELRKNLE EAVAEDLAEV LGSEEPTEGD VQCMRWIFEN WRLDAIGDHE RPAAREPVSG
GNVQATSRKF EEGSFTNSSD QEPEGLRPSG GDVQAARQMF ETKPLDALRG QEEATQTTMR
EPAATGDVQG TRKLFETRPL DRLGSRPSIQ EQSPLELRSE IQELKGDVKK TVKLFQTEPL
CAIQDAEGTI HEVKAACREE IQSNAVRSAR WLFETRPLDA FNQDPSQVRV IRGISLEEGA
LPDVSATRWI FETQPLDAIR EIEVDEKDFQ PSPDLIPPGP DVQHQRHLFE TCSLDTLKGE
RETEAEVPPK EEVIPGDVRS TLWLFETKPL DAFRDQVQVG HLQRVGHQEG EGLVTECLPS
NGTSVLPLSQ GVPQNDGLKG DVKTFKNLFE TLPLDSIGQG EPSAYGNINR GQNTDSAEQS
QGSDAPVYAM QDSRGQLHAL TSVSREQVVG GDVQGYKWMF ETQPLDTLGR SPSTIDVVRG
ITRQEVVAGD VGTTRWLFET QPLEMIHQQE QQKPEEEEGK GPGGPPPELP KKGDVQTIRW
LFETYPMSEL AEKRESEVTD PVSKAETQSC TWMFGPQSLN PAEGSGEQHL QTSQVPAGDR
QTDRHVFETE SLPASNQSSG RKPVRYCSRV EIPSGQVSRQ KEVFQALEAG KKEVPETTIN
LGSIPTGSVH KFTWLFENCP MGSLAAESIR GDNLQEEQPK GSAGHGTPER QETAAERTLR
TLHATPGILH HGGILMEARG PGELCLAKYV LPSPGQGRPY IRKEELVCGE LPRIVRQVLR
RTDVDQQGLL VQEDTAGQLQ LHPLMLPGPG DPGNIEDMDP ELQQLLACGL GVSVSKTGLV
MQETGQGLVA LTAYSLQPQL TSRAPERSSV QLLASCIDKG DLHSLHSLRW EPPTDPSSGP
ATEESQRVPP TESIIHVTPL DSTMEMGQLR ISGSTPCPPP SRAAGKVVLP NGKPVAQAPL
QEARKKRDIS HAGQKGKAAS GRPEASPLGS GAPDLQEAMQ NLRLATAEAQ SLHQQVLSRH
PQGSDPVATS MPVQDVLQAS TPATGVTQGS IRPVAGSEAR IPAVPRKLL
