ID   XIRP1_DANRE             Reviewed;        2297 AA.
AC   Q5PZ43;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Xin actin-binding repeat-containing protein 1;
DE   AltName: Full=Cardiomyopathy-associated protein 1;
GN   Name=xirp1; Synonyms=cmya1, xin;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Luo J., Liu M., Wu X.;
RT   "A novel gene containing Xin repeat.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-952, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18307296; DOI=10.1021/pr700667w;
RA   Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA   Slijper M., Heck A.J.R.;
RT   "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT   analysis down to a single embryo.";
RL   J. Proteome Res. 7:1555-1564(2008).
CC   -!- FUNCTION: Protects actin filaments from depolymerization.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with F-actin, FLNC and VASP. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000250}. Note=Colocalizes
CC       with actin stress fibers. {ECO:0000250}.
CC   -!- DOMAIN: Xin repeats bind F-actin. {ECO:0000255|PROSITE-
CC       ProRule:PRU00721}.
CC   -!- SIMILARITY: Belongs to the Xin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00721}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY812746; AAV68693.1; -; mRNA.
DR   RefSeq; NP_001012377.1; NM_001012377.1.
DR   RefSeq; XP_009296785.1; XM_009298510.1.
DR   AlphaFoldDB; Q5PZ43; -.
DR   SMR; Q5PZ43; -.
DR   STRING; 7955.ENSDARP00000042412; -.
DR   iPTMnet; Q5PZ43; -.
DR   PaxDb; Q5PZ43; -.
DR   PRIDE; Q5PZ43; -.
DR   Ensembl; ENSDART00000042413; ENSDARP00000042412; ENSDARG00000030722.
DR   GeneID; 497637; -.
DR   KEGG; dre:497637; -.
DR   CTD; 165904; -.
DR   ZFIN; ZDB-GENE-050221-2; xirp1.
DR   eggNOG; ENOG502QTAC; Eukaryota.
DR   GeneTree; ENSGT00530000063779; -.
DR   HOGENOM; CLU_001095_0_0_1; -.
DR   InParanoid; Q5PZ43; -.
DR   OMA; KTSLWLF; -.
DR   OrthoDB; 34408at2759; -.
DR   PhylomeDB; Q5PZ43; -.
DR   TreeFam; TF330745; -.
DR   PRO; PR:Q5PZ43; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 2.
DR   Bgee; ENSDARG00000030722; Expressed in cardiac ventricle and 21 other tissues.
DR   ExpressionAtlas; Q5PZ43; baseline.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   InterPro; IPR012510; Actin-binding_Xin_repeat.
DR   InterPro; IPR030072; XIRP1/XIRP2.
DR   PANTHER; PTHR22591; PTHR22591; 1.
DR   Pfam; PF08043; Xin; 15.
DR   PROSITE; PS51389; XIN; 26.
PE   1: Evidence at protein level;
KW   Actin-binding; Cell junction; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..2297
FT                   /note="Xin actin-binding repeat-containing protein 1"
FT                   /id="PRO_0000316986"
FT   REPEAT          104..119
FT                   /note="Xin 1"
FT   REPEAT          139..154
FT                   /note="Xin 2"
FT   REPEAT          169..184
FT                   /note="Xin 3"
FT   REPEAT          208..223
FT                   /note="Xin 4"
FT   REPEAT          248..263
FT                   /note="Xin 5"
FT   REPEAT          286..301
FT                   /note="Xin 6"
FT   REPEAT          323..338
FT                   /note="Xin 7"
FT   REPEAT          362..377
FT                   /note="Xin 8"
FT   REPEAT          396..411
FT                   /note="Xin 9"
FT   REPEAT          464..479
FT                   /note="Xin 10"
FT   REPEAT          494..509
FT                   /note="Xin 11"
FT   REPEAT          532..547
FT                   /note="Xin 12"
FT   REPEAT          570..585
FT                   /note="Xin 13"
FT   REPEAT          605..620
FT                   /note="Xin 14"
FT   REPEAT          638..653
FT                   /note="Xin 15"
FT   REPEAT          677..692
FT                   /note="Xin 16"
FT   REPEAT          715..730
FT                   /note="Xin 17"
FT   REPEAT          747..762
FT                   /note="Xin 18"
FT   REPEAT          779..794
FT                   /note="Xin 19"
FT   REPEAT          818..833
FT                   /note="Xin 20"
FT   REPEAT          856..871
FT                   /note="Xin 21"
FT   REPEAT          893..908
FT                   /note="Xin 22"
FT   REPEAT          928..943
FT                   /note="Xin 23"
FT   REPEAT          959..974
FT                   /note="Xin 24"
FT   REPEAT          997..1012
FT                   /note="Xin 25"
FT   REPEAT          1033..1048
FT                   /note="Xin 26"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          433..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1617..1680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1866..1900
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2147..2191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2243..2297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1617..1659
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1866..1885
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1886..1900
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2159..2184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2243..2281
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         952
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18307296"
SQ   SEQUENCE   2297 AA;  258390 MW;  868881EE077B2D3E CRC64;
     MAEVAKQKKA TEAVCGDEDF PPPPPPLPRP QVLESLQKDL SQNFLPVPPP KETFSEIYQQ
     RQKSELKRLF KHIHPELKMT VDDVVDDELI DAINPQAADA AYQGEVQSMR WIFENWTLDN
     IGDPHETKKL LCEENPQGGD VKGKSSLFEH STFDSQHAAG AERAGVVRGD VRTATWLFET
     QPLDSISKSK IEDEEIVEVV LKEPVQKGDV TGARRLFETK PLDSLGRCCS VEDQHFLTLK
     SELQENKGDV KKTVKLFQAD PCCALRDSNG KIHEIKSICR EEIMSSDFKT ARWLFETQPL
     DHINEGAHVQ IIRGISLEEA QRGGVDKKKW MFETQPLDAI HEGVVEEQKF QGTAVEGFSG
     AADVHNKLQL FENQPLSSLK GDSEGDVLEK EAIVGGNVGS TLWLFETQPM DTLKDSYEVG
     RLQKVMVSSD EKGEVQDKRM QFEKSTAGKT AGDSGNKVQN DEKGDVKTFK SLFETLPLNV
     SEKAQSQIHD ITSGDVKGHC SLFETTPLYA IKDCAGKFHE VTTVSREECI KGNVQNYKWM
     FETRPLDQFE EGSGKVELIK GITRQEDMTD DTRTAKWMFE TQPLDCMSLN SRTDVDSTQK
     EFKKSNVKTC KWLFETKPMD MLYEKSEGKQ DVEPVPKADV KSHTWLFETQ PLDNIKDKEN
     LGLKLCSTVQ EDVKSDVNVK TVKHLFETEP LDRITDQADS GQNVRCVSQV DMQSGDVSRV
     KEIFESKSLG TESSKWSEEQ KNEIQSGSVH KFTWLFENQP IGDINEKEER IVSCDVEAGD
     VGGKKFIFET LSLDKIKDKD ELLEHPSMII EKPLSSSVNV KSNTMLFESQ PLYAIRDKDG
     QFHEVTTVMK EEVMRGDVRG ARWMFETKPL DTIQADKEIY VIRAVTQEDV HKGDVKSARW
     KFETQPLDSF TPHEGPSVRV VEDIGNEKCV QQSRQLFETE QASQKKFVRM VSVTDVQQGD
     VRTSTWLFEN QPIDTLKGEP DEQNNLTAVH REDNTKGDVK RCTWLFESQS LDKIKDNKPT
     EELVSSREEI PKADVKSTTW LFETTPLDKI TVESVTDILY RLCHNSFIHS SGIIIQANDY
     KYVNMAKYQI MKDEGPKVLK EEVVEGNIRN LMLQLLFKPN IKPMVVLLKE DEQGKMHSTV
     LEIPFQQPGS ATNPEAECKT QEAVKIIENL LVQQKEIKTG LVMQESEGGQ PEMTVYSLHC
     ESSLTESQTI TRGDVKSTIG NLLATVHSQQ TKQSCRMEEI ERGNVNLYKS CIEKGDLKSL
     QRELSEEDLV TSCRDQIEIV QGDVKEAMRH LSQQREQVER TILDVVPGDV KNVKKVFSDV
     CTDLSIGNCV PREEIVRGDI LSAKQQLGEA VKQQVMVQKE EIVSGDIKAT LESLERAKQQ
     SMQVEREVIK PGTIYDLNVE AEEMCSEENE SKLVKEEIIP GDIKAAKRSL ERAKNQSMKV
     EREPITPGKL YNLNETSQCQ SSTTVEQSTT STYSNHRITT TFRKVSDIEK DQESIKRLCC
     LNEVGGGGKN IYINTEDALR MVDISESVPD VVKGDVKATI QSLRSASTEQ RSVDREEIVR
     GNMQETLQCL KKSSINISRG DYKAAMLYKQ SGQPYTQSKI TNDSGTKDCK QSFDHIPSSH
     TQLSSSVSVT RSEHPTSLAL NSESVSSNAD NSKNSSAFTG KDEHPPPILP KTGHQVKDQK
     PVIPPKPLHI TTSSPPLFTE TSNMCPNSTV SINDTQQTPA IPLKVTPSNK MFTHETEIAK
     TSNKIKDKES KIHEQVQRTN LTDPTDFQRM QYTEQWVQNS HMQITDTPSV NKTDSFKNGS
     FPGDSIGMEK NVVQRINAAE EIRMCYSKDN DELNKGFKAV LQNFGEKKTT TDTGSPFPKK
     IKVVQKENIQ EQAKTSNKDE LHFTSRDTSS TPNKHEVPSI HNNSENKVVL REKKAKRETE
     DERRQRLSIH RDEIMRGNVK AAMEIFENLM RREELKVILS KVQEIEGETF EVDVRSLKTL
     FENVPAWITN PKENTKRRHR PRVAKETEGL RDDLESISSV EAAFEDLEKA SMDIVNLKEQ
     TLAKLLDIEE AIKKALYSVS NLKSEADIAG LSGLFSESLS PDNVSPSTKN IRKISIVSSK
     TKPAQSNQMQ SADNRALYKE VPHVPQVQVS KQSSNVPSSP SFISIHSAAR KPAESPTDKP
     KTNADQSNAG SSSSQNSSAS HICSPPSPRR KVSVLEVQRV PEVPSGIFGT KTVSEKYEET
     DCFGNTYYSS KRSTFVTRQS ETELSSSYDV VTSPRRSEGM TSPVLQRSGQ SFSSNSLSKG
     KDRKVFVTFG HPNTEKH