ID A0A3Q1EQW0_9TELE Unreviewed; 2357 AA.
AC A0A3Q1EQW0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000007276.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000007276.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the spectrin family.
CC {ECO:0000256|ARBA:ARBA00006826, ECO:0000256|PIRNR:PIRNR002297}.
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DR Ensembl; ENSAPOT00000005194.1; ENSAPOP00000025859.1; ENSAPOG00000009237.1.
DR Ensembl; ENSAPOT00000005214.1; ENSAPOP00000007276.1; ENSAPOG00000009237.1.
DR GeneTree; ENSGT00940000158908; -.
DR Proteomes; UP000257200; 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; 14.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW 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..2153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2165..2184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2310..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"
FT COMPBIAS 2123..2153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2357 AA; 272990 MW; 4245A60A9016CEEC CRC64;
MTSTTDFDNV EITQQYSHIN TRFDLSDEEL DNDNSSARLF ERSRIKALAD EREAVQKKTF
TKWVNSILSR VGCRISDLYL DLRDGRMLIK LLEVLSGERL PKPTKGRMRI HCLENVDKAL
QFLKEQRVHL ENMGSHDIVD GNHRLILGLI WTIILRFQIQ DIVVETGQAD QKETRSAKDA
LLLWCQMKTA GYPNVNITNF TTSWKDGMAF NALIHKHRPD LLDYNRLKRS NPTHNLQNAF
NVAEQKLGVT KLLDPEDVFT ENPDEKSIIT YVVAFYHYFS KMKQLAVEGK RVGKVLDHAI
ETEKMIDKYE TLASDLLTWI EQTIIVLNNR KLANSLTGVQ QQLQAFNTYR TVEKPPKFQE
KGNLEVLLFT IQSRMRANNQ RVYTPKEGAL VADINRAWER LERAEHERER VLRDELIRQE
KLEQMARRFD RKAAMRETWL LENQRLVAQD NFGYDLPAVE AAKKKHDAIE TDIAAYEERV
KALVNISKEL ESERYHDAKR IDVRKDNILR LWDYLQELLK ARRGRLDKNL TLQRIFQEML
HIISWMDDMK ARLLSPDFGK HLLEVEDLLQ KHALVENDIA LQAERVQSAS ASALKFANGD
SYKPCDPQVI RDRVQHLDLC YQELCALAAQ RRARLEQSRL FWNFLWEVTE LESWIREKEH
IFSSMDYGKD LTSVLVLQSK HSAFEDELGA RRANLEQLLG EGEKMIQAKH FGSPKVQESM
DDIRRQWQQL EELAAFRKQN LQDTQTFFQF QGDADELKAW LLDAKRQMSS DDVGHDEYTT
QRLLKKHNNL KNEAIKNGAT IDALSKQANG LPEELQNTPD IQRRLKDIKD LYMELMSLAD
LRQKKLDDTM ALYTIFSETD ACELWMGQKE TWLVGLEVPE KLEDLEVVQN RLSILAQDMA
NVQSRVDDVN KAVKQLEDSR HPRTKEVKDC QTRLNKRWEA FKAMVEDKKR KTDSAVSLQN
YGLECDETEA WIKDKTRVIE STQDLGNDLA AVMTIQRKLF GMERDLAAIN TKLTFLRKEA
DQLAQDHPES AADILARRGE LDDAWDTLRK TLKDREDSLG EVSKLQTFLQ DMDDFQSWLF
KTQKAVASEE MPATLPEAEE QLSLHDAVRE DINNREEDYH RVRDTGAQVT QGQEDDPQYQ
QLLQRLNGMD RGWYELQKMW DSRKNFLDQG LGFQQFMRDG KAVEAILNNQ EYTLAHIDKP
DTLDGAEKAL KKHEDFVSTM EANVDKIDGA VQGGQRLVDS NNLYSGKVQE KMDSIKDRHN
KNKRRAEEVS EKLRDNRDLQ HFLQNTQDLT VWINEKMLTA QDTSYDEARN LHSKWLKHQA
FMAELASNKD WLNKVDQEGQ ELMESKPEFE PIVKERLAKL HELWDKLEST TQEKARLLFD
ANRSELFDQS QADMKKWLGE LQQQLQSGDE DVKDLTNANI LLKKHQMTEN QVRDRARELE
ELQEAVRKHG GGREDQPELE AEQQALQREF QQLLTPLAQR KGKLEAAKAV HQFYRDLADE
LLWIEERMPL AMSQEHGHNL QTVEMLSKKN QTLQREIEGH QPRVDEVLER GRRMASAASA
EGRPEAERIT EQLKELEEAW ARLQDEMAKR RERLNGSNLA QQYYNDADEA EAWIGEQELY
MIADEKAKDE QSAMLMLKRH MILKQAVEDY SDSIQKLADR AHKMFAEDHP DGEEIIRRQG
QVDKQYAGLK ELAEDRRKKL DHTYHHFLLS REVEDLEQWI AERDVVASSQ EMGQDLDHVT
LLRDKFRDFT RETGMAGQER VDMVNQTIDE LIEAGHTEAA AMAEWKDGIN ESWADLLELI
DTRAQLLTAS YELLKYFDDG KELVAQIHEK QNELPEDVGE DFSKAESFHR MHAAFERDIS
ALGKQVQQFQ ETASRLHAQY AGDRADAIQA TEREVVEAWK GLLDASDGRR AQLVDTAEKF
RFFTMVRDLM AWMESIIQQI ETQEKPRDVS SVELLQKYHQ GIRSEIETRG AKFTDCTDLG
KALLTRKHRD SAEIKEKLVQ LMDKRKEMMF KWDDRWDWLR LLLEVCQFAR DASVAEAWLV
AQEPYVTSRD LGQTVDEVEK LLKRHEAFEK STATWEERFS ALERLTTLEL LELRKQQQEM
EQFIKEEQRS DKDSRREDTG FVEESSQLYT IEEQTLSGTV EPSSGLQEGT AGDSTVPIVS
EIRESASLEL EPEPSLSSVT PKEPERAATM PMESLRAQTV LQQGMLGRKH DVEGSGKKAS
NRSWNNLYCV LKPGQLSAYK DAKSFDHGVT YHGEDPLSLN NASWEMLTTY KKKKHVAKLR
LADGSEYLFQ CKDEEELQRW SQAMEKAVQS LAAEEASGPS GAKAHSLPPP SSSAALPEPS
SAKKDKEKKF SRFAKKK
//
