ID A0A2K5HEQ8_COLAP Unreviewed; 781 AA.
AC A0A2K5HEQ8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Actinin alpha 2 {ECO:0008006|Google:ProtNLM};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000002827.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000002827.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the alpha-actinin family.
CC {ECO:0000256|ARBA:ARBA00010255}.
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DR AlphaFoldDB; A0A2K5HEQ8; -.
DR STRING; 336983.ENSCANP00000002827; -.
DR Ensembl; ENSCANT00000011575.1; ENSCANP00000002827.1; ENSCANG00000010367.1.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:UniProt.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd21214; CH_ACTN_rpt1; 1.
DR CDD; cd21216; CH_ACTN_rpt2; 1.
DR CDD; cd00176; SPEC; 1.
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; 1.
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:SF429; ALPHA-ACTININ-2; 1.
DR PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF08726; EFhand_Ca_insen; 1.
DR Pfam; PF00435; Spectrin; 4.
DR SMART; SM00033; CH; 2.
DR SMART; SM01184; efhand_Ca_insen; 1.
DR SMART; SM00150; SPEC; 2.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF46966; Spectrin repeat; 4.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080};
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 676..711
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT COILED 230..257
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 395..478
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 629..663
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 781 AA; 90217 MW; 0E1CA07874AF6D5C CRC64;
TFTAWCNSHL RKAGTQIENI EEDFRNGLKL MLLLEVISGE RLPKPDRGKM RFHKIANVNK
ALDYIASKGV KLVSIGAEEI VDGNVKMTLG MIWTIILRFA IQDISVEETS AKEGLLLWCQ
RKTAPYRNVN IQNFHTSWKD GLGLCALIHR HRPDLIDYSK LNKDDPIGNI NLAMEIAEKH
LDIPKMLDAE DIVNTPKPDE RAIMTYVSCF YHAFAGAEQA ETAANRICKV LAVNQENERL
MEEYERLASE LLEWIRRTIP WLENRTPEKT MQAMQKKLED FRDYRRKHKP PKVQEKCQLE
INFNTLQTKL RISNRPAFMP SEGKMVSDIA GAWQRLEQAE KGYEEWLLNE IRRLERLEHL
AEKFRQKAST HETWAYGKEQ ILLQKDYESA SLTEVRALLR KHEAFESDLA AHQDRVEQIA
AIAQELNELD YHDAVNVNDR CQKICDQWDR LGTLTQKRRE ALERMEKLLE TIDQLHLEFA
KRAAPFNNWM EGAMEDLQDM FIVHSIEEIQ SLITAHEQFK ATLPEADGER QSIMAIQNEV
EKVIQSYSIR ISSSNPYSTV TMDELRTKWD KVKQLVPIRD QSLQEELARQ HANERLRRQF
AAQANAIGPW IQNKMEEIAR SSIQITGALE DQMNQLKQYE HNIINYKNNI DKLEGDHQLI
QEALVFDNKH TNYTMEGEAE FARIMTLVDP NGQGTVTFQS FIDFMTRETA DTDTAEQVIA
SFRILASDKP YILAEELRRE LPPDQAQYCI KRMPAYSGPG SVPGALDYTA FSSALYGESD
L
//