ID A0A099YT33_TINGU Unreviewed; 852 AA.
AC A0A099YT33;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Alpha-actinin-1 {ECO:0000256|ARBA:ARBA00018384};
DE AltName: Full=Alpha-actinin cytoskeletal isoform {ECO:0000256|ARBA:ARBA00041477};
DE AltName: Full=F-actin cross-linking protein {ECO:0000256|ARBA:ARBA00043249};
DE AltName: Full=Non-muscle alpha-actinin-1 {ECO:0000256|ARBA:ARBA00042871};
DE Flags: Fragment;
GN ORFNames=N309_08045 {ECO:0000313|EMBL:KGL73434.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL73434.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL73434.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL73434.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cell projection, ruffle
CC {ECO:0000256|ARBA:ARBA00004466}. Cytoplasm, myofibril, sarcomere, Z
CC line {ECO:0000256|ARBA:ARBA00004216}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the alpha-actinin family.
CC {ECO:0000256|ARBA:ARBA00010255}.
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DR EMBL; KL885931; KGL73434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099YT33; -.
DR STRING; 94827.A0A099YT33; -.
DR Proteomes; UP000053641; Unassembled WGS sequence.
DR GO; GO:0005923; C:bicellular tight junction; ISS:AgBase.
DR GO; GO:0031252; C:cell leading edge; ISS:AgBase.
DR GO; GO:0097433; C:dense body; ISS:AgBase.
DR GO; GO:0005925; C:focal adhesion; ISS:AgBase.
DR GO; GO:0090637; C:inner dense plaque of desmosome; ISS:AgBase.
DR GO; GO:0030027; C:lamellipodium; ISS:AgBase.
DR GO; GO:0016328; C:lateral plasma membrane; ISS:AgBase.
DR GO; GO:0090636; C:outer dense plaque of desmosome; ISS:AgBase.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; ISS:AgBase.
DR GO; GO:0030486; C:smooth muscle dense body; ISS:AgBase.
DR GO; GO:0001725; C:stress fiber; ISS:AgBase.
DR GO; GO:1990357; C:terminal web; ISS:AgBase.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0005915; C:zonula adherens; ISS:AgBase.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0051393; F:alpha-actinin binding; ISS:AgBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:AgBase.
DR GO; GO:0017166; F:vinculin binding; ISS:AgBase.
DR GO; GO:0045214; P:sarcomere organization; ISS:AgBase.
DR GO; GO:0048741; P:skeletal muscle fiber development; ISS:AgBase.
DR CDD; cd21214; CH_ACTN_rpt1; 1.
DR CDD; cd21216; CH_ACTN_rpt2; 1.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 2.
DR Gene3D; 1.20.58.60; -; 4.
DR Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR014837; EF-hand_Ca_insen.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR11915:SF434; ALPHA-ACTININ-1; 1.
DR PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF08726; EFhand_Ca_insen; 1.
DR Pfam; PF00435; Spectrin; 4.
DR SMART; SM00033; CH; 2.
DR SMART; SM00054; EFh; 2.
DR SMART; SM01184; efhand_Ca_insen; 1.
DR SMART; SM00150; SPEC; 3.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 4.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053641};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..100
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 109..215
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 711..746
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 747..782
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT COILED 230..257
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 395..429
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL73434.1"
FT NON_TER 852
FT /evidence="ECO:0000313|EMBL:KGL73434.1"
SQ SEQUENCE 852 AA; 98405 MW; 47F83CF6625E765C CRC64;
TFTAWCNSHL RKAGTQIENI EEDFRDGLKL MLLLEVISGE RLAKPERGKM RVHKISNVNK
ALDFIASKGV KLVSIGAEEI VDGNVKMTLG MIWTIILRFA IQDISVEETS AKEGLLLWCQ
RKTAPYKNVN IQNFHISWKD GLGFCALIHR HRPELIDYGK LRKDDPLTNL NTAFDVAEKY
LDIPKMLDAE DIVGTLRPDE KAVMTYVSCY YHAFSGAQKA ETAANRICKV LAVNQENEQL
MEDYEKLASD LLEWIRRTIP WLENRVPENT MQAMQQKLED FRDYRRLHKP PKVQEKCQLE
INFNTLQTKL RLSNRPAFMP SEGKMVSDIN NAWGGLEQAE KGYEEWLLNE IRRLERLDHL
AEKFRQKASI HESWTDGKEA MLQQKDYEIA TLSEIKALLK KHEAFESDLA AHQDRVEQIA
AIAQELNELD YYDSPSVNAR CQKICDQWDN LGALTQKRRE ALERTEKLLE TIDQLYLEYA
KRAAPFNNWM EGAMEDLQDT FIVHTIEEIQ GLTTAHEQFK ATLPDADKER QAILGIHNEV
SKIVQTYHVN MAGTNPYTTI TPQEINGKWE HVRQLVPRRD QALMEEHARQ QQNERLRKQF
GAQANVIGPW IQTKMEEIGR ISIEMHGTLE DQLNHLRQYE KSIVNYKPKI DQLEGDHQQI
QEALIFDNKH TNYTMEHIRV GWEQLLTTIA RTINEVENQI LTRDAKGISQ EQMNEFRASF
NHFDRKKTGM MDCEDFRACL ISMGYNMGEA EFARIMSIVD PNRMGVVTFQ AFIDFMSRET
ADTDTADQVM ASFKILAGDK NYITVDELRR ELPPDQAEYC IARMAPYHGH DAVPGALDYM
SFSTALYGES DL
//
