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Database: UniProt
Entry: R7TST9_CAPTE
LinkDB: R7TST9_CAPTE
Original site: R7TST9_CAPTE 
ID   R7TST9_CAPTE            Unreviewed;      2338 AA.
AC   R7TST9;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN   ORFNames=CAPTEDRAFT_148581 {ECO:0000313|EMBL:ELT96714.1};
OS   Capitella teleta (Polychaete worm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Sedentaria; Scolecida; Capitellidae; Capitella.
OX   NCBI_TaxID=283909 {ECO:0000313|EMBL:ELT96714.1};
RN   [1] {ECO:0000313|Proteomes:UP000014760}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=I ESC-2004 {ECO:0000313|Proteomes:UP000014760};
RA   Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA   Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA   Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA   Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA   Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ELT96714.1, ECO:0000313|Proteomes:UP000014760}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=I ESC-2004 {ECO:0000313|EMBL:ELT96714.1,
RC   ECO:0000313|Proteomes:UP000014760};
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
RN   [3] {ECO:0000313|EnsemblMetazoa:CapteP148581}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the spectrin family.
CC       {ECO:0000256|ARBA:ARBA00006826, ECO:0000256|PIRNR:PIRNR002297}.
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DR   EMBL; AMQN01011188; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KB308745; ELT96714.1; -; Genomic_DNA.
DR   STRING; 283909.R7TST9; -.
DR   EnsemblMetazoa; CapteT148581; CapteP148581; CapteG148581.
DR   HOGENOM; CLU_000146_1_0_1; -.
DR   OMA; DNHEPWI; -.
DR   Proteomes; UP000014760; Unassembled WGS sequence.
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; -; 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:SF447; SPECTRIN BETA CHAIN; 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:UP000014760};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          24..128
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          143..248
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          2193..2305
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          2061..2082
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2116..2214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2308..2338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          427..461
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          753..787
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          965..999
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1217..1248
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1290..1317
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1396..1423
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        2061..2077
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2165..2179
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2197..2214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2338 AA;  271043 MW;  C23DA6C240515F8A CRC64;
     MEEGNPAKLF ERSRIKALAD ERESVQKKTF TKWVNSHLSR VGCRIQDLYV DLRDGKMLIK
     LLEVLSGERL PRPTKGKMRI HCLENVDKSL SFLLEQRVHL ENMGAHDIVD GNPRLTLGLI
     WTIILRFQIQ DITIEETTSR EVKSAKDALL LWCQMKTAGY ANVNVRNFTT SWRDGLAFNA
     LIHKHRSDLI EYNQLTKANP NYNLNNAFNV AEEKLGLTRL LDAEDVSTEY PDEKSIITYV
     VTYYHYFSKM KAESVQGRRV GKVVNQCLEH DHMIADYDSL TSELLDWIEN TIEVLNDRQF
     ANSLNGVQQQ LAAFNTYRTV EKPPRFVEKG NLEVQLFTIQ SKMRANNQKP YLPAEGKMIS
     DINRAWDRLE KSEHGRELAL REELIRQEKL EQLAARFDRK AGMRETWLSE NQRLVSQDNF
     GYDLAAVEAA TKKHEAIETD INAYEERVQA VISVANELEQ ENYHDIDRIN ARKDNVLRLW
     NYLLELLRAR RMRLELSLQL QKIFQEMLYI LDWMDEIKAR LQSEDYGKHL MGVEDLLQKH
     SLLESDIHIV GERVKTVNGN AGRFHEADFP DVAGYKPCDP EVVKDRMSHL DAAYEELLAL
     AADRRARLHE SRKLWQFYWD MADEEGWIKE KEQLMASPDL GHDLTSVHLL LKKHKANEDE
     LQARHSHLND VLKVGDDLIK ADNFGKEKIQ DRTDEINSQW ANLTELSNYR RKRLAEAVDF
     YQFFTDADDV DTWMLDILRL VSSEDVGRDE ASVQSLLKKH KDTTDELQNY QSVIQALHEQ
     AASLGEQDRE SPEVQGRLGS IDRRYQELLE LAKIRKQRLL DALALYKLYN EADGVEQWIT
     EKEKLLHTML ATDDVEEVEI LKARFDTFDQ EMNANADKVE TVKQLSRQLV HNEHPNSDEV
     LSRESDVNDK WDKLRSLADG KKGSLNLAHD VNTWHIECQE TMTWIREKAK LIESTDDLGN
     DLGGVITLQR RLSGLERDLA AIQAKLDSLQ GEADRLADEK PEEAEAIQVK VTQITELWQE
     LKTMLKVRDE RLGEANELQK FLADLDHFQQ WLTRTQTTIA REDFPQDMAE AEQMLNEHKA
     IKEEMEAYES DYAKMKEFGE KTVEGQEDVQ YMFLRERLKA LDDGWEDIHK MWQNKQHLLS
     QGLNLQMFMR DAKQAEVLLS QQDNFLSKEE VPHSLEHSEN LIKQHEAFIT TLDANDEKVN
     NVLSFSQRLI DENHFAQDKI AQKAENLKDR RQQNRQRAYD QLQKLKDSLK MQQFLQDCDE
     LSDWLGEKTI AAQDETYRDA KNIHSKYMRH QAFESEIKSN KDRLDKLIQE GEALQEEKPH
     MAEVVEPKLE ELRKQWDELE NITKQKGQRL FDANRHILYE QNCDDIDGWI TTIESCIEAD
     DTGHDLTTVN LLVQKQNILE SELKIKQQQV AELESQKDHL NDVEPEKEEV IRAKKVQVEE
     RFVKMLEPLQ ERRSKLERAK RLQQFLRDLE DEKLWISEKM PQSTSTNFGN NLLGVQMLQR
     RNKSLRNEID GHEPQHTHIM DLGKELIDEG HPQAEEFQQS LDELEKAWQD LLDSVEHRRK
     MLGLSEVAQQ YLFDASESEA WMSEQELYMM AEERAKDEVG ANNMLKKHST LEKTVEDYAD
     TIRELGDRSR ALIDEAHPDS DQVAVKQSQV DKLYASLKDL AGERRGKLDE VLKLYILNRE
     IEDIEQWIAE REVVAGSHEL GQDYEHVTML RDRFKDFAQE TETIGQERVS IVNDNCDALI
     EAGHSDAATI AEWKDQINEM WADLLELIDT RMEMLAASWK LHKFFHDCKE TLERIYEKQN
     TIPDELGRDA QTVAALQRRH ASFEHDLVTL GSQVQQVQEE AATLIVAYSG DRAQDIQDKE
     AEVVNAWRNL QINVERRKIL LADSSDLFRF FGMVRDLMNW MNDMTRQMST QEKPRDVSGV
     ELLMNNHQSL KAEIDARDEN FTICVNLGKD LLARKHSRSQ EVRERLIQLG TQRGGMMEQW
     EDRWEHLRLI LEVYQFARDA SVAETWLMAH EPYVQSHDYG DTIDIIEAMI KKHEAFERSA
     MTQEERFAAL ERLTTFELRE RQKQQEEEFR REHPDAPLPQ KTSFAERYIE EFLPPPEPEP
     EPEPTPAPVV ETLAPKAESP VKAKEAETQQ AEDGRPQSAV VMRSKDAIDS PQRHVLSEPG
     SPDGGDRGKA VHRSASADRG KQRASPTAGP SGDDSFEGQL VRKHEWESTT KKASNRSWDK
     VFCVLTAKAL ASFKDQKHAK SEPKTYFHNE QPIDLDGASA AKASDYQKRP HVFRLKLGNG
     GDYLYQCKDD DEMTSWINRI NVAVGSEGGA ASGRAQTLPA PGQRDEPKRR SFFTMKKK
//
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