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Database: UniProt
Entry: A0A3B3C9E8_ORYME
LinkDB: A0A3B3C9E8_ORYME
Original site: A0A3B3C9E8_ORYME 
ID   A0A3B3C9E8_ORYME        Unreviewed;      1580 AA.
AC   A0A3B3C9E8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Spectrin beta chain, non-erythrocytic 4-like {ECO:0000313|Ensembl:ENSOMEP00000014551.1};
OS   Oryzias melastigma (Marine medaka).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000014551.1, ECO:0000313|Proteomes:UP000261560};
RN   [1] {ECO:0000313|Ensembl:ENSOMEP00000014551.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the spectrin family.
CC       {ECO:0000256|ARBA:ARBA00006826}.
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DR   STRING; 30732.ENSOMEP00000014551; -.
DR   PaxDb; 30732-ENSOMEP00000014551; -.
DR   Ensembl; ENSOMET00000033605.1; ENSOMEP00000014551.1; ENSOMEG00000016078.1.
DR   GeneTree; ENSGT00940000156343; -.
DR   OMA; KEMRECW; -.
DR   OrthoDB; 4163551at2759; -.
DR   Proteomes; UP000261560; Unplaced.
DR   GO; GO:0043226; C:organelle; IEA:UniProt.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR   CDD; cd10571; PH_beta_spectrin; 1.
DR   CDD; cd00176; SPEC; 3.
DR   Gene3D; 1.20.58.60; -; 5.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
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; PF00169; PH; 1.
DR   Pfam; PF00435; Spectrin; 6.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00150; SPEC; 7.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 6.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Actin capping {ECO:0000256|ARBA:ARBA00022467};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1384..1496
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          899..934
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          949..1001
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1207..1387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1498..1580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          556..590
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1207..1236
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1253..1322
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1369..1384
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1499..1563
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1580 AA;  177126 MW;  56F0108419198533 CRC64;
     MLMARDTARD EAQKLHRKWL KHQAFMAELA RNKEWLAKIE QEGEELIQEK PELRSVVEQK
     LEEIRECWSD LENTTKAKAR QLFENNKAEP VVKSYSDLDS QLSHLEQQPP QLEQAHHLPT
     FNEQLQKFQA MESQIGDFYK DVGELGTLQG LCLPQQGLMP GDKDDTEQSG VVETRIVRLI
     EPLKERRRIL LASKEMHQVA QDLEDEILWI QERLPLASCK DFGNNLQSVQ QHVKKNQALQ
     RELTGRRARV EEVLDRAGII ASLRTPEVEF VREGAGHVRQ LWEVLQLETE RRAVILEAAL
     QAQQYYSEGA KVESWLSGQK LHLASEEKGT DEASTLQLLK AHLTLEQTVE TYAETVGMLS
     QQCQHLLELG HPESEQIMKQ QSHIDRLYVS LKDMVEHRKT KLEQQYWLYQ LNKEVEDLER
     WITEHEAVAS STELGQDLQE VSVLQERFTK FATETNSTGE QRMEQVNKMV NEMIDCGHSD
     AATIAEWKDG LNESWADLLE LMETRRQMLA ASYQLHKFFT DCKEVLAQIA GKTKQLPEVR
     ACQANISNPA TLQRLMHSFE HALQLLVAQV RQLQENAAQL RTIYAGEKAE AIMVKEQEVM
     DAWKELLRAC EASRVQVTSV TDKVQFFSVV RENLMWMEGI MGQIRWDEPR DLTALEVMMK
     QHQELKAKID GRSKTIQQCA DLGKILIAAG NPASEEIKEK LDSLLTKQKD LVEKWDRHQE
     KLQSKQERFQ FAQETVKAEA WLKAKEPLIT SKQKEGGEAP AHTDEVEQLI LRHEAFRKAA
     VTWKERFSSL RQLSAAEKKQ EEDKKKIPLS SRRMFPLSCL TPSVPSTSST SSFLRQTVHA
     QIEPKPLQTS LELGSSSATQ RLSSSLASYN PVLNGSGYQG LEQRSTGLVN TSYLGMNQPA
     TAGANNPSFS ASQIGGTDTS TFQGKSNQPG GSAESSWYFA STTVSGIQNH PSSGKLGSSG
     NIAQQPSSGG IGSPGYSSPQ NFGSSSFFGQ QPSMGSSGYL AQQPNIESSG YLAQQSNIGS
     SGYLAQQPNM GSSGYLAQQP NMGSSGYLAQ QPNMGSSGYL AQQPNMGSSG YLAQQPNMGS
     SGYLAQQPNM GSSGYLAQQP NMGSSGYLAQ NYQSSGLGSS SYLAQNHYSS GSLGSSGYLA
     QSGGIMDPKM AYAWQHLKAD FMQPRINHIH KAINPLLEAT RMQREQFGDI PMADMVGPES
     GLELLHGRLQ RDPRGSRSDP QMDHLRRERE YKLGRQTSSE QEIQARLNEL PMIVRQERYR
     RRMERQSSSE QEGSNKQRLQ RQDSSDLEGS VKDGSDKRSG EKRSTMAEIV EQVQEREAAN
     ARGEPYRPPS SLSAPVTRFD GRPRARDRPK PRRRPRPKEP EETRRSRSAP ATGAPTTPQP
     PSHTAHNEGF LYRKKATSTE LEAQQRSPNS KSWVNVYCVL KDGKLTFYKD ARNHSTSYNG
     EPSVDLGNCS FDPSMGYKKK KNVFILQEND GNNFIFHAKD EEDLKAWTSN ITTSIAEHEA
     MGKWDKPGTS SMDPDRSERK EKSEGDADAR SERSELVEME ERSEKERSDK GDGSEKLDTS
     EIADKLEGGA GGSSTSGKSK
//
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