ID T1HWC3_RHOPR Unreviewed; 2297 AA.
AC T1HWC3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
OS Rhodnius prolixus (Triatomid bug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX NCBI_TaxID=13249 {ECO:0000313|EnsemblMetazoa:RPRC008343-PA, ECO:0000313|Proteomes:UP000015103};
RN [1] {ECO:0000313|Proteomes:UP000015103}
RP NUCLEOTIDE SEQUENCE.
RA Wilson R.K., Warren W., Dotson E., Oliveira P.L.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:RPRC008343-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-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; ACPB03018627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 13249.T1HWC3; -.
DR EnsemblMetazoa; RPRC008343-RA; RPRC008343-PA; RPRC008343.
DR VEuPathDB; VectorBase:RPRC008343; -.
DR eggNOG; KOG0517; Eukaryota.
DR HOGENOM; CLU_000146_1_2_1; -.
DR InParanoid; T1HWC3; -.
DR OMA; DNHEPWI; -.
DR OrthoDB; 2872403at2759; -.
DR Proteomes; UP000015103; 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; 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; 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}; Cytoplasm {ECO:0000256|PIRNR:PIRNR002297};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW ECO:0000256|PIRNR:PIRNR002297};
KW Reference proteome {ECO:0000313|Proteomes:UP000015103};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
SQ SEQUENCE 2297 AA; 265708 MW; 3E1698843389B28F CRC64;
MTTDISVVRW DPSLQQEIVD DYEYDGGNSS SRLFERSRIK ALADERENVQ KKTFQKWVNS
HLVRVNCRIS DLYVDLRDGK MLIQLLEVLS GERLPRPTKG KMRIHCLENV DKALQFLRDQ
RVHLENMGSH DIVDGNARLS LGLIWTIILR FQILDIRIEE TDNKETKSAK DALLLWCQMK
TAGYHNVNVR NFTTSWRDGL AFNAIIHKHR PDLVQFEKLS KSNAMYNLNN AFTVAEDKLG
LTKLLDPEDV FVEQPDEKSI ITYVVTYYHY FSKMKQETVQ GKRIGKVVGI AMDNDRMVQE
YERLTSDLLK WIESTIQQLG DRRFANSLVG VQQQLAQFNN YRTVEKPPKF VEKGNLEVLL
FTLQSKMRAN NQKPYTPREG KMISDINKAW ERLEKAEHEK ELALREELIR QEKLEQLAAR
FNRKASMRET WLSENQRLVS QDNFGFDLAA VEAAAKKHEA IETDIFAYEE RVQAVVTVSQ
ELEAENYHDI DRINARKDNV LRLWNYLLEL LRSRRMRLEL SLQLQQNFQE MIYILDSMEE
LKMRLLSDDY GKHLMGVEDL LQKHSLVEAD INVLGERVKV VVQQSQKFND DETTEGYRPC
DSAIIVERVQ QLEHAYHELV KLAVERRARL EESRKLWQFY WDMADEENWI KEKEQIVSQG
DIGHDLITIN LLLSKHKALE NEISSHEPQL VSVVSVGEDL VKQGHFGAER IQSRLNDTLD
SWKHLQELVA FRRKRLEEAV DFHQFFADAD DVDIWMLDAL RLVSSEDVGR DEANVQSLLK
KHKEATDELK NYSSAIEALH SQADALGEET RNSPEVSQRL NSIDSRYKEL LELAKLRKQR
LLDALSLYKL FSEADGVEQW IGEKDRMLET MSPGKDIEDV EIMKHRYNGF DKEMNSNASR
VAVVNQLARQ LLHVEHPNSE QIVARQNKLN HEWAELREKA ETKREELSAA HGVQTFHIEC
RETVSWIEDK KRILQSTDSL EMDLTGIMTL QRRLSGMERD LAAIQAKLDS LQAESEAIAA
THPEEAELIK QRISQITIIW QELTMMLKER DAKLEEAGDL HRFLRDLDHF QSWLQKTQTD
VASEDIPGSL ADAEKLLSQH QAIKEEIDNY TQDYAKMMEY GEKITAEPST QSDPQYMFLR
ERLKALRDGW TELHQMWENR QQLLSHWLNL QMFHRDARQA EVLLSHQEHV LAKDDTPINL
EQAENLIKRH EAFLTTMEAN DEKINAVVQF AGQLSDDGHF ASDKVVKKAH NIDERRKNNR
EKAQQQMEKL KDQLELHQFL QDCDELSEWI QEKKFISQDE SYRSAKTVHS KWTRHQAFEA
EIASNKDRLI RVQEVITLIS CLGEKSSEVI GPKVTDLVEQ FNDLETMTKD KGERLFDANR
EVLIHQTCDD IDSWMNDLEK QIESADVGSD LASVNILMQK QQMIETQMAV KARQVTELET
QANYLERTVP EKMGEIKQKK VAVEERFQKL KEPLLHRQRQ LEKNKEADVE DEKLWIAEKM
PLATSTDFGN SLFNVHTLKK KNQSLSTEID NHEPRLHAVL RNGEKLVEEG HEEAPQFRKL
MDELLDRWQH LKDAVANRKH QLLHSEKAQQ YLFDANEAES WMSEQELYMM VEDRGKDEIS
AQNLMKKHEC LEHAVDDYAN TIRQLGETAR ALAAENNPLS DQIGVKQSQV DKLYAGLKDL
AGERRAKLDE ALQLFMLNRE VDDLEQWIAE REVVAGSHEL GQDYDHVTLL WERFKEFARD
TEATGAERVQ AVNGIADGLI AQGHSDSATI AEWKDGLIEA WQDLLELIST RTQMLEASRE
LHKFFHDCKD VLGRIYEKQH AMSDELGRDA GSVSTLQRKH QNFIQDLQTL QSQVQAISDE
SSKLQASYAG DKAKEITNRE SEVVSAWAAL QAMCDARRAK LADTGDLFKF FNMVRTLILW
MDDVIRQMNT TEKPRDVSGV ELLMNNHQSL KAEIDTREDN FTSCITLGKE LLSRNHYASN
EIKEKLLSLN NQRNSLLHRW EERWENLQLI LEVYQFARDA AVAEAWLIAQ EPYLMSTELG
HTIDEVENLI KKHESFEKSA TAQEERFSAL ERLTTFELKE LKRREEEEEE RKRQEELAKK
QATPPSSPQQ VATGSHRQDS RSPGEGSSSA PRKKRSRSKS PFRSFRWKKS SSSSTGSRPG
AVSDDEENLA AAAGNTVFIQ LPSPSGTESH IEGILVRKHV WEALKKASNR SWHEMYVVAR
GHQLLAYKDA KAAKSSPETY YKGESPIDLR GATVDVATDY TKKKHVFKIK LSNGSEYLMQ
AKDDDDMRNW VSALNSA
//