ID A0A195EYG8_9HYME Unreviewed; 812 AA.
AC A0A195EYG8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Dystrophin, isoforms A/C/F/G/H {ECO:0000313|EMBL:KYN33263.1};
GN ORFNames=ALC56_12412 {ECO:0000313|EMBL:KYN33263.1};
OS Trachymyrmex septentrionalis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=34720 {ECO:0000313|EMBL:KYN33263.1, ECO:0000313|Proteomes:UP000078541};
RN [1] {ECO:0000313|EMBL:KYN33263.1, ECO:0000313|Proteomes:UP000078541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN33263.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN33263.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex septentrionalis WGS genome.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000256|ARBA:ARBA00004278}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004278}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004278}.
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DR EMBL; KQ981906; KYN33263.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A195EYG8; -.
DR STRING; 34720.A0A195EYG8; -.
DR Proteomes; UP000078541; Unassembled WGS sequence.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IEA:UniProt.
DR GO; GO:0043232; C:intracellular non-membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007154; P:cell communication; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:UniProt.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:UniProt.
DR GO; GO:0023052; P:signaling; IEA:UniProt.
DR CDD; cd16242; EFh_DMD_like; 1.
DR CDD; cd00201; WW; 1.
DR CDD; cd02334; ZZ_dystrophin; 1.
DR Gene3D; 1.20.58.60; -; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR015153; EF-hand_dom_typ1.
DR InterPro; IPR015154; EF-hand_dom_typ2.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR12268:SF14; DYSTROPHIN-1; 1.
DR PANTHER; PTHR12268; E3 UBIQUITIN-PROTEIN LIGASE KCMF1; 1.
DR Pfam; PF09068; EF-hand_2; 1.
DR Pfam; PF09069; EF-hand_3; 1.
DR Pfam; PF00435; Spectrin; 1.
DR Pfam; PF00397; WW; 1.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00150; SPEC; 1.
DR SMART; SM00456; WW; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000078541};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 184..217
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 439..495
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT REGION 640..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 91347 MW; 4DF51C65FD69BBD6 CRC64;
MELVKSGTIE MLSRRSVAIK DYSVENGSED EERCDESDRT SLKIDLSMAE QFYYEVISSF
EQEEKICVFQ KSLEDLSSRM AAAEAIQSGW QNPNDANEAT EMLEQLQKFG ERLVPIQRNI
EDANDQASVF ASSSVIVSHA LLAKLEDLNT RWKVLQVAVD ERYKLLSGFG KDGSTPGSQA
FLASSVEPPW ERALTPAKVP YYINHQLETT HWDHPKMIEL MSSLADLNEV RFSAYRTAMK
LRTVQKRLCL DMLSLSTALE QFDSHGLRAQ NDKLIDIPDM VTVLTSLYEV IAADNPAQVS
VPLCIDLAIN WLLNVYDSQR TGQIRVLSFK VGLVLLCKGH LEEKYRYLFR LIADPNRLVD
QRKLGLLLHD CIQVPRQLGE VAAFGGSNIE PSVRSCFEKA GKDKNEIEAV HFLSWLQQEP
QSMVWLPVLH RLSAAETAKH QAKCNICKEY PIIGFRYRCL KCFNFDMCQN CFFSGRKAKN
HKLTHPMQEY CTATTSGEDV RDFTRALRNK FKSKRYFKKH PRVGYLPVQT VLEGDALESP
APSPQHSSLS QDMHSRLEMY ASRLAEVELS RTRSNSTPDS DDEHQLIAHY CQSLNGGDNI
NVPRSPVQVM AAIDAEQREE LEAMIRELEE ENATLQAEYE RLRSKQTPGS TPEDGHSTRQ
PDCDMIAEAK LLRQHKGRLE ARMQLLEDHN RQLEAQLQRL RQLLDEPNAS SPSKTGTLQT
RSVTASQLAT DSPAKMNGHY HDSPGGGSSN EGRVGSLERP PPPPHSHSVT HNVGNLLHMA
GDLGKAVGEL VTVMTEDTSK TNGQRAPPPA FK
//
