ID A0A0V1D8Z9_TRIBR Unreviewed; 2365 AA.
AC A0A0V1D8Z9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 03-MAY-2023, entry version 30.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN Name=beta-Spec {ECO:0000313|EMBL:KRY58049.1};
GN ORFNames=T03_9385 {ECO:0000313|EMBL:KRY58049.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY58049.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY58049.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY58049.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the spectrin family.
CC {ECO:0000256|ARBA:ARBA00006826, ECO:0000256|PIRNR:PIRNR002297}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY58049.1}.
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DR EMBL; JYDI01000024; KRY58049.1; -; Genomic_DNA.
DR Proteomes; UP000054653; 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; 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; 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; PF00169; PH; 1.
DR Pfam; PF00435; Spectrin; 17.
DR PIRSF; PIRSF002297; Spectrin_beta_subunit; 2.
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|PIRNR:PIRNR002297};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 59..163
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 217..322
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 2218..2328
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 2138..2194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1039..1080
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1364..1423
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1608..1642
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2149..2164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2177..2192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2365 AA; 275634 MW; 1411C5382FF45BBE CRC64;
MTTDIAIRPD YVDEHIFEDY DENSSARLFE RSRIKALAED LDLYTMDKIV KILKDERENV
QKKTFTKWVN SHLERAQCRI QDLYTDLRDG KMLIKLLEIL SGERLPKPTK GKMRIHCLEN
VDKALQFLRL QHVHLENMGS HDIVDGNPRL SLGLIWTIIL RFQTVSSAIL VRISLSVVLL
NLGESVVSVC DNCDRFFMAC VQIQGIELFD TESQETRSAR EALLLWCQMK TAGYPNVNVR
NFTTSWRDGL AFNALIHKHR PDLISFEKLQ RSNALHNLKN AFEVAENQLG ITSLLDAEDV
NVEMPDEKSI ITYLVSYYHY FNKLRQETIQ GRRIGKVVSE LMENDVMIEE YERLSSDLLQ
WIKKTIEKLN DRVFVNSLVG VQKQLTTFNN YRTEEKPPKF VSKGNLEVLL FTLQSRMRAN
NQKPYLPREG RMISDINKAW ENLEKAEHER ELALKEELIR QEKLEQLAAR FDRKAGMRET
WLAENQRLVS QDNFGSDLPS VEAATKKHEA IETDIYAYEE RVQAVVAVAQ DLEAENYNDI
DRINARKDNV LQLWNFLLEL LMARRVRLEL SMVIQKIFQD MIHVLGWMEE LKARMLSDDY
GKHLMGVEDL IQKHQLVEAD VNIVGDRLKL VCQQAEKFTH PDGPDGSGYQ PVEPALVQER
IQMLEAAYKE LLAMVEQRRQ RLEDSKRLCQ FFLDAEELEQ GFKELEQVLS SPDVGHDVVS
VNLLLAKHKS VEDQIASLQR NKNAVIDIGR GLIGENLPGS SDIQAQIDHI EEMWQALQTL
ANLRKQRLVG AVDYYQLFSD IDDNEAWLLD SLRILSSEDV GKDEPSVQHL IKQHDGVTEE
LQNGRNSLDQ LYAQAEQLPE AARAGPDVAD RLGQIEKRYA EVMELGSMRK QRLLDALTLY
KLFNDTDNLE AWIDEKAKLL ESLKPADDLE EVEIMRHRFE TLEQDLNNQS AKVLTVNKLS
RQLLHVEHPN SDAILQRQNR LNARWAQLQD MVRRKRLELD QAHRLQTFRI DCQETVTWIQ
DKTRVLEDTE ELKDDLSGIM KLQRRLSMME RDLGAIQAKL DNLEQQAVRL QQERPEEVEA
IRENIARIQY VWDRLTGKVR EYEAKLDEAG DLQRFLRDLD HFQGWLSSVM RQVASEDEPQ
SLAEAEQLLS QHSVIREEID GYAEDYAKMR MMGDRVTQDQ TDPQYLLLRQ RLDGLQEGWQ
ELHRMWDNRQ AMLSQALNLQ MFLRDAKQAE LLLNQQENYL AKDEAPTSLE QAETMLKRHG
DFLTTMEAGD EKIRAVVVFG NQLCEDGHFA ADRIHKKVSN VHERRELNRE KANSMTERLR
EHVALQQFLS DCEELRRWIE EKMIRAQDET YRDAKTVHSK FMRHQAFEAE IQSNKERLQR
LQEACVRLIA EKPQLDSFVD PHVAELTAQF DELESKTKEK GQRLFDANRE AIYVQACEDM
TEWVEAMEKQ MGTEDVAQDL ATVNVEIQKQ QLIESEMLKR VQQVCQLQAM EPQLEELRPE
EFDAIKTHRL TVQEKFSKLQ APLEQRRQLL ERKKEAFQFL RDVEDEKLWI ADRRPMARSP
MLGDTLFDCH RLQKQNQSLK NEIENHQPWI QRICDNGRKL IASGHENAPE FEAKIKELLE
ALEELKKDVE KRRERLAESE KAHQYIYDAN EAEVWMSEQE LYMMTDDRGR DEFTTENLIK
KHERQRQDVE QFADTIRDLA DRAQKLIAEH APMSDTIAIR QAQIDKSYAG LQDLSRERRH
RLGETLQLFN LHRQIEDILQ WIAEREVVAA SQDAGQDYEH VQMLQERFRQ FAKDTETIGT
ERVSNANEEC DQLMAVHHPD APTVALWKDN LNEAWENLLE LMQTRAQMLD ASCQLHKFFH
DCRDTLSRIL EKSHSMPEDL GRDASSVSAL QRKHQNFLTD LLSLESQVKQ VQADARSLQA
SYAGDRALEI QAREGEVLNA WRLLQANCEG RRTKLLDTSD LFRFMQMVRD LLLWMEEVKR
EMNTQERPKD VSGVELLMNN HQSLKAEIDA REENFSSCIA LGRDLLARKH YASSEIEKKL
IKLTTERAEM MRRWEDRWEY LQLILEVYQF ARDAAVADAW LLAQEPYLLS KEYGRTLEEV
VKLIKKHEAF EKSTIAQEER FQALEKLTTF ELKELQRRQD EQERLRRTGS PRTSTPTRSP
EKLETTFPAE SGGRTETTLG VDEERRRQLH SSESPGWRIS LSRSKYFDAN DSVGTESAEG
FEGHLIRKHT WETLDRKASI RSWDKLYCVI RGSQLEFYKD HKHREDGELY RGETPISLVG
WNVEIASSYT KRRNVLSLRS PAGFEYLLQA RDEDDMLRWL HQLRTAVGIL ETSTSSSGKA
STLPAAQQPS AKKRFFGTLK KKQAL
//
