ACTN_ANOGA
ID ACTN_ANOGA Reviewed; 922 AA.
AC Q7PKQ5; Q380H9; Q7PUX2;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Alpha-actinin, sarcomeric;
DE AltName: Full=F-actin cross-linking protein;
GN Name=Actn; ORFNames=AGAP001497;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
CC -!- FUNCTION: F-actin cross-linking protein which is thought to anchor
CC actin to a variety of intracellular structures. This is a bundling
CC protein (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; antiparallel. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the alpha-actinin family. {ECO:0000305}.
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DR EMBL; AAAB01008987; EAA43174.2; -; Genomic_DNA.
DR RefSeq; XP_321625.2; XM_321625.5.
DR AlphaFoldDB; Q7PKQ5; -.
DR SMR; Q7PKQ5; -.
DR STRING; 7165.AGAP001497-PA; -.
DR PaxDb; Q7PKQ5; -.
DR GeneID; 1281675; -.
DR KEGG; aga:AgaP_AGAP001497; -.
DR CTD; 1281675; -.
DR VEuPathDB; VectorBase:AGAP001497; -.
DR eggNOG; KOG0035; Eukaryota.
DR InParanoid; Q7PKQ5; -.
DR OrthoDB; 543832at2759; -.
DR PhylomeDB; Q7PKQ5; -.
DR Proteomes; UP000007062; Chromosome 2R.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0055001; P:muscle cell development; IBA:GO_Central.
DR CDD; cd00014; CH; 2.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 3.
DR Gene3D; 1.10.418.10; -; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR014837; EF-hand_Ca_insen.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF08726; EFhand_Ca_insen; 1.
DR Pfam; PF00435; Spectrin; 4.
DR SMART; SM00033; CH; 2.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00150; SPEC; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 3: Inferred from homology;
KW Actin-binding; Calcium; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..922
FT /note="Alpha-actinin, sarcomeric"
FT /id="PRO_0000073446"
FT DOMAIN 36..140
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 149..255
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 253..393
FT /note="Spectrin 1"
FT REPEAT 394..508
FT /note="Spectrin 2"
FT REPEAT 509..629
FT /note="Spectrin 3"
FT REPEAT 630..742
FT /note="Spectrin 4"
FT DOMAIN 776..811
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 817..852
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..252
FT /note="Actin-binding"
FT BINDING 789
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 791
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 793
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 795
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 800
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 922 AA; 106527 MW; AE150B65BFF2B934 CRC64;
MMENGGYVGQ YGGEENYMEQ EEEWEREGLL DPAWEKQQKK TFTAWCNSHL RKAGTSIENI
EDDFRNGLKL MLLLEVISGE TLPKPDRGKM RFHKIANVNK ALDFIASKGV KLVSIGAEEI
VDGNLKMTLG MIWTIILRFA IQDISVEEMT AKEGLLLWCQ RKTAPYKNVN VQNFHLSFKD
GLAFCALIHR HRPDLIDYSK LSKDNPLENL NTAFDVAEKY LDIPRMLDPD DLINTPKPDE
RAIMTYVSCY YHAFQGAQQP GSTPFVIHLT KTGLSYRFFV RLFAAETAAN RICKVLKVNQ
ENERLMEEYE RLASDLLEWI RRTMPWLNSR QSDSTLAGVQ KKLEEYRTYR RKHKPPRVEQ
KAKLETNFNT LQTKLRLSNR PAYMPTEGKM VSDITNSWKG LEHAEKAFEE WLLAETMRLE
RLEHLAQKFK HKADTHEDWT KGKEEMLQSQ DFRNCKLNEL KALKKKHEAF ESDLAAHQDR
VEQIAAIAQE LNTLEYHDCA SVNARCQRIC DQWDRLGALT QRRRQGLDEA ERILEKIDLL
HLEFAKRAAP FNNWLDGARE DLVDMFIVHT MEEIQGLIQA HDQFKATLGE ADKEFNVIIG
LVRDAEAIVK QEQVPGGLVN PYTTLSADLI SRKWSEVRAL VPQRDQTLAN ELRKQQNNEM
LRRQFAEKAN AVGPWIERQM DAVTAIGMGI SGSLEEQLHR LKEYEQAVYA YKPSIEELEK
IHQAVQESMI FENRYTHYTM ETLRVGWEQL LTSINRNINE VENQILTRDS KGITQEQLTE
FRSSFNHFDK NRTGRLAPEE FKSCLVSLGY SIGKDKQGDM DFQRILAVVD PNASGYVQFD
AFLDFMTRES TDTDTAEQVI DSFRILASDR PYILPDELRR ELPPDQAEYC IQRMPPYKGP
NAIPGALDYM SFSTALYGES DL
