ID A0A3P9AKS5_ESOLU Unreviewed; 2339 AA.
AC A0A3P9AKS5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN Name=SPTBN1 {ECO:0000313|Ensembl:ENSELUP00000041295.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000041295.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000041295.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000041295.2}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_010862787.1; XM_010864485.2.
DR STRING; 8010.ENSELUP00000041295; -.
DR Ensembl; ENSELUT00000042590.2; ENSELUP00000041295.2; ENSELUG00000022149.2.
DR GeneID; 105006131; -.
DR GeneTree; ENSGT00940000154864; -.
DR OrthoDB; 2872403at2759; -.
DR Proteomes; UP000265140; LG09.
DR Bgee; ENSELUG00000022149; Expressed in heart and 15 other cell types or tissues.
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; 8.
DR Gene3D; 1.20.58.60; -; 12.
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; 13.
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:UP000265140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 45..149
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 165..270
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2172..2282
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 2079..2173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2285..2339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 449..483
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 983..1017
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2079..2093
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2102..2126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2133..2173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2285..2314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2315..2333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2339 AA; 270029 MW; 43CB41A009B07479 CRC64;
MDVDWELGGQ DGQYTDPDHG YTAQVAFNYN MLEGRFKQLQ DEREAVQKKT FTKWVNSHLS
RVSCRITDLY RDLSDGRMLI KLLEVLSGER LPKPTKGRMR IHCLENVDKA LQFLKEQRVH
LENMGSHDIV DGNHRLTLGL IWTIILRFQI QDISVETDGD NKEKRSAKDA LLLWCQMKTA
GYPNVNIHNF STSWRDGMAF NALIHKHRPD LIDFEKLKKS NAHHNLQNAF NLAEQHLGLT
KLLDPEDISV DHPDEKSVIT YVVTYYHYFS KMKALKVEGK RIGKVLDNAI ETEKMIEKYE
SLASDLLEWI EQTIIILNNR KFANSLNGVQ QQLQAFNTYR TVEKPPKFTE KGNLEVLLFT
IQSKMRANNQ KVYMPREGKL ISDINKTWEK LEKAEHEREL ALRTELIRQE KLEQLARRFD
RKAAMRETWL SENQRLVSQD NFGFDLPAVD AATKKHEAIE TDITAYEERV QAVVSVAKEL
ETENYHDIKR IVARKDNVIR LWEYLLELLK ARRQRLELNL GLQRVFQEML YIMDWMDEMK
MMLLSQEYGK HLLGVEDLLQ KHALVEADIS IQADRVKAVN NNAQKFAIDG DVYKPCDPQV
IRDRVAHMEF CYQELAQLAA ERRARLEESR RLWKFFWEMA EEEGWIREKE QILSSDETGK
DLTGAMRLLS QHRALEDEMS GRAGHLQNTI AEGQAMADAG HFGAAKIRER IADLQAQWAA
LEELANVQKA RLEEACALHQ FQADAGDVDA WTLDALRIVS SGEVGHDEFS TQALVRKHKA
ASAEVASYRP VIDALHEQAA TLPKEQIQSE EVKGRLSGIE ERYKEVAELT RLRKQALQDA
LALYKMFSEA DACEVWIDEK EQWLNSMEIP EKLEDLEVIQ HRFESLEPEM NNQASRVAVV
NQIARQLMHN GHPSEKDIKA QQDKLNNRWS QFRDLVDQKK EFLHSALGVQ NYHLECNETK
SWIREKTKVI ESTQELGNDL TGVMALQRKL TGMERDLAAI EDKLGDLRGE AERLAGEHPD
QANAITGRLA EITAVWEEMK ATLRNREESL GEASKLQQFL RELDDFQSWL SRTQTAIASE
ETPNTLAEAE KLLAQHESIK NEICNYEEDY QKMRDMGEMV TQGQTDAQYM FLRQRLQALD
TGWNELHKMW ENRQNLLSQS HAYQLFLRDT KQAETFLNNQ EYVLAHTEMT TTLEGAEGAI
KKQEDFMTTM DANEEKINGV VEAGRRLASD GNINGDRIQE RATSIDDRHK KNREAAVELL
MRLKDNRDLQ KFLQDCQELS LWINEKMLTA QDMSYDEARN LHSKWLKHQA FMAELQSNKE
WLDKIEKDGM LLVSEKPETE SVVREKLSAL QKMWEDLEST TQTKAQCLFD ANKAELFTQS
CADLDKWLGG LEGQIQSDDY GKDLTSVNIL LKKQQILENQ VEVRQREVVE LQSQALALSQ
EGKDTEEVDG QRQVVEHKLK ELLEPLRKRK NFLMASREIH QFNRDVEDEI LWVEERLPIA
TSTDHGLNLQ TVQLLIKKNQ TLQKEIQGHQ PRCNDIFERS ESLLKEDSLA VEAIRQRLAD
LKQLWSRIIE ETEKRHARLE EAHNAQKYYF DAAEAEAWMS EQELYMMSEE KAKDEQSAVA
MLKKHQIVEQ SVEDYAETVH QLSKTSRGLT AAGHPESERI GMRQSQVDKL YAGMKDLSEE
RRGKLDERLR LFQLNREVDD LEQWIAEREV VAGSHELGQD YEHVTMLQER FREFARDTGN
IGQERVDAVN RMADELINAG HADAATVAEW KDGLNEAWAD LLELIDTRTQ ILAASYELHK
FYHDAKEILG RILDKHKKLP EEVGRDQNTV ETLQRMHTTF EHDIQALGTQ VRQLQEDAVR
LQSAYAGDKA DDIQRRESEV LEAWKTLLEA CDGRRVHLLD TGDKFRFFSM VRDLMLWMED
VIRLIEAQEN PRDVSSVELL MNNHQGIKAE IDARNDNFTA CIELGKSLLA RKHYASEEIK
DKLLQLMDKR KDMIDKWEDR REWLRLILEV HQFGRDAGVA EAWLLGQEPY LFGRELGQSV
DEVEKLIKRH EAFEKSAATW EERFSALERL TTLELLEVRR QQEEEERRKP PSPEPLPMQE
SPPQSGLENG LQNGLPSDQD SPRNCVNGVE IMNGVAEQNS KDPSPIPSPT ASQRGKGSIS
SALPSKNQDS PTAQLEGFLH RKHEWEGHNK KASSRSWHNV YCVINNQEMG FYKDNKAAGQ
GIPYHNEIPI SLMGAVCDVA MDYKKKKHVF KLRVTDGNEY LFQAKDEEEM STWIQAILNA
GTPDKISITP SNQSTPATSR AQTLPTTVTL TTESSPGKRE KDKEKDKEKR FSLFSKKKQ
//
