ID E9QQ93_MOUSE Unreviewed; 1132 AA.
AC E9QQ93;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Xin actin-binding repeat containing 1 {ECO:0000313|Ensembl:ENSMUSP00000107262.4};
GN Name=Xirp1 {ECO:0000313|Ensembl:ENSMUSP00000107262.4,
GN ECO:0000313|MGI:MGI:1333878};
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 {ECO:0000313|Ensembl:ENSMUSP00000107262.4, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000107262.4, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000107262.4,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000107262.4}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000107262.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Protects actin filaments from depolymerization.
CC {ECO:0000256|ARBA:ARBA00002375}.
CC -!- DOMAIN: Xin repeats bind F-actin. {ECO:0000256|PROSITE-
CC ProRule:PRU00721}.
CC -!- SIMILARITY: Belongs to the Xin family. {ECO:0000256|PROSITE-
CC ProRule:PRU00721}.
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DR AlphaFoldDB; E9QQ93; -.
DR MaxQB; E9QQ93; -.
DR PeptideAtlas; E9QQ93; -.
DR ProteomicsDB; 305748; -.
DR Antibodypedia; 12167; 89 antibodies from 21 providers.
DR Ensembl; ENSMUST00000111635.4; ENSMUSP00000107262.4; ENSMUSG00000079243.6.
DR UCSC; uc009sbw.2; mouse.
DR AGR; MGI:1333878; -.
DR MGI; MGI:1333878; Xirp1.
DR VEuPathDB; HostDB:ENSMUSG00000079243; -.
DR GeneTree; ENSGT00530000063779; -.
DR HOGENOM; CLU_280589_0_0_1; -.
DR OrthoDB; 5351065at2759; -.
DR TreeFam; TF330745; -.
DR BioGRID-ORCS; 22437; 1 hit in 79 CRISPR screens.
DR Proteomes; UP000000589; Chromosome 9.
DR Bgee; ENSMUSG00000079243; Expressed in cardiac muscle of left ventricle and 73 other cell types or tissues.
DR ExpressionAtlas; E9QQ93; baseline and differential.
DR Genevisible; E9QQ93; MM.
DR GO; GO:0030054; C:cell junction; IEA:InterPro.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR InterPro; IPR012510; Actin-binding_Xin_repeat.
DR InterPro; IPR030072; XIRP1/XIRP2.
DR PANTHER; PTHR22591; XIN; 1.
DR PANTHER; PTHR22591:SF2; XIN ACTIN-BINDING REPEAT-CONTAINING PROTEIN 1; 1.
DR Pfam; PF08043; Xin; 10.
DR PROSITE; PS51389; XIN; 12.
PE 1: Evidence at protein level;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00721};
KW Proteomics identification {ECO:0007829|MaxQB:E9QQ93,
KW ECO:0007829|PeptideAtlas:E9QQ93};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT REPEAT 151..166
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 186..201
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 226..241
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 302..317
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 340..355
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 376..391
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 440..455
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 511..526
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 549..564
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 593..608
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 658..673
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 727..742
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
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 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 1018..1051
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"
SQ SEQUENCE 1132 AA; 123665 MW; E72F83F71DB0050A 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 LHPLTLPGPG DPGNIEDMDP ELQQLLACGL GVSVSKTGLV
MQETGQGLVA LTAYSLQPQL TSRAPERSSV QLLASCIDKG DLHSLHSLRW EPPTDPSSGP
ATEESQRVPP TESIIHVTPL DSTMEMGQLR ISGSTPCPPP SRAAGKVVLP NGKPVAQAPL
QEARKKTDIS HAGQKGKAAS GRPEGTIASP LGSGAPDLQE AMQNLRLATA EAQSLHQQVL
SRHPQGSDPV ATSMPVQDVL QASTPATGVT QGSIRPVAGS EARIPAFPRK LL
//
