Q00963 (SPTCB_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Spectrin beta chain

Gene names

Name:	beta-Spec
Synonyms:	Spec-b
ORF Names:	CG5870

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	2291 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.5
Subunit structure	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.
Sequence similarities	Belongs to the spectrin family. Contains 2 CH (calponin-homology) domains. Contains 1 PH domain. Contains 17 spectrin repeats.
Sequence caution	The sequence AAR82828.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Domain	Repeat
Ligand	Actin-binding Calmodulin-binding
Molecular function	Actin capping
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	actin filament capping Inferred from electronic annotation. Source: UniProtKB-KW axon midline choice point recognition Inferred from mutant phenotype. Source: FlyBase fusome organization Traceable author statement. Source: FlyBase long-term strengthening of neuromuscular junction Inferred from mutant phenotype. Source: FlyBase maintenance of presynaptic active zone structure Inferred from direct assay. Source: FlyBase negative regulation of microtubule depolymerization Inferred from mutant phenotype. Source: FlyBase neuromuscular synaptic transmission Inferred from mutant phenotype. Source: FlyBase photoreceptor cell axon guidance Inferred from mutant phenotype. Source: FlyBase plasma membrane organization Traceable author statement. Source: FlyBase spectrosome organization Traceable author statement. Source: FlyBase
Cellular component	apicolateral plasma membrane Traceable author statement. Source: FlyBase axon Inferred from direct assay. Source: FlyBase fusome Inferred from direct assay. Source: FlyBase lateral plasma membrane Inferred from direct assay. Source: FlyBase neuromuscular junction Inferred from direct assay. Source: FlyBase spectrin Inferred from electronic annotation. Source: InterPro spectrosome Inferred from direct assay. Source: FlyBase
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW ankyrin binding Inferred from direct assay. Source: FlyBase calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW microtubule binding Inferred from direct assay. Source: FlyBase phosphatidylinositol-4,5-bisphosphate binding Inferred from direct assay. Source: FlyBase structural constituent of cytoskeleton Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2291

2291

Spectrin beta chain

PRO_0000073468

Regions

Domain

1 – 271

271

Actin-binding

Domain

50 – 154

105

CH 1

Domain

169 – 271

103

CH 2

Repeat

298 – 408

111

Spectrin 1

Repeat

418 – 522

105

Spectrin 2

Repeat

524 – 633

110

Spectrin 3

Repeat

635 – 739

105

Spectrin 4

Repeat

741 – 844

104

Spectrin 5

Repeat

846 – 950

105

Spectrin 6

Repeat

952 – 1057

106

Spectrin 7

Repeat

1059 – 1167

109

Spectrin 8

Repeat

1169 – 1273

105

Spectrin 9

Repeat

1275 – 1378

104

Spectrin 10

Repeat

1380 – 1485

106

Spectrin 11

Repeat

1487 – 1591

105

Spectrin 12

Repeat

1593 – 1697

105

Spectrin 13

Repeat

1699 – 1804

106

Spectrin 14

Repeat

1806 – 1910

105

Spectrin 15

Repeat

1912 – 2016

105

Spectrin 16

Repeat

2018 – 2078

61

Spectrin 17

Domain

2147 – 2259

113

PH

Amino acid modifications

Modified residue

2195

1

Phosphoserine Ref.6

Experimental info

Sequence conflict

2278

1

D → Y in AAA28399. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

2291

Helix Strand Turn

Details...

Beta strand

2146 – 2157

12

Beta strand

2173 – 2182

10

Beta strand

2185 – 2191

7

Helix

2192 – 2195

4

Beta strand

2219 – 2223

5

Beta strand

2226 – 2230

5

Beta strand

2232 – 2234

3

Beta strand

2236 – 2240

5

Beta strand

2242 – 2244

3

Helix

2245 – 2258

14

Sequences

	Sequence		Length	Mass (Da)
	Q00963 [UniParc]. Last modified June 1, 2001. Version 2. Checksum: 5CDFB0C548BBC39B	FASTA	2,291	265,739
	10 20 30 40 50 60 MTTDISIVRW DPSQGPGNEY IDEYEYDGGN SSSRLFERSR IKALAEERES VQKKTFTKWV 70 80 90 100 110 120 NSHLCRVNCR IADLYVDMRD GKHLIKLLEV LSGERLPKPT KGKMRIHCLE NVDKALQFLR 130 140 150 160 170 180 EQRVHLENIG SHDIVDGNAS LNLGLIWTII LRFQIQDITI EEVDNKETKS AKDALLLWCQ 190 200 210 220 230 240 MKTAGYHNVN VRNFTTSWRD GLAFNAIIHK HRPDLVQFEK LSKTNAIHNL NNAFDVAEDK 250 260 270 280 290 300 LGLAKLLDAE DVFVEHPDEK SIITYVVTYY HYFSKLKQET VQGKRIGKVV GIAMENDKMV 310 320 330 340 350 360 HDYENFTSDL LKWIETTIQS LGEREFENSL AGVQGQLAQF SNYRTIEKPP KFVEKGNLEV 370 380 390 400 410 420 LLFTLQSKMR ANNQKPYTPK EGKMISDINK AWERLEKAEH ERELALREEL IRQEKLEQLA 430 440 450 460 470 480 ARFDRKASMR ETWLSENQRL VSQDNFGFDL AAVEAAAKKH EAIETDIFAY EERVQAVVAV 490 500 510 520 530 540 CDELESERYH DVKRILLRKD NVMRLWTYLL ELLRARRMRL EISLQLQQNF QEMLYILDNM 550 560 570 580 590 600 EEIKQLLMTD DYGKHLMGVE DLLQKHSLVE ADINILGERV KVVVQNSQKF LSDDPESYKP 610 620 630 640 650 660 CDPEIIVSRV QQLEDAYAEL VRLAVERRSR LEESRKLWQF YWDTADEENW IKEKEQIVST 670 680 690 700 710 720 DEVGHDLTTV NLMLSKHKAL ESEITSHDPQ LQNVAKVGSE LITEGHFGAD RIKDRLKEIL 730 740 750 760 770 780 NKWDHLLDLT KYRRQRLENA VEYFQLFADA DDVDNWMLDT LRIVSSEDVG RDEANVQSLL 790 800 810 820 830 840 KKHKDVADEL KNYAEVIDAL HKQAESLKLN EAEKANVDKR LEAIDNRYKE LTELAKLRKQ 850 860 870 880 890 900 RLLDALSLYK LMSEADGVEQ WIKEKTKMLD TMTPGKDIED VEIMKHRFEG FDKEMNANAS 910 920 930 940 950 960 RVAVVNQLAR QLLHVEHPNS DEILERQNHL NQEWSTLREK AEAKMDDLKS AHGVQTFYIE 970 980 990 1000 1010 1020 CRETISWIED KKRILTETDS LEMDLTGVMT LQRRLSGMDR DLAAIQAKLS SLEREANSIE 1030 1040 1050 1060 1070 1080 DEHPEEAKII RERIAQIELI WEQLTQMLKE RDSKLEEAGD LHRFLRDLDH FQTWLTKTQT 1090 1100 1110 1120 1130 1140 DVASEDTPTS LPEAEKLLNQ HQSIREEIDN YTEDYKNMME YGERLTSEGS TSDDPQYMFL 1150 1160 1170 1180 1190 1200 RERLNALKDG WEELHQMWEN RQVLLSQSLD QQLFNRDARQ TEVLLSQQEH FLSKDDTPVN 1210 1220 1230 1240 1250 1260 LEQAENQLKR HEAFLTTMEA NDDKINTLLQ VADTLVEKDH FDADKIGKRA ENITGRRDDN 1270 1280 1290 1300 1310 1320 RQRALDQHEK LKNQVKLHEF LQDLEELAEW VQEKYATSQD ESYRSAKTIH SKWTRHQAFE 1330 1340 1350 1360 1370 1380 AEIAANKERL FEAEKSAQEL SKEKPEFKDV IEPKLKELAK QFDDLEVHTK EKGAMLFDAN 1390 1400 1410 1420 1430 1440 REVLVQQTCD DIDSYITDLE KQIVSGDTAN DLTSVNILMQ KQQVIQTQMA VKARQVEEID 1450 1460 1470 1480 1490 1500 KQTEYLQKTV PEEKIEPIVV KKTAVLERFE KIKAPLLERQ KALEKKKEAF QFCRDVEDEK 1510 1520 1530 1540 1550 1560 LWIDEKLPVA NSPDYGNSLF NVHVLKKKNQ SLATEIDNHE PRINAICNNG RKLIDEGHED 1570 1580 1590 1600 1610 1620 AKKFEALISD LTQKWQELKD AIENRRKHLL ESEKVQQYFF DAQEAESWMS EQELYMMVED 1630 1640 1650 1660 1670 1680 RGKDEISAQN LMKKHENLEQ SVEDYANTIR QLGEVARQFS GDDISSGDAV AVKQSQLDKL 1690 1700 1710 1720 1730 1740 YAGLKDLAGE RRARLNEALQ LFMLSREVDD LEQWITDREV VAGSQELGQD FDHVTLLSER 1750 1760 1770 1780 1790 1800 FNEFARDTEA VGGERVAKVN GIADNLIQAG HSDSATIAEW KDNLNESWQD LLELIETRTQ 1810 1820 1830 1840 1850 1860 MLAASRELHK FFHDCKDVLG RILEKQHGVS DELGRDAGSV STLQRKHYNF LQDLITLYSQ 1870 1880 1890 1900 1910 1920 VQQIQEESAK LQDAYAGDKA KEITNREQEV LHAWDNLQAM CDARKQKLAD TGDLFRFFNM 1930 1940 1950 1960 1970 1980 VRILMIWMED LVRQMNTSEK PRDVSGVELL MNNHQSLKAE IDTREDNFGA CISLGKELLT 1990 2000 2010 2020 2030 2040 RNHYASADIK DRLMTLSNSR NALLRRWEER WENLQLILEV YQFARDAAVA EAWLIAQEPY 2050 2060 2070 2080 2090 2100 LLSSELGHTI DEVENLIKKH EAFEKSAAAQ EERFSALERL TTFELKEMKR RQELAEEAER 2110 2120 2130 2140 2150 2160 QRIKEEQEAK AASEAAEQAK REAERRDDVD VGASHDDSER GGTPGAGEGH EGYVTRKHEW 2170 2180 2190 2200 2210 2220 DSTTKKASNR SWDKVYMAAK AGRISFYKDQ KGYKSNPELT FRGEPSYDLQ NAAIEIASDY 2230 2240 2250 2260 2270 2280 TKKKHVLRVK LANGALFLLQ AHDDTEMSQW VTSLKAQSDS TAVAASRSQT LPATSQKDEP 2290 KRRSFFTLKK K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete sequence of Drosophila beta-spectrin reveals supra-motifs comprising eight 106-residue segments." Byers T.J., Brandin E., Lue R., Winograd E., Branton D. Proc. Natl. Acad. Sci. U.S.A. 89:6187-6191(1992) [PubMed: 1631106] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The genome sequence of Drosophila melanogaster." 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. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." 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. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1404. Strain: Berkeley. Tissue: Testis.
[5]	"Drosophilia spectrin. I. Characterization of the purified protein." Dubreuil R., Byers T.J., Branton D., Goldstein L.S.B., Kiehart D.P. J. Cell Biol. 105:2095-2102(1987) [PubMed: 3680372] [Abstract] Cited for: FUNCTION.
[6]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2195, MASS SPECTROMETRY. Tissue: Embryo.
[7]	"Solution structure of the pleckstrin homology domain of Drosophila beta-spectrin." Zhang P., Talluri S., Deng H., Branton D., Wagner G. Structure 3:1185-1195(1995) [PubMed: 8591029] [Abstract] Cited for: STRUCTURE BY NMR OF 2145-2262.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M92288 mRNA. Translation: AAA28399.1.
AE014298 Genomic DNA. Translation: AAF48751.1.
BT011160 mRNA. Translation: AAR82828.1. Sequence problems.

PIR

A46147.

RefSeq

NP_523388.1. NM_078664.2.

UniGene

Dm.7022.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DRO	NMR	-	A	2145-2262	[»]

ProteinModelPortal

Q00963.

SMR

Q00963. Positions 45-278, 293-1273, 1278-2087, 2141-2262.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-18565N.

IntAct

Q00963. 3 interactions.

MINT

MINT-922069.

STRING

Q00963.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0074454; FBpp0074228; FBgn0250788.

GeneID

32746.

KEGG

dme:Dmel_CG5870.

NMPDR

fig|7227.3.peg.18368.

Organism-specific databases

CTD

32746.

FlyBase

FBgn0250788. beta-Spec.

Phylogenomic databases

eggNOG

inNOG04429.

GeneTree

EMGT00050000000686.

InParanoid

Q00963.

OMA

KEGEDMI.

OrthoDB

EOG4JM64F.

PhylomeDB

Q00963.

Gene expression databases

Bgee

Q00963.

GermOnline

CG5870. Drosophila melanogaster.

Family and domain databases

InterPro

IPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR001605. PH_dom-spectrin-type.
IPR011993. PH_type.
IPR001849. Pleckstrin_homology.
IPR018159. Spectrin/alpha-actinin.
IPR016343. Spectrin_bsu.
IPR002017. Spectrin_repeat.
[Graphical view]

Gene3D

G3DSA:1.10.418.10. Calponin-homology. 2 hits.
G3DSA:2.30.29.30. PH_type. 1 hit.

KO

K06115.

Pfam

PF00307. CH. 2 hits.
PF00169. PH. 1 hit.
PF00435. Spectrin. 17 hits.
[Graphical view]

PIRSF

PIRSF002297. Spectrin_beta_subunit. 1 hit.

PRINTS

PR00683. SPECTRINPH.

SMART

SM00033. CH. 2 hits.
SM00233. PH. 1 hit.
SM00150. SPEC. 17 hits.
[Graphical view]

SUPFAM

SSF47576. Calponin-homology. 1 hit.

PROSITE

PS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

780161.

Entry information

Entry name

SPTCB_DROME

Accession

Primary (citable) accession number: Q00963
Secondary accession number(s): Q6NNX2, Q9VX30

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	June 1, 2001
Last modified:	January 25, 2012
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project