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Database: UniProt
Entry: A0A3B4Y881_SERLL
LinkDB: A0A3B4Y881_SERLL
Original site: A0A3B4Y881_SERLL 
ID   A0A3B4Y881_SERLL        Unreviewed;      2357 AA.
AC   A0A3B4Y881;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000027055.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000027055.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the spectrin family.
CC       {ECO:0000256|ARBA:ARBA00006826, ECO:0000256|PIRNR:PIRNR002297}.
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DR   STRING; 1841481.ENSSLDP00000027055; -.
DR   Ensembl; ENSSLDT00000027889.1; ENSSLDP00000027055.1; ENSSLDG00000020976.1.
DR   GeneTree; ENSGT00940000158908; -.
DR   Proteomes; UP000261360; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProt.
DR   GO; GO:0008091; C:spectrin; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:UniProtKB-UniRule.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-UniRule.
DR   CDD; cd21246; CH_SPTB-like_rpt1; 1.
DR   CDD; cd10571; PH_beta_spectrin; 1.
DR   CDD; cd00176; SPEC; 8.
DR   Gene3D; 1.20.58.60; -; 13.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR041681; PH_9.
DR   InterPro; IPR001605; PH_dom-spectrin-type.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR016343; Spectrin_bsu.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   PANTHER; PTHR11915:SF248; SPECTRIN BETA CHAIN, ERYTHROCYTIC; 1.
DR   PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF15410; PH_9; 1.
DR   Pfam; PF00435; Spectrin; 17.
DR   PIRSF; PIRSF002297; Spectrin_beta_subunit; 1.
DR   PRINTS; PR00683; SPECTRINPH.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00150; SPEC; 17.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF46966; Spectrin repeat; 15.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Actin capping {ECO:0000256|ARBA:ARBA00022467,
KW   ECO:0000256|PIRNR:PIRNR002297};
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203,
KW   ECO:0000256|PIRNR:PIRNR002297}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR002297};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW   ECO:0000256|PIRNR:PIRNR002297}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          54..158
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          175..280
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          2199..2309
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          2104..2123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2132..2189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2306..2357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          459..493
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          885..919
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1398..1445
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1566..1593
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        2104..2122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2357 AA;  272730 MW;  536B4513F835714D CRC64;
     MTSTTDFDNV EITQQYSHIN TRFDLCDEEL DNDNSSARLF ERSRIKALAD EREAVQKKTF
     TKWVNSILSR VGCRISDLYL DLRDGRMLIK LLEVLSGERL PKPTKGRMRI HCLENVDKAL
     QFLKEQRVHL ENMGSHDIVD GNHRLILGLI WTIILRFQIQ DIIVETGQAD QKETRSAKDA
     LLLWCQMKTA GYPNVNITNF TTSWKDGMAF NALIHKHRPD LVDYNSLKRS NPTHNLQNAF
     NVAEQKLGVT KLLDPEDVFT ENPDEKSIIT YVVAFYHYFS KMKQLAVEGK RVGKVLDHAI
     ETEKMIDKYE TLASDLLTWI EQTIIVLNNR KLANSLAGVQ QQLQAFNTYR TVEKPPKFQE
     KGNLEVLLFT IQSRMRANNQ RVYTPKEGAL VADINRAWER LERAEHERER VLRDELIRQE
     KLEQMARRFD RKAAMRETWL MENQRLVAQD NFGYDLPAVE AAKKKHDAIE TDIAAYEERV
     QALVDISKEL ESERYHDAKR IDARKDNILR LWDYLQELLK ARRARLDKNL TLQRIFQEML
     HIISWMDDMK ARLLSPDFGK HLLEVEDLLQ KHALVENDIA LQADRVHSAS AAALKFANGD
     SYKPCDPQVI RDRVQHLDLC YQELCALAAQ RRAHLEQSRR FWYFLWEVTE LESWIREKEH
     IFSSLDYGKD LTSVLVLQSK HSAFEDELGA RRANLEQVLA EGEKMIQAKH FGSPKVQECM
     DDIRRQWQQL EELAAFRKQN LQDTQRFFQF QGDADELKAW LLDAKRLMSS EDVGHDEYTT
     QRLLKKLNDL RNEAIKNGAT IDALSKQANA LPEELQNTPD IQRRLKDIKD LYMELMSLAD
     LRQKKLDDTM ALYTIFSETD ACELWMGQKE TWLVDLEVPE KLEDLEVVQN RLSILAQDMA
     NVQSRVDDVN KAVKQLEDSR HPRTKEVKEC QTRLNKRWEA FKAMVEDKKR KVDSAVSLHN
     YGLECDETET WIKDKTRVIE STQDLGNDLA AVMTIQRKLF GMERDLAAID TKLTFLRKEA
     DQLAKDHPEN ADDILARRGE LDAAWDTLRK TLKDREDSLG EVSKLQTFLQ DMDDFQSWLF
     KTQKAVASEE MPATLPEAEE QLSLHDAVRE DIGNHEEDFH RVRDTGAQVM QGQEDDPQYQ
     QLEQRLKGMD RGWVELQKMW DSRKNFLDQG VGFQQFMRDG KAVEAILNNQ EYTLAHIDKP
     DTLAGAEKAL KKHEDFVSTM EANEDKIDGA LQGGQRLVDS NNLYSGKVQE KMDSIKDRHD
     KNNRRAQEVS EKLRDNRDLQ HFLQNTQDLT VWINEKMLTA QDTSYDEARN LHSKWLKHQA
     FMAELASNKD WLNNIDQEGQ ELMESKPEFE PIVKERLAKL HELWDKLEST TQEKARLLFD
     ANRSELFDQS LADMKKWLGE LQQQLQSGDE DVKDLTNANI LLKKHQMTEN QVRGRARELE
     ELQEAVRQHG GGREDQPELE AEQQALQRDF QQLLTPLAER KGKLEAAKAV HQFYRDLADE
     LLWIEERMPL AMSEEHGHNL QTVQMLLNKN QTLQREIEGH QPRVDEVLER GRRMAAAANA
     EGRPEADRIT DQLKELEEAW ARLQDEMAKR RERLNGSNLA QQYYNDADEA EAWIGEQELY
     MIADEKAKDE QSAMLMLKRH TILKRAVDDY ADSIQKLADR AQKMFAEDHP DGEEIIRRQG
     QVDKQYAGLK ELAEDRRRKL DHTYHHFLLS REVEDLEHWI AERDVVASSQ EMGQDLDHVT
     LLRDKFRDFA RETGMVGQER VDFVNQTIDE LIEAGHTEAA AMAEWKDGIN DSWADLLELI
     DTRAQLLTAS YELLKYFDDG KELVAQIHEK QKELPDDVGE DFSKAESFHR MHAAFERDIT
     ALGKQVQQFQ ETAARLHAQY AGDRAVAIQA TEQEVVEAWK GLLDACDGRR AQLVDTAEKF
     RFFTMVRDLM AWMESIIQQI ETQEKPRDVS SVELLQKYHQ GIRSEIEARG VKFSDCMDLG
     KALLTRKHRD SAEIKEKLVQ LMEKRKEMMF KWDDRWDWLR LLLEVCQFAR DASVAEAWLI
     AQEPYVTSRD LGHTVDEVEK LLKRHEAFEK STATWEERFS ALERLTTLEL LELRKQQQEM
     EQFIKDEQRS DKESRREDTG FVEESSQLYT IEEQTLSGSG AIEPSSGLLE GAAGDSTVPI
     ESEMRESGSL ELEPSVSVVT PREPERAATM PVEPLRAHTV LLEGTLGRKH DVEGSGKKAS
     NRSWNNLYCV LKPGQLSAYK DAKSFGHGTT YHGEDPQSLS NASWEILTTY KKKKHVAKLR
     LGDGSEYLFQ CKDEEELQRW SQAMDKAVQP LAAEEASGPS GAKAHSLPPP SSSAALPEPS
     SAKKDKEKKF SRFAKKK
//
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