ID A0A3B1IWF8_ASTMX Unreviewed; 2333 AA.
AC A0A3B1IWF8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN Name=SPTBN1 {ECO:0000313|Ensembl:ENSAMXP00000034046.1};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000034046.1, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000034046.1}
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; ENSAMXT00000030945.1; ENSAMXP00000034046.1; ENSAMXG00000009193.2.
DR GeneTree; ENSGT00940000154864; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000009193; Expressed in brain and 12 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; cd21248; CH_SPTB_like_rpt2; 1.
DR CDD; cd10571; PH_beta_spectrin; 1.
DR CDD; cd00176; SPEC; 8.
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:UP000018467};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 54..158
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 173..278
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2177..2287
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 2090..2177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2289..2333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 991..1025
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1097..1124
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1422..1449
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2114..2129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2144..2174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2289..2313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2333 AA; 269506 MW; D188A53CA23E87DD CRC64;
MTSVAADFDH MEIQQQFTSD VNNRWDADEW DNENSSARLF ERSRIKALAD EREAVQKKTF
TKWVNSHLAR VSCRITDLYM DLRDGRMLIK LLEVLSGEKL PKPTKGRMRI HCLENVDKAL
QFLKEQRVHL ENMGSHDIVD GNHRLTLGLI WTIILRFQIQ DISVETEDNK EKKSAKDALL
LWCQMKTAGY PNVNIHNFTT SWRDGMAFNA LIHKHRPDLI DFDKLKKSNA HYNLQNAFNL
AEQHLGLTKL LDPEDISVEH PDEKSIITYV VTYYHYFSKM KALKVEGKRI GKVLDNAIET
EKMIEKYESL ASDLLEWIEQ TIIILNNRKF ANSLVGVQQQ LQAFNTYRTV EKPPKFTEKG
NLEVLLFTIQ SKMRANNQKV YMPREGKLIS DINKAWERLE KAEHERELAL RTELIRQEKL
EQLARRFDRK AAMRETWLSE NQRLVSQDNF GFDLQAVEAA TKKHEAIETD IAAYEERVQV
VVAVAGELEA ENYHDIKRIT ARKDNVLRLW DYLLELLRAR RQRLELNLGL QRVFQEMLYI
MDWMDEMKML LLSQDYGKHL LGVEDLLQKH ALVEADIAIQ ADRVKSVNSN AQKFADDSEG
YKPCDPQVIR DRVAHMEFCY QELTQLAAER RGRLEESRRL WKFFWEMAEE EGWIREKEQI
LSSEDCGKDL TAVVRLLSKH KALEDERSGR AGRLQQTVQQ GEELVAAGHF GADKIRQRIS
DVQEQWASLE RLFSARRTRL QDACALHQFQ ADADDMDAWM LDVLRIVSSA DVGHDEFSAQ
SLVKKHKDVA EEISSYRPVL DALHEQARTL PEEQARAGEV SGRLAGIEER YKEVAELTRL
RKQALQDALA LYKMLSEADA CELWIVEKEQ WLNSMEIPEK LEDLEVIQHR FDSLEPEMNS
QASRVAVVNQ IARQLIHSGH PSEKEIKGQQ DKLNTRWSQF RDLVDRKKEA LNSTLGVQNY
YLECNETKSW IREKTKVIES TQDLGNDLAG VMALQRKLTG MERDLVAIED KLGDLGKEAD
RLSEEHGDKA SGIKGRLGEI KDVWEEMKGT LRTREESLGE ASKLQQFLRE LDDFQAWLSR
TQTAVASEDK PNTLAEAEKL LAQHEGIKNE IRNYEEDYQK MRDMGEMVTQ GQTDAQHMFL
RQRLQALDTG WNELQKMWEN RQKLLSQSHA YQLFLRDTKQ AEAFLNNQEY VLAHTEMADT
LEGAEAAIKK QEDFMTTMDA NEEKINAVVE TGRRLVSDGN ISAERIQEKV DSIDERRKKN
RGAASELLTK LKDNRDLQRF LQDCQELSLW ISEKMLTAKD MSYDEARNLH SKWLKHQAFM
AELQSNKEWL DKIQKAGSAL VEEKPETEAV VQGKMEMLKK TWEELESTTQ TKAQCLFDAN
KAELFTQSCA DLDKWLSGLE GQIHSDDFGK DLTSVNILLK KQQMLESQVE VRQKEVEELR
SQAQALSQEG KGSDEVDGRR RGVEVKFQQV QEPLKKRRSN LMASREIHQF NRDVEDEILW
VEERMALATS TDHGNNLQTV QLLIKKNQTL QKEIQGHQPR YDDIFERSVR TLQEESPVSA
GIRLRLEDLQ RIWKLIQEEV EKRHGRLEEA HRAQQYYFDA AEAEAWMSEQ ELYMMSEEKA
KDEQSSVAML KKHQILEQAV EDYAETVHQL SKTSRALVAA GHPESERISM RQSQVDKLYA
GLKDLSEERR GKLDERSRLF QLNREVDDLE QWIAEREVVA GSHELGQDYE HVTMLQERFR
EFARDTGNIG QERVDAVNKM ADDLINSGHA DAATIAEWKD GLNEAWADLL ELIDTRTQIL
AASYELHKFY HDAKEVLGRI LDKHKKLPDE LGRDQNTVET LQRMHTTFEH DIQALGTQVK
QLQEDAVRLQ SAYAGDKADD IQRREGEVLE AWRSLLEACD GRRVRLLDTS DKFRFFSMVR
DLMLWMEDVI RLIDAQEKPR DVSSVELLMN NHQGIKAEID ARNDSFTTCI ELGKALLARK
HYASEEIKEK LLQLTDKRKE MIDKWEDRWE WLRLVLEVHQ FSRDAGVAEA WLLGQEPYLS
SREMGQNVDE VEKLIKRHEA FEKSAATWEE RFSALERLTT MELLEVRRMQ EEEEKKRQPP
PEEAPPAEEP SPQQREGEQV SQNGLPTEQD SPREAAGGSD VVNGVAETSP SSSPTGSRKG
KASQAATLPT KAQDTPPAQI EGFLNRKHEW EGHNKKASNR SWHNVYCVIN NQEMGFYKDS
KSASQGIPYH SEIPISLKDS TCEIALDYKK RKHVFKLKLS DGNEYLFQAK DDEEMNSWIQ
AISCATPSEI SSHSTPASGR AHTLPASASV SDSSPGKREK DKEKRFSLFS KKK
//
