ID A0A1S3EJX1_DIPOR Unreviewed; 733 AA.
AC A0A1S3EJX1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Alpha-actinin-2-like {ECO:0000313|RefSeq:XP_012864683.1};
GN Name=LOC105980377 {ECO:0000313|RefSeq:XP_012864683.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012864683.1};
RN [1] {ECO:0000313|RefSeq:XP_012864683.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012864683.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the alpha-actinin family.
CC {ECO:0000256|ARBA:ARBA00010255}.
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DR RefSeq; XP_012864683.1; XM_013009229.1.
DR AlphaFoldDB; A0A1S3EJX1; -.
DR STRING; 10020.ENSDORP00000015124; -.
DR GeneID; 105980377; -.
DR KEGG; dord:105980377; -.
DR InParanoid; A0A1S3EJX1; -.
DR OrthoDB; 2872403at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd21214; CH_ACTN_rpt1; 1.
DR CDD; cd00176; SPEC; 2.
DR Gene3D; 1.20.58.60; -; 3.
DR Gene3D; 1.10.418.10; Calponin-like domain; 3.
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; 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; 3.
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; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 3.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 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:UP000081671};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..103
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT COILED 505..539
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 733 AA; 83709 MW; 2024DC54295F2E95 CRC64;
MVDTFTAWCN SHLRKAGTQI ENIEEDFRNG LKLMLLLEVI SGERLPKPDR GKMRFHKIAN
VNKALDYIAS KGVKLVSIGA EEIVDGNVKM TLGMIWTIIL RFAIQDISVE ETSAKEGLLL
WCQRKTAPYR NVNIQNFHTR QAPARRRGGA LPVSQEPTCD DPIGNINLAM EIAEKHLDIP
KMLDAEDLVY TARPDERALM TYVSCYYHAF AGAQKKVLSV DGPHRLHDEV SLQGMNGRAE
TAANRICKVL AVNQENERLM EEYERLASEV KDRGARLRTP LQGRLCRLHL ASQREGKQEP
HGLSLAPVVA SSVQCQRCSD AESQSMRACA EALACCIQAP PLDSLVLAKS RSLATLAQVL
LLEWIRRTIP WLENRTPEKT MQAMQKKLED FRDYRRKHKP PKVQEKCQLE INFNTLQTKL
RISNRPAFMP SEGKMVSDIA GAWQRLEQAE KGYEEWLLNE IRRLERLEHL AEKFRQKAST
HETWAYGKEQ ILLQKDYESA SLTEVRALLR KHEAFESDLA AHQDRVEQIA AIAQELNELD
YHDAVNVNDR CQKICDQWDR LGTLTQKRRE ALERTEKLLE TIDQLHLEFA KRAAPFNNWM
EGAMEDLQDM FIVHSIEEIQ SLITAHEQFK ATLPEADGER QSIMAIQNEV EKVIQSYSIR
ISSSNPYSTV TMDELRNKWE KPYILADELR RELPPDQAQY CIKRMPAYSG PGSVPGALDY
TAFSSALYGE SDL
//
