ID A0A3Q2WB13_HAPBU Unreviewed; 2011 AA.
AC A0A3Q2WB13;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN Name=SPTBN1 {ECO:0000313|Ensembl:ENSHBUP00000022928.1};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000022928.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000022928.1}
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 STRING; 8153.ENSHBUP00000022928; -.
DR Ensembl; ENSHBUT00000012395.1; ENSHBUP00000022928.1; ENSHBUG00000003534.1.
DR GeneTree; ENSGT00940000154864; -.
DR OMA; NFGYDLQ; -.
DR Proteomes; UP000264840; 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:0005200; F:structural constituent of cytoskeleton; IEA:UniProtKB-UniRule.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-UniRule.
DR CDD; cd21248; CH_SPTB_like_rpt2; 1.
DR CDD; cd00176; SPEC; 8.
DR Gene3D; 1.20.58.60; -; 10.
DR Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR016343; Spectrin_bsu.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR11915:SF226; SPECTRIN BETA CHAIN, NON-ERYTHROCYTIC 1; 1.
DR PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF00435; Spectrin; 17.
DR PIRSF; PIRSF002297; Spectrin_beta_subunit; 2.
DR SMART; SM00033; CH; 2.
DR SMART; SM00150; SPEC; 17.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 13.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
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|PIRNR:PIRNR002297};
KW Reference proteome {ECO:0000313|Proteomes:UP000264840};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..79
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 94..199
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT REGION 1988..2011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 378..412
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 996..1023
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1321..1348
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1751..1808
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2011 AA; 233608 MW; 5198BC2F385B9762 CRC64;
MDLRDGRMLI KLLEVLSGER LPKPTKGRMR IHCLENVDKA LQFLKEQRVH LENMGSHDIV
DGNHRLTLGL IWTIILRFQI QDISVETEDN KEKKSAKDAL LLWCQMKTAG YPNVNIHNFT
TSWRDGMAFN ALIHKHRPDL IDFDKLKKSN AHYNLQNAFN LAEQHLGLTK LLDPEDISVD
HPDEKSIITY VVTYYHYFSK MKALKVEGKR IGKVLDNAIE TEKMIEKYES LASDLLEWIE
QTIIILNNRK FANSLVGVQQ QLQAFNTYRT VEKPPKFTEK GNLEVLLFTI QSKMRANNQK
VYTPREGKLI SDINKAWERL EKAEHERELA LRTELIRQEK LEQLARRFDR KAAMRETWLS
ENQRLVSQDN FGFDLQAVEA ATKKHEAIET DIAAYEERVQ AVVAVAKELE AESYHDIKRI
TARKDNVIRL WEYLLELLKA RRQRLEMNLG LQRVFQEMLY IMDWMDEMKM LLLSQDYGKH
LLGVEDLLQK HALVEADISI QADRVRNVNR NAQKFASDTE DYKPCDPQII KDRVAHLEFC
YQELNQLAAE RRARLEESRR LWKFFWEMAE EEGWIREKEQ ILSSEDYGKD LTGSLRLLSQ
HKAFEDEMTG RAAHLQQTIK QGEELVADNH FGADKIKERI KDIQVRRTCA AVTHDTIESP
PATSTSSSVD VGHDEFSTQA LVKKHKDVAE EIGSYRPVID ALHEQSRTLP PEKANSEEVQ
SRLAGIEERY KEVAELTRLR KQALQDALAL YKMMSEADAC EVWIDEKEQW LNSMDIPEKL
EDLEVVQHRF ESLEPEMNSQ ASRVAVVNQV ARQLIHSGHP SEKEIKAQQD KLNTRWSQFR
DLVDQKKESL NSALGVQNYH LECNETKSWI KEKTKVIEST QELGNDLAGV MALQRKLTGM
ERDLVAIQDK LSDLGKEAER LGSEHPEQSE AIKGRLAEIT GVWDEMKDTL KNREESLGEA
SKLQQFLRDL DDFQSWLSRT QTVIASEDMP NTLAEAEKLL AQHEGIKNEI RNYEEDYQKM
RDMGEMVTQG QTDAQYMFLR QRLQALDTGW NELHKMWENR QNLLSQSHAY QLFLRDTKQA
EAFLNNQEYV LAHTEMPTTL EGAEAAIKKQ EDFMTTMDAN EEKIGAVVDT GRRLVADDNI
NAERIQEKVD SIDQRHKKNR AAASDLLTRL KDNRDLQKFL QDCQELSLWI NEKMLTAQDM
SYDEARNLHS KWLKHQAFMA ELQSNKEWLD KINKDGQTLM AEKPDTEAMV KEKLASLQTM
WDELESTTQT KAKCLFDANK AELFTQSCAD LDKWLGGLEA QLQSDDYGKD LTSVNILLKK
QQILESQVDV RQKEVEELQK QSQALSQEGK GSEEVDGQRV TVERKFQTLQ EPLKKRRDHL
MASREIHQFN RDVEDEILWV EERMPLATST DHGHNLQTVQ LLIKKNQTLQ KEIQGHQPRY
DDIFERSQHV LREDSPTTEL IRQRLADLQS LWEQIKKETE KRHTRLSEAH EAQQYYFDAA
EAEAWMSEQE LYMMSEEKAK DEQSSVAMLK KHQILEQAVE DYADTVHQLS STSRGLVAAG
HPDSERIGMR QSQVDKLYAG LKDLSEERRG KLDERFRLFQ LNREVDDLEQ WIAEREVVAG
SHELGQDYEH VTMLQERFRE FARDTGNIGQ ERVDGVNKLA DELINTGHGD AATIAEWKDG
LNEAWADLLE LIDTRTQILA ASYELHKFYH DAKEILNRIL DKHKKLPEEL GRDQNTVETL
QRMHTTFEHD IQALGTQVRQ LQEDAVRLQS AYAGDKADDI QKREGEVLEA WKNLLEAAEG
RRAKLVDTGD KFRFFSMVRD LMLWMEDVIR LIEAQEKPRD VSSVELLMNN HQGIKAEIDA
RNDSFTACIE LGKALLARKH YASEEIKEKL LQLTDKRKDM IDKWEDRWEW LRLVLEVHQF
SRDAGVAEAW LLGQEPYLSS REMGQSVDEV EKLIKRHEAF EKSAATWEER FAALERLTTM
ELLEVRRRQE EEEKKRQPPA EAQPADAAAQ R
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