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Spectrin beta chain

 SPTCB_DROME             Reviewed;        2291 AA.
Q00963; Q6NNX2; Q9VX30;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 2.
05-DEC-2018, entry version 185.
RecName: Full=Spectrin beta chain;
Name=beta-Spec; Synonyms=Spec-b; ORFNames=CG5870;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1631106; DOI=10.1073/pnas.89.13.6187;
Byers T.J., Brandin E., Lue R., Winograd E., Branton D.;
"The complete sequence of Drosophila beta-spectrin reveals supra-
motifs comprising eight 106-residue segments.";
Proc. Natl. Acad. Sci. U.S.A. 89:6187-6191(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1404.
STRAIN=Berkeley; TISSUE=Testis;
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W.,
Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
Celniker S.E.;
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION.
PubMed=3680372; DOI=10.1083/jcb.105.5.2095;
Dubreuil R., Byers T.J., Branton D., Goldstein L.S.B., Kiehart D.P.;
"Drosophilia spectrin. I. Characterization of the purified protein.";
J. Cell Biol. 105:2095-2102(1987).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2195, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[7]
STRUCTURE BY NMR OF 2145-2262.
PubMed=8591029; DOI=10.1016/S0969-2126(01)00254-4;
Zhang P., Talluri S., Deng H., Branton D., Wagner G.;
"Solution structure of the pleckstrin homology domain of Drosophila
beta-spectrin.";
Structure 3:1185-1195(1995).
-!- FUNCTION: Spectrin is the major constituent of the cytoskeletal
network underlying the erythrocyte plasma membrane. It associates
with band 4.1 and actin to form the cytoskeletal superstructure of
the erythrocyte plasma membrane. Interacts with calmodulin in a
calcium-dependent manner. {ECO:0000269|PubMed:3680372}.
-!- SUBUNIT: Native spectrin molecule is a tetramer composed of two
antiparallel heterodimers joined head to head so that each end of
the native molecule includes the C-terminus of the alpha subunit
and the N-terminus of the beta subunit.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell
cortex.
-!- SIMILARITY: Belongs to the spectrin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAR82828.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M92288; AAA28399.1; -; mRNA.
EMBL; AE014298; AAF48751.1; -; Genomic_DNA.
EMBL; BT011160; AAR82828.1; ALT_SEQ; mRNA.
PIR; A46147; A46147.
RefSeq; NP_523388.1; NM_078664.3.
UniGene; Dm.7022; -.
PDB; 1DRO; NMR; -; A=2142-2262.
PDBsum; 1DRO; -.
ProteinModelPortal; Q00963; -.
SMR; Q00963; -.
BioGrid; 59071; 16.
DIP; DIP-18565N; -.
IntAct; Q00963; 3.
STRING; 7227.FBpp0074228; -.
iPTMnet; Q00963; -.
PaxDb; Q00963; -.
PRIDE; Q00963; -.
EnsemblMetazoa; FBtr0074454; FBpp0074228; FBgn0250788.
GeneID; 32746; -.
KEGG; dme:Dmel_CG5870; -.
CTD; 32746; -.
FlyBase; FBgn0250788; beta-Spec.
eggNOG; KOG0035; Eukaryota.
eggNOG; COG5069; LUCA.
GeneTree; ENSGT00940000154864; -.
InParanoid; Q00963; -.
KO; K06115; -.
OrthoDB; EOG091G003V; -.
PhylomeDB; Q00963; -.
Reactome; R-DME-375165; NCAM signaling for neurite out-growth.
Reactome; R-DME-5673001; RAF/MAP kinase cascade.
Reactome; R-DME-6807878; COPI-mediated anterograde transport.
ChiTaRS; beta-Spec; fly.
EvolutionaryTrace; Q00963; -.
GenomeRNAi; 32746; -.
PRO; PR:Q00963; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0250788; Expressed in 38 organ(s), highest expression level in embryo.
ExpressionAtlas; Q00963; baseline and differential.
Genevisible; Q00963; DM.
GO; GO:0016327; C:apicolateral plasma membrane; TAS:FlyBase.
GO; GO:0030424; C:axon; IDA:FlyBase.
GO; GO:0045169; C:fusome; IDA:FlyBase.
GO; GO:0016328; C:lateral plasma membrane; IDA:FlyBase.
GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
GO; GO:0008091; C:spectrin; ISS:FlyBase.
GO; GO:0045170; C:spectrosome; IDA:FlyBase.
GO; GO:0003779; F:actin binding; ISS:FlyBase.
GO; GO:0030506; F:ankyrin binding; IDA:FlyBase.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0008092; F:cytoskeletal protein binding; ISS:FlyBase.
GO; GO:0008017; F:microtubule binding; IDA:FlyBase.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:FlyBase.
GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
GO; GO:0007411; P:axon guidance; IMP:FlyBase.
GO; GO:0016199; P:axon midline choice point recognition; IMP:FlyBase.
GO; GO:0007409; P:axonogenesis; IMP:FlyBase.
GO; GO:0042062; P:long-term strengthening of neuromuscular junction; IMP:FlyBase.
GO; GO:0048790; P:maintenance of presynaptic active zone structure; IDA:FlyBase.
GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:FlyBase.
GO; GO:0007399; P:nervous system development; IMP:FlyBase.
GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:FlyBase.
GO; GO:0072499; P:photoreceptor cell axon guidance; IMP:FlyBase.
GO; GO:0007009; P:plasma membrane organization; TAS:FlyBase.
GO; GO:0050807; P:regulation of synapse organization; IMP:FlyBase.
CDD; cd00014; CH; 2.
Gene3D; 1.10.418.10; -; 2.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR001589; Actinin_actin-bd_CS.
InterPro; IPR001715; CH-domain.
InterPro; IPR036872; CH_dom_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001605; PH_dom-spectrin-type.
InterPro; IPR001849; PH_domain.
InterPro; IPR018159; Spectrin/alpha-actinin.
InterPro; IPR016343; Spectrin_bsu.
InterPro; IPR002017; Spectrin_repeat.
Pfam; PF00307; CH; 2.
Pfam; PF00435; Spectrin; 17.
PIRSF; PIRSF002297; Spectrin_beta_subunit; 1.
PRINTS; PR00683; SPECTRINPH.
SMART; SM00033; CH; 2.
SMART; SM00233; PH; 1.
SMART; SM00150; SPEC; 17.
SUPFAM; SSF47576; SSF47576; 1.
PROSITE; PS00019; ACTININ_1; 1.
PROSITE; PS00020; ACTININ_2; 1.
PROSITE; PS50021; CH; 2.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; Actin capping; Actin-binding; Calmodulin-binding;
Complete proteome; Cytoplasm; Cytoskeleton; Phosphoprotein;
Reference proteome; Repeat.
CHAIN 1 2291 Spectrin beta chain.
/FTId=PRO_0000073468.
DOMAIN 50 154 Calponin-homology (CH) 1.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 169 274 Calponin-homology (CH) 2.
{ECO:0000255|PROSITE-ProRule:PRU00044}.
REPEAT 300 408 Spectrin 1. {ECO:0000255}.
REPEAT 420 521 Spectrin 2. {ECO:0000255}.
REPEAT 525 633 Spectrin 3. {ECO:0000255}.
REPEAT 636 739 Spectrin 4. {ECO:0000255}.
REPEAT 743 843 Spectrin 5. {ECO:0000255}.
REPEAT 848 948 Spectrin 6. {ECO:0000255}.
REPEAT 954 1057 Spectrin 7. {ECO:0000255}.
REPEAT 1060 1166 Spectrin 8. {ECO:0000255}.
REPEAT 1170 1272 Spectrin 9. {ECO:0000255}.
REPEAT 1276 1376 Spectrin 10. {ECO:0000255}.
REPEAT 1386 1484 Spectrin 11. {ECO:0000255}.
REPEAT 1488 1591 Spectrin 12. {ECO:0000255}.
REPEAT 1594 1697 Spectrin 13. {ECO:0000255}.
REPEAT 1701 1802 Spectrin 14. {ECO:0000255}.
REPEAT 1807 1909 Spectrin 15. {ECO:0000255}.
REPEAT 1913 2015 Spectrin 16. {ECO:0000255}.
REPEAT 2020 2089 Spectrin 17. {ECO:0000255}.
DOMAIN 2147 2259 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
REGION 1 271 Actin-binding.
MOD_RES 2195 2195 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
CONFLICT 2278 2278 D -> Y (in Ref. 1; AAA28399).
{ECO:0000305}.
STRAND 2146 2157 {ECO:0000244|PDB:1DRO}.
STRAND 2173 2182 {ECO:0000244|PDB:1DRO}.
STRAND 2185 2191 {ECO:0000244|PDB:1DRO}.
HELIX 2192 2195 {ECO:0000244|PDB:1DRO}.
STRAND 2219 2223 {ECO:0000244|PDB:1DRO}.
STRAND 2226 2230 {ECO:0000244|PDB:1DRO}.
STRAND 2232 2234 {ECO:0000244|PDB:1DRO}.
STRAND 2236 2240 {ECO:0000244|PDB:1DRO}.
STRAND 2242 2244 {ECO:0000244|PDB:1DRO}.
HELIX 2245 2258 {ECO:0000244|PDB:1DRO}.
SEQUENCE 2291 AA; 265739 MW; 5CDFB0C548BBC39B CRC64;
MTTDISIVRW DPSQGPGNEY IDEYEYDGGN SSSRLFERSR IKALAEERES VQKKTFTKWV
NSHLCRVNCR IADLYVDMRD GKHLIKLLEV LSGERLPKPT KGKMRIHCLE NVDKALQFLR
EQRVHLENIG SHDIVDGNAS LNLGLIWTII LRFQIQDITI EEVDNKETKS AKDALLLWCQ
MKTAGYHNVN VRNFTTSWRD GLAFNAIIHK HRPDLVQFEK LSKTNAIHNL NNAFDVAEDK
LGLAKLLDAE DVFVEHPDEK SIITYVVTYY HYFSKLKQET VQGKRIGKVV GIAMENDKMV
HDYENFTSDL LKWIETTIQS LGEREFENSL AGVQGQLAQF SNYRTIEKPP KFVEKGNLEV
LLFTLQSKMR ANNQKPYTPK EGKMISDINK AWERLEKAEH ERELALREEL IRQEKLEQLA
ARFDRKASMR ETWLSENQRL VSQDNFGFDL AAVEAAAKKH EAIETDIFAY EERVQAVVAV
CDELESERYH DVKRILLRKD NVMRLWTYLL ELLRARRMRL EISLQLQQNF QEMLYILDNM
EEIKQLLMTD DYGKHLMGVE DLLQKHSLVE ADINILGERV KVVVQNSQKF LSDDPESYKP
CDPEIIVSRV QQLEDAYAEL VRLAVERRSR LEESRKLWQF YWDTADEENW IKEKEQIVST
DEVGHDLTTV NLMLSKHKAL ESEITSHDPQ LQNVAKVGSE LITEGHFGAD RIKDRLKEIL
NKWDHLLDLT KYRRQRLENA VEYFQLFADA DDVDNWMLDT LRIVSSEDVG RDEANVQSLL
KKHKDVADEL KNYAEVIDAL HKQAESLKLN EAEKANVDKR LEAIDNRYKE LTELAKLRKQ
RLLDALSLYK LMSEADGVEQ WIKEKTKMLD TMTPGKDIED VEIMKHRFEG FDKEMNANAS
RVAVVNQLAR QLLHVEHPNS DEILERQNHL NQEWSTLREK AEAKMDDLKS AHGVQTFYIE
CRETISWIED KKRILTETDS LEMDLTGVMT LQRRLSGMDR DLAAIQAKLS SLEREANSIE
DEHPEEAKII RERIAQIELI WEQLTQMLKE RDSKLEEAGD LHRFLRDLDH FQTWLTKTQT
DVASEDTPTS LPEAEKLLNQ HQSIREEIDN YTEDYKNMME YGERLTSEGS TSDDPQYMFL
RERLNALKDG WEELHQMWEN RQVLLSQSLD QQLFNRDARQ TEVLLSQQEH FLSKDDTPVN
LEQAENQLKR HEAFLTTMEA NDDKINTLLQ VADTLVEKDH FDADKIGKRA ENITGRRDDN
RQRALDQHEK LKNQVKLHEF LQDLEELAEW VQEKYATSQD ESYRSAKTIH SKWTRHQAFE
AEIAANKERL FEAEKSAQEL SKEKPEFKDV IEPKLKELAK QFDDLEVHTK EKGAMLFDAN
REVLVQQTCD DIDSYITDLE KQIVSGDTAN DLTSVNILMQ KQQVIQTQMA VKARQVEEID
KQTEYLQKTV PEEKIEPIVV KKTAVLERFE KIKAPLLERQ KALEKKKEAF QFCRDVEDEK
LWIDEKLPVA NSPDYGNSLF NVHVLKKKNQ SLATEIDNHE PRINAICNNG RKLIDEGHED
AKKFEALISD LTQKWQELKD AIENRRKHLL ESEKVQQYFF DAQEAESWMS EQELYMMVED
RGKDEISAQN LMKKHENLEQ SVEDYANTIR QLGEVARQFS GDDISSGDAV AVKQSQLDKL
YAGLKDLAGE RRARLNEALQ LFMLSREVDD LEQWITDREV VAGSQELGQD FDHVTLLSER
FNEFARDTEA VGGERVAKVN GIADNLIQAG HSDSATIAEW KDNLNESWQD LLELIETRTQ
MLAASRELHK FFHDCKDVLG RILEKQHGVS DELGRDAGSV STLQRKHYNF LQDLITLYSQ
VQQIQEESAK LQDAYAGDKA KEITNREQEV LHAWDNLQAM CDARKQKLAD TGDLFRFFNM
VRILMIWMED LVRQMNTSEK PRDVSGVELL MNNHQSLKAE IDTREDNFGA CISLGKELLT
RNHYASADIK DRLMTLSNSR NALLRRWEER WENLQLILEV YQFARDAAVA EAWLIAQEPY
LLSSELGHTI DEVENLIKKH EAFEKSAAAQ EERFSALERL TTFELKEMKR RQELAEEAER
QRIKEEQEAK AASEAAEQAK REAERRDDVD VGASHDDSER GGTPGAGEGH EGYVTRKHEW
DSTTKKASNR SWDKVYMAAK AGRISFYKDQ KGYKSNPELT FRGEPSYDLQ NAAIEIASDY
TKKKHVLRVK LANGALFLLQ AHDDTEMSQW VTSLKAQSDS TAVAASRSQT LPATSQKDEP
KRRSFFTLKK K


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