ID A0A493TKH2_ANAPP Unreviewed; 942 AA.
AC A0A493TKH2;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Alpha-actinin-4 {ECO:0000256|ARBA:ARBA00040341};
DE AltName: Full=Non-muscle alpha-actinin 4 {ECO:0000256|ARBA:ARBA00042924};
GN Name=ACTN4 {ECO:0000313|Ensembl:ENSAPLP00000026354.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000026354.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000026354.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC Cytoplasm, cytoskeleton, stress fiber {ECO:0000256|ARBA:ARBA00004529}.
CC Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
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DR AlphaFoldDB; A0A493TKH2; -.
DR Ensembl; ENSAPLT00000047122.1; ENSAPLP00000026354.1; ENSAPLG00000026055.1.
DR GeneTree; ENSGT00940000159343; -.
DR Proteomes; UP000016666; Unassembled WGS sequence.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0001725; C:stress fiber; IEA:UniProtKB-SubCell.
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; 3.
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; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR11915:SF425; ALPHA-ACTININ-4; 1.
DR PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF00435; Spectrin; 4.
DR SMART; SM00033; CH; 2.
DR SMART; SM00054; EFh; 1.
DR SMART; SM00150; SPEC; 4.
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; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 99..203
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 212..318
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 814..849
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 899..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 498..532
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 942 AA; 106580 MW; 3A89179203B0266F CRC64;
MAVGFLGPPL QDFGAVPLRL LGWPPQNPQT RGFVPGGVFL PPCRGGTRPA LGAAGGLAGA
RQRPWGRART FWGRSITFWG RASTRGAVPG VAADPGVPAP PRPTFTAWCN SHLRKAGTQI
ENIDEDFRDG LKLMLLLEVI SGERLPKPER GKMRVHKINN VNKALDFIAS KGVKLVSIGA
EEIVDGNAKM TLGMIWTIIL RFAIQDISVE ETSAKEGLLL WCQRKTAPYK NVNVQNFHIS
WKDGLAFNAL IHRHRPELIE YDKLRKDDPV TNLNNAFEVA EKYLDIPKML DAEDIVGTLR
PDEKAIMTYV SCFYHAFSGA QKAETAANRI CKVLAVNQEN EHLMEDYEKL ASDLLEWIRR
TIPWLEDRSP QKTIQEMQQK LEDFRDYRRV HKPPKVQEKC QLEINFNTLQ TKLRLSNRPA
FMPSEGRMVA DINNGWQHLE QAEKGYEEWL LNEIRRLERL DHLAEKFRQK ASIHEAWTEG
KEAMLKQKDY ESATLSDIKA LIRKHEAFES DLAAHQDRVE QIAAIAQELN ELDYYDSPSV
NARCQKICDQ WDVLGSLTHS RREALEKTEK QLETIDELHL EYAKRAAPFN NWMESAMEDL
QDMFIVHTIE EIEGLIAAHD QFKSTLPDAD KEREAILGIQ REAQRIADFN SIKLGGNNPY
TSVTPQIINS KWERVQQLVP KRDHALLDEQ SKQQSNEHLR RQFASQANIV GPWIQTKMEE
IGRISIEMNG TLEDQLNHLK QYEQSIVDYK PNIDLLEQQH QLIQEALIFD NKHTNYTMEH
IRVGWEQLLT TIARTINEVE NQILTRDAKG ISQEQMQEFR ASFNHFDKDH GGALGPEEFK
ACLISLGYDV ENDRQKRTGS TDADDFRALL ISAGCSLVTL SALFSLLFPP PPVPFWSSSH
RCEPPGLGEG AGGHKETPPE PKTGAGLSLQ PGDSVVGGGG AP
//
