ID A0A3B4XKB6_SERLL Unreviewed; 2038 AA.
AC A0A3B4XKB6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN Name=SPTBN1 {ECO:0000313|Ensembl:ENSSLDP00000016180.1};
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:ENSSLDP00000016180.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000016180.1}
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.ENSSLDP00000016180; -.
DR Ensembl; ENSSLDT00000016776.1; ENSSLDP00000016180.1; ENSSLDG00000012799.1.
DR GeneTree; ENSGT00940000154864; -.
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: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; -; 12.
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; 1.
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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..73
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 88..200
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT REGION 2010..2038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 379..413
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 913..947
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1019..1046
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1344..1371
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1474..1501
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2038 AA; 236948 MW; 2FC2AD88675CEBA0 CRC64;
SDCGSGSLVV ILVLLPKPTK GRMRIHCLEN VDKALQFLKE QRVHLENMGS HDIVDGNHRL
TLGLIWTIIL RFQIQDISVE TEDNKEKRSA KDALLLWCQM KTQLTCGPNE AYPNVNIHNF
TTSWRDGMAF NAIIHKHRPD LIDFDKLKKS NAHYNLQNAF NLAEQHLGLT KLLDPEDISV
DHPDEKSVIT YVVTYYHYFS KMKALKVEGK RIGKVLDNAI ETEKMIEKYE SLASDLLEWI
EQTIIILNNR KFANSLLGVQ QQLQAFNTYR TVEKPPKFTE KGNLEVLLFT IQSKMRANNQ
KVYMPREGKL ISDINKAWER LEKAEHEREL ALRTELIRQE KLEQLARRFD RKAAMRETWL
SENQRLVSQD NFGFDLQAVE AATKKHEAIE TDIAAYEERV QAVVAVAKEL EVEHYHDIKR
ITARKDNVIR LWEYLLELLK ARRLRLEMNL GLQRVFQEML YIMDWMDEMK MLLLSQDYGK
HLLGVEDLLQ KHALVEADIA IQADRVKAVT TNANKYSVND SGYKPCDPQV IQDRVAHLEF
CYQELTQLAA ERRARLEESR RLWKFFWEMA EEEGWIREKE QILSSLEHGK DLTGALRLLS
QQRALEDEMS GRAGHLQHTI DEGQAMVQAG HFAAAKIHER IEDLQAQWAA LEQLAAVRKR
RLEEALALHQ FQADADDVDA WTFDALRIVS SGETGHDEFS TQALVRKHKD AAAEVASYRP
VIDSLHEQAA SLPKEEVESD EVRGRLAGIE ERYKEVSELT KLRKQALQDA LALYKMFSEA
DACEVWIDEK ELWLNSMEIP EKLEDLEVIQ HRFESLEPEM NNQASRVAVV NQIARQLIHN
GHPSEKDIKT QQDKLNNRWS QFRDLVDQKK ESLNSALGVQ NYHLDCNETK SWIKEKTKVI
ESTQELGNDL TGVMALQRKL TGMERDLAAI EDKLGDLRSE AQRLAEEHPD QAKAITGRLA
EITAVWEEMK NTLKNREESL GEARKLQQFL RELDDFQSWL SRTQTAIASE DMPNTLAEAE
KLMAQHEGIK NEIQNYEEDY QKMRDMGEMV TQGQNDAQYM FLRQRLQALD TGWNELHKMW
ENRQNLLSQS HAYQLFLRDT KQAEAFLNNQ EYVLAHTEMP TTLEAAEAAI KKQEDFMTTM
DANEDKINSV VEAGRRLASD GNINAERIQE RVSSIDDRHK KNREAAVELL MRLKDNRDLQ
KFLQDCQELS LWINEKMLTA QDMTYDEARN LHSKWLKHQA FMAELQSNKE WLDKIQKDGM
LLVSEKPETE AVVKEKLSAL HAMWEELEST TQTKAQCLFD ANKAELFTQS CADLDKWLVG
LEGQIQSDDY GKDLTSVNIL LKKQQMLENQ VEVRQREVVE LQSQVKALGQ EVKDTDEVDG
RRQLVERKFQ ELLDPLRRRR NFLVASREVH QFNRDVEDEI LWVQERMPVA TSTDHGHNLQ
TVQLLIKKNQ TLQKEIQGHQ PRIDDILERS QSLLQDESSN ADVIRQRLAD LQELWRQLME
EGERRHARLE EAHKAQQYYF DAAEAEAWMS EQELYMMSEE KAKDEQSAVT MQKKHQIVEQ
AVEDYAEAVH QLSKTSRGLV ADGHPESERI SMRQSQVDKL YAGLKDLSEE RRGKLDERLR
LFQLNREVDD LEQWIAEREV VAGSHELGQD YEHVTMLQER FREFARDTGN IGQERVDAVN
RLADELINTG HGDAATVAEW KDGLNEAWAD LLELIDTRTQ ILAASFELHK FYHDAKEILG
RIVDKQKKLP EEVGRDQNTV ETLQRMHTTF EHDIQALGTQ VRQLQEDAVR LQSAYAGDKA
DDIQRRESEV LEAWRSLLEA CDGRRLRLLD TGDKFRFFSM VRDLMLWMDD VIRLIEAQEK
PRDVSSVELL MNNHQGIKAE IDARNDSFTA CIELGKALLA RKHYASEEIK EKLLQLTDKR
KEMIDKWEDR WEWLRLILEV HQFSRDAGVA EAWLLGQEPY LSSREMGQSV DEVEKLIKRH
EAFEKSAATW EERFSALERL TTLELLEVRR QQEEEERRRK PPSPEPAVIQ QEECQQER
//
