XIRP2_RAT
ID XIRP2_RAT Reviewed; 3302 AA.
AC Q71LX6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Xin actin-binding repeat-containing protein 2;
DE AltName: Full=Beta-xin;
DE AltName: Full=Cardiomyopathy-associated protein 3;
DE AltName: Full=L-NAME-induced actin cytoskeletal protein;
GN Name=Xirp2; Synonyms=Cmya3, Xin2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar Kyoto;
RA Inoue S., Egashira K., Koike G., Takeshita A.;
RT "Identification of a novel gene involved in the pathogenesis of cardiac
RT hypertrophy in rats.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1930 AND SER-1935, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-565; SER-633; SER-1210;
RP SER-1573; SER-2198; SER-2211; SER-2252 AND SER-3225, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Protects actin filaments from depolymerization.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ACTN2. Interacts with F-actin (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell junction. Note=Colocalizes with actin stress
CC fibers.
CC -!- DOMAIN: Xin repeats bind F-actin.
CC -!- SIMILARITY: Belongs to the Xin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00721}.
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DR EMBL; AF466694; AAQ05020.1; -; mRNA.
DR RefSeq; NP_973718.1; NM_201989.1.
DR SMR; Q71LX6; -.
DR BioGRID; 259825; 1.
DR STRING; 10116.ENSRNOP00000048045; -.
DR iPTMnet; Q71LX6; -.
DR PhosphoSitePlus; Q71LX6; -.
DR PaxDb; Q71LX6; -.
DR PRIDE; Q71LX6; -.
DR GeneID; 311098; -.
DR KEGG; rno:311098; -.
DR UCSC; RGD:1302980; rat.
DR CTD; 129446; -.
DR RGD; 1302980; Xirp2.
DR eggNOG; ENOG502SF50; Eukaryota.
DR InParanoid; Q71LX6; -.
DR OrthoDB; 30028at2759; -.
DR PhylomeDB; Q71LX6; -.
DR PRO; PR:Q71LX6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR GO; GO:0051393; F:alpha-actinin binding; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0055008; P:cardiac muscle tissue morphogenesis; ISO:RGD.
DR GO; GO:0045216; P:cell-cell junction organization; ISO:RGD.
DR GO; GO:0003281; P:ventricular septum development; ISO:RGD.
DR InterPro; IPR012510; Actin-binding_Xin_repeat.
DR InterPro; IPR030072; XIRP1/XIRP2.
DR InterPro; IPR030107; XIRP2.
DR PANTHER; PTHR22591; PTHR22591; 1.
DR PANTHER; PTHR22591:SF1; PTHR22591:SF1; 1.
DR Pfam; PF08043; Xin; 19.
DR PROSITE; PS51389; XIN; 28.
PE 1: Evidence at protein level;
KW Actin-binding; Cell junction; Coiled coil; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..3302
FT /note="Xin actin-binding repeat-containing protein 2"
FT /id="PRO_0000316989"
FT REPEAT 306..321
FT /note="Xin 1"
FT REPEAT 341..356
FT /note="Xin 2"
FT REPEAT 381..396
FT /note="Xin 3"
FT REPEAT 418..433
FT /note="Xin 4"
FT REPEAT 456..471
FT /note="Xin 5"
FT REPEAT 496..511
FT /note="Xin 6"
FT REPEAT 534..549
FT /note="Xin 7"
FT REPEAT 572..587
FT /note="Xin 8"
FT REPEAT 606..621
FT /note="Xin 9"
FT REPEAT 640..655
FT /note="Xin 10"
FT REPEAT 677..692
FT /note="Xin 11"
FT REPEAT 713..728
FT /note="Xin 12"
FT REPEAT 744..759
FT /note="Xin 13"
FT REPEAT 782..797
FT /note="Xin 14"
FT REPEAT 820..835
FT /note="Xin 15"
FT REPEAT 859..874
FT /note="Xin 16"
FT REPEAT 892..907
FT /note="Xin 17"
FT REPEAT 930..945
FT /note="Xin 18"
FT REPEAT 965..980
FT /note="Xin 19"
FT REPEAT 1004..1019
FT /note="Xin 20"
FT REPEAT 1040..1055
FT /note="Xin 21"
FT REPEAT 1077..1092
FT /note="Xin 22"
FT REPEAT 1115..1130
FT /note="Xin 23"
FT REPEAT 1152..1167
FT /note="Xin 24"
FT REPEAT 1186..1201
FT /note="Xin 25"
FT REPEAT 1217..1232
FT /note="Xin 26"
FT REPEAT 1254..1269
FT /note="Xin 27"
FT REPEAT 1289..1304
FT /note="Xin 28"
FT REGION 166..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1848..1882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1920..1939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1957..2002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2039..2296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2311..2378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2546..2593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2626..2687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2835..2934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3278..3302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2303..2328
FT /evidence="ECO:0000255"
FT COILED 2696..2724
FT /evidence="ECO:0000255"
FT COILED 2751..2777
FT /evidence="ECO:0000255"
FT COMPBIAS 171..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1855..1878
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1920..1938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2050..2083
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2137..2161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2226..2245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2248..2264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2278..2294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2311..2360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2626..2640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2641..2663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2664..2687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2872..2903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2917..2931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 813
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4U4S6"
FT MOD_RES 1210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1573
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1930
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 1935
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 2158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4U4S6"
FT MOD_RES 2198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2987
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4U4S6"
FT MOD_RES 3225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 3302 AA; 373982 MW; 65EFEFEED1778ECB CRC64;
MARYQAAVSR GDTRSFSANV MEESDLCTVP GGLAKMKRQF EKDEMTSTCN AFSEYQYQHE
SRSEQEAIHN RQEIRRNEEE VSKGHRTDVF KAEMMSHLEK HTEETNQASQ FRQYVQETVI
DTPEDEEIPK VSTKILKEQF EKTAQENFLY SDKETTTPAK CIKIENDSEE TLKPSSAMGT
SSYTSARQSK ETSTSSYSNH SLTSTILAQE KGTPSGKMEE FPPPPPDVFQ TPMDVTAFSQ
SPEFPSPPRR LPMPRDVYSK QRNLYELNRL YRHIHPELRK NLEKDYISEV SEIVSSHINS
GNSISAGVQQ ARYVFENTND SSQKDLSSER ENLEWDEILK GEVQSIRWIF ENQPLDSINQ
GFTDEAYTSK GIADQELIAG GDVKYTTWMF ETQPIDALGV PSAGTEENTE KIPELAKGDV
CTARWMFETR PLDSMNKMHE WEDETASTFI KDITGGDVKT VRYMFETQQL DQLGQLHSVD
EMNLLQLRSE LKEIKGNVKR SIKCFETQPL YVIRDGSGQM LEIKTVQRED IEKGDVRTAR
WMFETQPLDT IKQDITEIKV VRGISMEENV KGEVGRARWL FETQPLEKIK EESGEAVLKT
EAVVGIDVSK KCWMFETQPL DTLKQSPDTE SVSPEERIGG DVKTTKHLLE TLPIEALKDS
PDVGKLQKIT ASEEEKGDVK HQKWVFETQR LEDIREDKKE YTQTVKLEAV DRGHVKNYTH
IFESNNLIKV DASHQIEVEG VTRGTVELNK SLFETTPLYA IQDHLGKYHQ VKTVQQEEIV
RGDVRSCRWL FETRPIDQFD ESLHKFQIIR GISAQEIQAG NVKSARWLFE TQPLDSIKYF
SNVEETDSKT EQSTDIVKGD VKTCKWLFET QPMESLYEKA SLMTNSEDIH KGDVRTCMWL
FETQPLDAIK NDSEATVKLQ TVKQEEIQGG DVRTACLLFE TENLDNIQGG EGKETKPVEM
DIESGDVSGM KYKFENQSLD SISCSSENVL NKIKTLKIED IQKGNVLNCR WLFENQPIDM
IKENQEGDGL VKTVTDIQGG DVRKGCFIFE TFSLDEIKDE SDVISTRQTN TEEVIKGDVK
SYKMLFETQP LYAIQDQEGF YHEVTTVKKE ETIHGDVRGT RWLFETKPLD SINASEDVYI
IKSVTQEDIQ KGDVSSVRYR FETQPLDMIS DKSHNIMPTI DHIQGGNVQM NKQLFESEGG
DKKNYVRTVS INEIQKGNVK TSTWLFETHS IDELGEVSTY ENIKTVTQED VQKGDVKQAV
WLFENQTLDS IKELDESDTK ITKEEIPPSD VKTTTWLFET TPIHEFNETR IEKEEIIGKS
IKETLEDLYS QRVVEAPGII IEADEVGDVR MAKYKLMNQR TPEIQKEEVI RADLGNIMMN
LLSQRDCTKK EIFISEEEKG NVNFTKTQLL NRSMEFHAEK EEIVRGDVKQ AIQKLFSEER
CAKRGILIQE DEKGDVNMTI YCLLHENAGD KTKREDILGG DVRRTIHNLL SSASNDKISE
RTKIDASERG NVQFFTTCIE TGALDYLKQL QTGSNETLTA RKQEGEEEII GGDVEGTKFL
LKKRQSSIER TVSETDIIPG DVRNTVKVFM TEPQSASFKT AKEEIVKGDL KSTLNSLNQA
MNQKVVAKTE DIMKDDKAAI LKSLKESGGR QKEHKQSASI SSDIGQAIEC LEKATNTRTE
ILKKELILDD LKTSLRSLKE EQYSFKEVGK QGMVKDVLGF SERQELGIHP AAVQREKKSL
LQPVPGPCEP AIRQQAGPGP LDEATQKSCH RSLTEERTEA NLPKAPKGTV KIVIDREQNN
DALEKSLRKM SNSEHRAMKN VLDMGDRRGV WTESKECLCS DDHMSKYVSA SMSRKKSLKT
KESENVRESK DDVSSTQSVD KTFRKQQTQN CELGKDHQKS QFQDSYAKNQ KNTQNISMSA
ETQSYRPDPT QHPVSNPAGE TLEMTRDFQK QALIRQEKQN SNKDMRKNDM GLQPLPVGKD
AHSAPGVTVS GKNHKRTQAP DKKQRIDVCL ESQDFLMKTN TSKELKMAME RSFNPVNLYP
DCGVKENEDA LPPPSPPPPP PSNASSEIEF PLPPPPPIML LPEKNEFPPS SPTEKSRAEL
ESLPTLPLPP PPGDEKSDQE CLPTSLPPPP PTAPSQPAHL LSSSVLEHHS EAFLQQYSRK
ETLDSHQLHS QAKILTGKSP PPTLPKPKLP ERIKAKMSQD SPSGELERSL SDVEIKTTLS
KDQKSSLVAE SREHTEAKQE VFRKSLGRKQ LSISSANSLS QTVPEIPAPK EKQTAPLVKS
HSFPSGSEQQ SPKPYMRKFK TPLMIAEEKY RQQREELEKQ RRESSCHSII KTETQHRSLS
EKEKETELQK AAEAMSTPRK DSDFTRAQPN LEPKSKAVIA SECSESQLST ASALTVATER
LQHVLAASDD KLTLRREGTQ NSSDTLQSKT ACEINQSHKE CRTEQTFEQH VEKLPFPQTK
PISPSFKVKT IRLPALDHTL TETDLSSERR VKQSEIDVQT STKEMNKEIK KTEVSTQCDN
KQSVAEKYFQ LPKTEKRVTV QMPKDYAAKS HQSKLQTVPK KHGGLGEFDR GNVLGREGKN
QDSSMSSTKE SRVIVERKQE HLQDQSVPRL VQQKIIGESL DSRVQNFQQT QTQTSRIEHK
ELSQPYSEKK CLRDKDKQQK QVSSNTDDSK QEITQKQSSF SSVRESQQDG EKCAINILEF
LRKREELQQI LSRVKQFEAD SNKSGLKTFQ TLLNIAPVWL ISEEKREYGV RVAMENNLEK
VKEEIIHIKT QAEEMLVHCE HVIRTAMMAS QTGKQKDKPT NLNEMPLKVS NVNLSSHKGT
EQKESKIVEE KLASRQVATH SEAATHNPAK TYQEAKGDDS KMAPPSLKTR PPSPTFITIE
STARRAETST KSELSQSPKN NSCVEPLPRR PMEHTSRLPR TSTSPSPPRS RSEQLVRLKD
TTARLAKGTI PCSPGTPVPV VEKRSEVVMS PATLRRQIKI ESRGGDSPPT ITIPVSVNHH
VVSGSFRESV DAQEAVKKTE KTETYVHKDK KNSVSSAMPE TESYDAVEII RKVEGPHLSE
HRERFEATNQ TVQMAEHFLN GHENEVNRWF REFENGPVFG AKTERRAYAN GEINHNMKQE
SHTFCKEEFG LESSETANFT GFSYRHPREH RAKAPATQPR VHSEARALNE HFLSVDAFDS
QIVESQVATS SSRSSEAGRS GFDFKHAPPT YEDVIAGHIL DIADSPTNLR RNFQKTWQES
ERVFKSVGYE TSDAHATEMS RAFQEELAFL SETVGPRQGN LHNLSKDGLS NGVPRSRPAE
FS
