ID A0A3Q1CFN4_AMPOC Unreviewed; 2377 AA.
AC A0A3Q1CFN4;
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:ENSAOCP00000024304.1};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000024304.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000024304.1}
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; 80972.ENSAOCP00000024304; -.
DR Ensembl; ENSAOCT00000003104.1; ENSAOCP00000024304.1; ENSAOCG00000011119.1.
DR GeneTree; ENSGT00940000154864; -.
DR Proteomes; UP000257160; 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; cd21248; CH_SPTB_like_rpt2; 1.
DR CDD; cd10571; PH_beta_spectrin; 1.
DR CDD; cd00176; SPEC; 9.
DR Gene3D; 1.20.58.60; -; 11.
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:SF226; SPECTRIN BETA CHAIN, NON-ERYTHROCYTIC 1; 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:UP000257160};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 85..189
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 204..309
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2213..2323
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2124..2214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2326..2377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 488..558
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1022..1056
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1128..1155
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1453..1480
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2151..2165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2181..2214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2326..2356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2377 AA; 273247 MW; 1B400FC880A7DA7F CRC64;
MELQTGLPGP LTPVPLSPTS DYAGPLSPSS GGPGPSHGAS PGRGPSPSLS PIRGPSPGPG
FSGQAAFNYN QLEGRFKQLQ DEREAVQKKT FTKWVNSHLS RVSCRITDLY MDLRDGRMLI
KLLEVLSGER LPKPTKGRMR IHCLENVDKA LQFLKEQRVH LENMGSHDIV DGNHRLTLGL
IWTIILRFQI QDISVETEDN KEKKSAKDAL LLWCQMKTAG YPNVNIHNFS 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 RRQRLESNLG LQRVFQEMLY IMDWMDEMKM LLLSQDYGKH LLGVEDLLQK
HALVEADIGI QADRVRNVNS NAQKFANDTE GYKPCDPQII RDRVAHMEFC YQELSQLAAE
RRARLEESRR LWKFFWEMAE EEGWIREKEQ ILSSEDYGKD LTGALRLLSQ HKAFEDEMSG
RAAHLQQTIK QGEELVANNH FGADKIKERN QDIQEQWAAL ERLSAVRKAR LQEACNQHQF
QADADDIDTW MLDVLRIVSS VDVGHDEFST QALVKKHKDV AEEIASYRPV IDALHEQSRT
LPPEKANSEE VQSRLAGIEE RYKEVVELTR LRKQALQDAL ALYKMLSEAN ACEVWIDEKE
QWLNSMEIPE KLEDLEVVQH RFESLEPEMN NQASRVAVVN QVARQLIHSG HPSEKEIKAQ
QDKLNTRWSQ FRDLVDQKKD SLSSALGVQN YHLECNETKS WIKEKTKVIE STQELGNDLA
GVMALQRKLT GMERDLAAIE DKLGDLGKEA DRLASEHPEQ SEAIKGRLAE ITGVWEEMKD
TMKNREESLG EASKLQQFLR ELDDFQSWLS RTQTAIASED MPNTLAEAEK LLAQHEGIKN
EIRNYEEDYQ KMRDMGEMVT QGQTDAQYMF LRQRLQALDT GWNELHKMWE NRQNLLSQSH
AYQLFLRDTK QAEAFLNNQE YVLAHTEMPT TLEGAEAAIK KQEDFMTTMD ANEEKISGVV
DTGRRLVADG NISAERIQEK VDSIDQRHKK NRAAASDLLA RLKDNRDLQK FLQDCQELSL
WINEKMLTAQ DMSYDEARNL HSKWLKHQAF MAELQSNKEW LDKIDKDGQT LMAEKPETEA
MVKEKLASLK TMWQDLESTT QTKAKCLFDA NKAELFTQSC ADLDKWLGNL DGQLQSDDYG
KDLTSVNILL KKQQILESQV EVRQKEVEEL RSQSQALSQE GKGSEEVDGQ RISVEKKFQS
LQDPLKKRRD NLMASREIHQ FNRDVEDEIL WVEERMPLAT STDHGHNLQT VQLLIKKNQT
LQKEIQGHQP RYDDIFERSQ HVLREDSPTA EMIRQRLTGL QTLWEQIRKE TEKRHARLSE
AHEAQQYYFD AAEAEAWMSE QELYMMSEEK AKDEQSSVAM LKKHQILEQA VEDYADTVHQ
LSSTSRGLVA AGHPDSERIG MRQSQVDKLY AGLKDLSEER RGKLDERFRL FQLNREVDDL
EQWIAEREVV AGSHELGQDY EHVTMLQERF REFARDTGNI GQERVDTVNR LADDLINAGH
GDAATIAEWK DGLNEAWADL LELIDTRTQI LAASYELHKF YHDAKEILNR ILDKHKKLPE
ELGRDQNTVE TLQRMHTTFE HDIQALGTQV RQLQEDAVRL QSAYAGDKAD DIQKREGEKR
KGEVLEAWKN LLEAAEGRRV KLVDTGDKFR FFSMVRDLML WMEDVIRLIE AQEKPRDVSS
VELLMNNHQG IKAEIDARND SFTACIELGK ALLARKHYAS EEIKEKLLQL TDKRKDMIDK
WEDRWEWLRL VLEVHQFSRD AGVAEAWLLG QEPYLSSREM GQNVDEVEKL IKRHEAFEKS
AATWEERFAA LERLTTMELL EVRRRQEEEE RRRQPPAAEG QTAEAAAQQR EGEPVSQNGL
PSDQESPREN VEGAEVVNGV SEPSPSGSPG ASRKGKASQA ATLPAKTQQD APTSQLEGFL
HRKHEWEGHN KKASSRSWHN VYCVINQQEM GFYKDQKSAS QGIPYHSEIP VSLKDAVCEV
AVDYKKKKHV FKLKITDGNE YLFQAKDDEE MNTWISAISA AVSGDKSEVT PSSHSTPAPA
ARAQTLPASV ATATAESSPG KREKDKEKRF SLFSKKK
//
