ID F7AXY9_MACMU Unreviewed; 3375 AA.
AC F7AXY9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Xin actin binding repeat containing 2 {ECO:0000313|Ensembl:ENSMMUP00000025960.4};
GN Name=XIRP2 {ECO:0000313|Ensembl:ENSMMUP00000025960.4,
GN ECO:0000313|VGNC:VGNC:78953};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000025960.4, ECO:0000313|Proteomes:UP000006718};
RN [1] {ECO:0000313|Proteomes:UP000006718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [2] {ECO:0000313|Ensembl:ENSMMUP00000025960.4}
RP IDENTIFICATION.
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000025960.4};
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 SMR; F7AXY9; -.
DR Ensembl; ENSMMUT00000027751.4; ENSMMUP00000025960.4; ENSMMUG00000013251.4.
DR VEuPathDB; HostDB:ENSMMUG00000013251; -.
DR VGNC; VGNC:78953; XIRP2.
DR GeneTree; ENSGT00530000063779; -.
DR HOGENOM; CLU_000319_0_0_1; -.
DR Proteomes; UP000006718; Chromosome 12.
DR Bgee; ENSMMUG00000013251; Expressed in hindlimb stylopod muscle and 9 other cell types or tissues.
DR ExpressionAtlas; F7AXY9; baseline.
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:SF1; XIN ACTIN-BINDING REPEAT-CONTAINING PROTEIN 2; 1.
DR Pfam; PF08043; Xin; 18.
DR PROSITE; PS51389; XIN; 27.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00721};
KW Reference proteome {ECO:0000313|Proteomes:UP000006718}.
FT REPEAT 315..330
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 350..365
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 390..405
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 427..442
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 465..480
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 505..520
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 543..558
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 581..596
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 614..629
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 648..663
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 685..700
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 721..736
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 790..805
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 828..843
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 867..882
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 900..915
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 938..953
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 973..988
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 1012..1027
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 1048..1063
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 1085..1100
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 1123..1138
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 1160..1175
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 1194..1209
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 1225..1240
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 1263..1278
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REPEAT 1298..1313
FT /note="Xin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00721"
FT REGION 55..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2052..2222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2583..2611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2815..2962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3011..3039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2065..2100
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2141..2155
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2156..2193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2815..2845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2846..2884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2912..2943
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2944..2958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3020..3035
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3375 AA; 383387 MW; E6E4AED5EDA1470F CRC64;
MARYQAAVSR GDCRSFSANM MEESEMCTVP GGLAKVKKQF EDEITSSRNT FAQYQYQHQN
RSEQEAIHSS QVGTSKSSQE LARNEQEGSK VQKIDVHGTE MVSHLEKHTK EINQASQFHQ
YVQETVIDTP EDEEIPKVST KLLKEQFEKS AQEKILYSDK EMTTPAKQIK IESECEETLK
PSSVVSTSST SCISTSQRKE TSTTRYSDHS VTSSTLAQIN ATSSGMTEEF PPPPPDVLQT
SVDATAFSQS PELPSPPRRL PVPKDVYSKQ RNLYELNRLY KHIHPELRKN LEKDYISEVS
EIVSSQMNSG SSVSADVQQA RYVFENTNDS SQKDLNSERE YLEWDEILKG EVQSIRWIFE
NQPLDSINNG SPDEGDISRG VADQEIIAGG DVKYTTWMFE TQPIDTLGAH SSDTVENAEK
IPELARGDVC TARWMFETRP LDSMNKMHQS QEESAVTISK DITGGNVKTV RYMFETQHLD
QLGQLHSVDE VHLLQLRSEL KEIKGNVKRS IKCFETQPLY VIRDGSGQML EIKTVHREDV
EKGDVRTARW MFETQPLDTI NKDITEIKIV RGISMEENVK GGVSKAKWLF ETQPLEKIKE
SEEVIIEKET IIGTDVSRKC WMFETQPLDI LKEVPDADPL QHEEIIGGDV QTTKHLFETL
PIEALKDSPD IGKLQKITAS EEEKGDVRHQ KWIFETQPLE DIRKDKKEYT RTVKLEEVDR
GDVKNYTHIF ESNNLIKFDA SHKIEVEGVT RGAVELNKSL FETTPLYAIQ DPLGKYHQVK
TVQQEEIIRG DVRSCRWLFE TRPIDQFDES IHKFQIIRGI SAQEIQTGNV KSAKWLFETQ
PLDSIKYFSD VEETESKTEQ ARDIIKGDVK TCKWLFETQP MESLYEKVSL MTSSEEIHKG
DVKTCTWLFE TQPLDAIKDD SETKVKLQTV KQEEIQGGDV RTTCFLFETE NLDSIQGEEV
KEIKPVEMDI QAGDVSSMRY KFENQSLDSI SSSSEEVLKK IKTLKTEDIQ KGNVLNCRWL
FENQPIDKIK ESQEGDECVK TVTDIQGGDV RKGCFIFETF SLDEIKEESD YISTKKTITE
EVMQGDVKSY RMLFETQPLY AIQDREGSYH EVTTVKKEEV IHGDVRGTRW LFETKPLDSI
NKSETVYVIK AVTQEDIQKG DVSSVRYRFE TQPLDQISEE SHNIVPTVDH IQGGNVKTSK
QFFESENFDK NNYIRTVSVN EIQKGNVKTS TWLFETHTID ELRGEGLEYE NIKTVTQEDV
QKGDVKQAVW LFENQTFDSI MEAHKGVTKV TKEEIPPSDV KTTTWLFETT PLHEFNENRI
EKIEIIGKSI KKTLEDLYSQ KVIQAPGIII EADEVGDVRM AKYKLMNQAS PEIQKEEIIR
ADLRNIMVNL LSKRDYTKRE ILVSEEEKGN VNLTKTQLLN KSTEFHAEKE EIVKGDVQHA
IKNLFSEERS VKKGILIQED ERGDINMTIY CLLHENDGDT IEREEVIGGD VRRTIHNLLS
STSNNKISER AKFDASERGN VQFFTTCIEA GALDYLKQLH TESNETLTAK KQEGEKEIIG
GDVEGTKLLL KKRQSLVERT VSETDIIPGD VHNTVKVFMT EPQSTLGKIP KEEIIKGDLA
STLNSLSQAV NQKTVTKTEE IIKGDMLATL KSLKESTRRW KESKQPDAIP GDIEKAIECL
EKATNTRTEI LKKELLKDDL ETSLRSLKEA QRSFKEVDKE GVIKKDAHVV MAGSSGEQKT
DIHQVAVQRN KNSLLQPKSG PFEPAAEWQG GADTLSQTMG KSCHGNLVEE RTEVNLPKAP
KGSVKIVIDR EQNNDALEKS LRRLSNSHHK SIKNVLESGD KMGVWTDITG EQHLRDEYMS
RQLTSTVSVK NNLKTKESDR EVRELKKDDD FNSVQSADKT VGKQQTYERR NDHQKTEAFH
IKSPKKTENI KILTDTQNSK PSPTQHPVSM PVGGTYKISG DFQKQTLLKQ ETKYSNKNIK
QKNINFQPMW QPLPVEQDTT SVTEVKVSEK NHNTFKTTNK KQETDVHLKS QDFLMKTNTS
TDLKTAMERS LNPINFNPEN NVKESECPLP PPSPPPPPPS NASSEIEFPL PPPPPLMMFP
EKNGFLPSLS TEKIKAEFES FPGLPLPPPS VDEKSERESP SMFLPPPPPP TPSQNPAHLL
SSSAPEKHSG AFMQQYSQKE ASNSQNSQAK IITGKSGVLP PPTLPKPKLP KHIKDNKNHF
SPKVELTNSL SDMECKITTS KDQKKVMMMT SSEHIETKQN VISKSLDERK QLFVDSANCL
SHTVPGTSAP KKKQIAPLIK SHSFPESSGQ QSPKPYMRKF KTPLMIAEEK YRQQKEELEK
QKQESSYYNI VKTESQNQHI SEVEKEMPLR KTNEEVSVSG IDSERTVVQP NPGSQSNARV
LGVCSDNQLS TTSPVTVTAK RLHHVLAASE DKDKMKKEVL QSARDIMQSK SACEIKQSHQ
ECSTQQTQQN QYLEQLHLPQ SKPISPNFKV KTIKLPTLDH TLNETDHSYE SHKQQSEVDV
QTFAKQQYLE TKKTEASTEC SHKQSLAERH YQLPKKEKRV TIKLPTESIQ KNHEDKLQIV
PGKQEEFAGS DRGKLPGSEE KNKGPSMISR KEERLITERK QEVLKNKSAP KVVKQKVIDA
HLDSQTQNFQ QTQIQTSESK AEHKKWPQPY NSLQEEKCLQ VKGIQQKQVF SNTKDSKQEI
TQNKSFFSAV KESQQDDGKC AVNIVEFLRK REELQQILSR VKQFEAEPNK SGLKTFQTLL
NTIPGWLISE EKREYAVHIA MENNLEKVKE EITHIKTQAE DMLVSYENII QTAMMSSKTG
KSGNKPTSLD ETSSKVSNVH VSNNKNSEQK ENKIAKEKTG QHQVAAHREA AVHSHVKTHQ
EIKLDESNIP PPSLKTRPPS PTFITIESTV RRTETPTKDE LSQSPKKDSY VEPPPRRPKS
QTSEIHRANT SPSPPRSRSE QLVRLKDTTA KLSKGAIPCP AVTPVPVVEK RSEIIMSPAT
LRRQIKIETR GRDSPPTITI PVNIHHTPSG SSRESTEAQE EIRKVEKRAT YVHNAGLNST
DPIVPDTESY DAVEIIRKVE VPPRLSEHTQ RYEAANRTVQ MAENFVDDRE NEINRWFREF
EHGPVSEAKS NRRVYANGET NHNIQQESHT FCQEEFGLTS LGNTSFTDFS CTHPRELQEK
IPVKQPRICS ETRSLSEHFS GMDAFESQIV ESKMKTSSSH SSEAGKSGCD FKHAPPTYED
VIAGHILDIS DSPKEVRKNF QNTWQESGRV FKSLGYATSD SSATEMRTAF QEESAFISVW
EIMHHFMDKY TANLTLNNFS NLKEIMMKVL DTSSIKIDGT AKTKADQWTL FLMKNQMCVK
ILQKTPLYLE IVMNI
//
