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Protein

Spectrin beta chain

Gene

beta-Spec

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  • actin binding Source: FlyBase
  • ankyrin binding Source: FlyBase
  • cytoskeletal protein binding Source: FlyBase
  • microtubule binding Source: FlyBase
  • phosphatidylinositol-4,5-bisphosphate binding Source: FlyBase
  • structural constituent of cytoskeleton Source: InterPro

GO - Biological processi

  • actin filament capping Source: UniProtKB-KW
  • axon guidance Source: FlyBase
  • axon midline choice point recognition Source: FlyBase
  • axonogenesis Source: FlyBase
  • fusome organization Source: FlyBase
  • long-term strengthening of neuromuscular junction Source: FlyBase
  • maintenance of presynaptic active zone structure Source: FlyBase
  • negative regulation of microtubule depolymerization Source: FlyBase
  • nervous system development Source: FlyBase
  • neuromuscular synaptic transmission Source: FlyBase
  • photoreceptor cell axon guidance Source: FlyBase
  • plasma membrane organization Source: FlyBase
  • regulation of synapse organization Source: FlyBase
  • spectrosome organization Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding, Calmodulin-binding

Enzyme and pathway databases

ReactomeiR-DME-375165. NCAM signaling for neurite out-growth.
R-DME-5673001. RAF/MAP kinase cascade.
R-DME-6807878. COPI-mediated anterograde transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Spectrin beta chain
Gene namesi
Name:beta-Spec
Synonyms:Spec-b
ORF Names:CG5870
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0250788. beta-Spec.

Subcellular locationi

GO - Cellular componenti

  • apicolateral plasma membrane Source: FlyBase
  • axon Source: FlyBase
  • fusome Source: FlyBase
  • lateral plasma membrane Source: FlyBase
  • lipid particle Source: FlyBase
  • neuromuscular junction Source: FlyBase
  • plasma membrane Source: FlyBase
  • spectrin Source: FlyBase
  • spectrosome Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000734681 – 2291Spectrin beta chainAdd BLAST2291

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2195Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ00963.
PRIDEiQ00963.

PTM databases

iPTMnetiQ00963.

Expressioni

Gene expression databases

BgeeiFBgn0250788.
ExpressionAtlasiQ00963. baseline.
GenevisibleiQ00963. DM.

Interactioni

Subunit structurei

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.

GO - Molecular functioni

  • actin binding Source: FlyBase
  • ankyrin binding Source: FlyBase
  • cytoskeletal protein binding Source: FlyBase
  • microtubule binding Source: FlyBase

Protein-protein interaction databases

BioGridi59071. 9 interactors.
DIPiDIP-18565N.
IntActiQ00963. 3 interactors.
MINTiMINT-922069.
STRINGi7227.FBpp0074228.

Structurei

Secondary structure

12291
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2146 – 2157Combined sources12
Beta strandi2173 – 2182Combined sources10
Beta strandi2185 – 2191Combined sources7
Helixi2192 – 2195Combined sources4
Beta strandi2219 – 2223Combined sources5
Beta strandi2226 – 2230Combined sources5
Beta strandi2232 – 2234Combined sources3
Beta strandi2236 – 2240Combined sources5
Beta strandi2242 – 2244Combined sources3
Helixi2245 – 2258Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DRONMR-A2142-2262[»]
ProteinModelPortaliQ00963.
SMRiQ00963.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00963.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 271Actin-bindingAdd BLAST271
Domaini50 – 154CH 1PROSITE-ProRule annotationAdd BLAST105
Domaini169 – 271CH 2PROSITE-ProRule annotationAdd BLAST103
Repeati298 – 408Spectrin 1Add BLAST111
Repeati418 – 522Spectrin 2Add BLAST105
Repeati524 – 633Spectrin 3Add BLAST110
Repeati635 – 739Spectrin 4Add BLAST105
Repeati741 – 844Spectrin 5Add BLAST104
Repeati846 – 950Spectrin 6Add BLAST105
Repeati952 – 1057Spectrin 7Add BLAST106
Repeati1059 – 1167Spectrin 8Add BLAST109
Repeati1169 – 1273Spectrin 9Add BLAST105
Repeati1275 – 1378Spectrin 10Add BLAST104
Repeati1380 – 1485Spectrin 11Add BLAST106
Repeati1487 – 1591Spectrin 12Add BLAST105
Repeati1593 – 1697Spectrin 13Add BLAST105
Repeati1699 – 1804Spectrin 14Add BLAST106
Repeati1806 – 1910Spectrin 15Add BLAST105
Repeati1912 – 2016Spectrin 16Add BLAST105
Repeati2018 – 2078Spectrin 17Add BLAST61
Domaini2147 – 2259PHPROSITE-ProRule annotationAdd BLAST113

Sequence similaritiesi

Belongs to the spectrin family.Curated
Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 17 spectrin repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118813.
InParanoidiQ00963.
KOiK06115.
OrthoDBiEOG091G003V.
PhylomeDBiQ00963.

Family and domain databases

CDDicd00014. CH. 2 hits.
Gene3Di1.10.418.10. 2 hits.
2.30.29.30. 1 hit.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011993. PH_dom-like.
IPR001605. PH_dom-spectrin-type.
IPR001849. PH_domain.
IPR018159. Spectrin/alpha-actinin.
IPR016343. Spectrin_bsu.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamiPF00307. CH. 2 hits.
PF00435. Spectrin. 17 hits.
[Graphical view]
PIRSFiPIRSF002297. Spectrin_beta_subunit. 1 hit.
PRINTSiPR00683. SPECTRINPH.
SMARTiSM00033. CH. 2 hits.
SM00233. PH. 1 hit.
SM00150. SPEC. 17 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q00963-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTDISIVRW DPSQGPGNEY IDEYEYDGGN SSSRLFERSR IKALAEERES
60 70 80 90 100
VQKKTFTKWV NSHLCRVNCR IADLYVDMRD GKHLIKLLEV LSGERLPKPT
110 120 130 140 150
KGKMRIHCLE NVDKALQFLR EQRVHLENIG SHDIVDGNAS LNLGLIWTII
160 170 180 190 200
LRFQIQDITI EEVDNKETKS AKDALLLWCQ MKTAGYHNVN VRNFTTSWRD
210 220 230 240 250
GLAFNAIIHK HRPDLVQFEK LSKTNAIHNL NNAFDVAEDK LGLAKLLDAE
260 270 280 290 300
DVFVEHPDEK SIITYVVTYY HYFSKLKQET VQGKRIGKVV GIAMENDKMV
310 320 330 340 350
HDYENFTSDL LKWIETTIQS LGEREFENSL AGVQGQLAQF SNYRTIEKPP
360 370 380 390 400
KFVEKGNLEV LLFTLQSKMR ANNQKPYTPK EGKMISDINK AWERLEKAEH
410 420 430 440 450
ERELALREEL IRQEKLEQLA ARFDRKASMR ETWLSENQRL VSQDNFGFDL
460 470 480 490 500
AAVEAAAKKH EAIETDIFAY EERVQAVVAV CDELESERYH DVKRILLRKD
510 520 530 540 550
NVMRLWTYLL ELLRARRMRL EISLQLQQNF QEMLYILDNM EEIKQLLMTD
560 570 580 590 600
DYGKHLMGVE DLLQKHSLVE ADINILGERV KVVVQNSQKF LSDDPESYKP
610 620 630 640 650
CDPEIIVSRV QQLEDAYAEL VRLAVERRSR LEESRKLWQF YWDTADEENW
660 670 680 690 700
IKEKEQIVST DEVGHDLTTV NLMLSKHKAL ESEITSHDPQ LQNVAKVGSE
710 720 730 740 750
LITEGHFGAD RIKDRLKEIL NKWDHLLDLT KYRRQRLENA VEYFQLFADA
760 770 780 790 800
DDVDNWMLDT LRIVSSEDVG RDEANVQSLL KKHKDVADEL KNYAEVIDAL
810 820 830 840 850
HKQAESLKLN EAEKANVDKR LEAIDNRYKE LTELAKLRKQ RLLDALSLYK
860 870 880 890 900
LMSEADGVEQ WIKEKTKMLD TMTPGKDIED VEIMKHRFEG FDKEMNANAS
910 920 930 940 950
RVAVVNQLAR QLLHVEHPNS DEILERQNHL NQEWSTLREK AEAKMDDLKS
960 970 980 990 1000
AHGVQTFYIE CRETISWIED KKRILTETDS LEMDLTGVMT LQRRLSGMDR
1010 1020 1030 1040 1050
DLAAIQAKLS SLEREANSIE DEHPEEAKII RERIAQIELI WEQLTQMLKE
1060 1070 1080 1090 1100
RDSKLEEAGD LHRFLRDLDH FQTWLTKTQT DVASEDTPTS LPEAEKLLNQ
1110 1120 1130 1140 1150
HQSIREEIDN YTEDYKNMME YGERLTSEGS TSDDPQYMFL RERLNALKDG
1160 1170 1180 1190 1200
WEELHQMWEN RQVLLSQSLD QQLFNRDARQ TEVLLSQQEH FLSKDDTPVN
1210 1220 1230 1240 1250
LEQAENQLKR HEAFLTTMEA NDDKINTLLQ VADTLVEKDH FDADKIGKRA
1260 1270 1280 1290 1300
ENITGRRDDN RQRALDQHEK LKNQVKLHEF LQDLEELAEW VQEKYATSQD
1310 1320 1330 1340 1350
ESYRSAKTIH SKWTRHQAFE AEIAANKERL FEAEKSAQEL SKEKPEFKDV
1360 1370 1380 1390 1400
IEPKLKELAK QFDDLEVHTK EKGAMLFDAN REVLVQQTCD DIDSYITDLE
1410 1420 1430 1440 1450
KQIVSGDTAN DLTSVNILMQ KQQVIQTQMA VKARQVEEID KQTEYLQKTV
1460 1470 1480 1490 1500
PEEKIEPIVV KKTAVLERFE KIKAPLLERQ KALEKKKEAF QFCRDVEDEK
1510 1520 1530 1540 1550
LWIDEKLPVA NSPDYGNSLF NVHVLKKKNQ SLATEIDNHE PRINAICNNG
1560 1570 1580 1590 1600
RKLIDEGHED AKKFEALISD LTQKWQELKD AIENRRKHLL ESEKVQQYFF
1610 1620 1630 1640 1650
DAQEAESWMS EQELYMMVED RGKDEISAQN LMKKHENLEQ SVEDYANTIR
1660 1670 1680 1690 1700
QLGEVARQFS GDDISSGDAV AVKQSQLDKL YAGLKDLAGE RRARLNEALQ
1710 1720 1730 1740 1750
LFMLSREVDD LEQWITDREV VAGSQELGQD FDHVTLLSER FNEFARDTEA
1760 1770 1780 1790 1800
VGGERVAKVN GIADNLIQAG HSDSATIAEW KDNLNESWQD LLELIETRTQ
1810 1820 1830 1840 1850
MLAASRELHK FFHDCKDVLG RILEKQHGVS DELGRDAGSV STLQRKHYNF
1860 1870 1880 1890 1900
LQDLITLYSQ VQQIQEESAK LQDAYAGDKA KEITNREQEV LHAWDNLQAM
1910 1920 1930 1940 1950
CDARKQKLAD TGDLFRFFNM VRILMIWMED LVRQMNTSEK PRDVSGVELL
1960 1970 1980 1990 2000
MNNHQSLKAE IDTREDNFGA CISLGKELLT RNHYASADIK DRLMTLSNSR
2010 2020 2030 2040 2050
NALLRRWEER WENLQLILEV YQFARDAAVA EAWLIAQEPY LLSSELGHTI
2060 2070 2080 2090 2100
DEVENLIKKH EAFEKSAAAQ EERFSALERL TTFELKEMKR RQELAEEAER
2110 2120 2130 2140 2150
QRIKEEQEAK AASEAAEQAK REAERRDDVD VGASHDDSER GGTPGAGEGH
2160 2170 2180 2190 2200
EGYVTRKHEW DSTTKKASNR SWDKVYMAAK AGRISFYKDQ KGYKSNPELT
2210 2220 2230 2240 2250
FRGEPSYDLQ NAAIEIASDY TKKKHVLRVK LANGALFLLQ AHDDTEMSQW
2260 2270 2280 2290
VTSLKAQSDS TAVAASRSQT LPATSQKDEP KRRSFFTLKK K
Length:2,291
Mass (Da):265,739
Last modified:June 1, 2001 - v2
Checksum:i5CDFB0C548BBC39B
GO

Sequence cautioni

The sequence AAR82828 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2278D → Y in AAA28399 (PubMed:1631106).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M92288 mRNA. Translation: AAA28399.1.
AE014298 Genomic DNA. Translation: AAF48751.1.
BT011160 mRNA. Translation: AAR82828.1. Sequence problems.
PIRiA46147.
RefSeqiNP_523388.1. NM_078664.3.
UniGeneiDm.7022.

Genome annotation databases

EnsemblMetazoaiFBtr0074454; FBpp0074228; FBgn0250788.
GeneIDi32746.
KEGGidme:Dmel_CG5870.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M92288 mRNA. Translation: AAA28399.1.
AE014298 Genomic DNA. Translation: AAF48751.1.
BT011160 mRNA. Translation: AAR82828.1. Sequence problems.
PIRiA46147.
RefSeqiNP_523388.1. NM_078664.3.
UniGeneiDm.7022.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DRONMR-A2142-2262[»]
ProteinModelPortaliQ00963.
SMRiQ00963.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59071. 9 interactors.
DIPiDIP-18565N.
IntActiQ00963. 3 interactors.
MINTiMINT-922069.
STRINGi7227.FBpp0074228.

PTM databases

iPTMnetiQ00963.

Proteomic databases

PaxDbiQ00963.
PRIDEiQ00963.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0074454; FBpp0074228; FBgn0250788.
GeneIDi32746.
KEGGidme:Dmel_CG5870.

Organism-specific databases

CTDi32746.
FlyBaseiFBgn0250788. beta-Spec.

Phylogenomic databases

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118813.
InParanoidiQ00963.
KOiK06115.
OrthoDBiEOG091G003V.
PhylomeDBiQ00963.

Enzyme and pathway databases

ReactomeiR-DME-375165. NCAM signaling for neurite out-growth.
R-DME-5673001. RAF/MAP kinase cascade.
R-DME-6807878. COPI-mediated anterograde transport.

Miscellaneous databases

ChiTaRSibeta-Spec. fly.
EvolutionaryTraceiQ00963.
GenomeRNAii32746.
PROiQ00963.

Gene expression databases

BgeeiFBgn0250788.
ExpressionAtlasiQ00963. baseline.
GenevisibleiQ00963. DM.

Family and domain databases

CDDicd00014. CH. 2 hits.
Gene3Di1.10.418.10. 2 hits.
2.30.29.30. 1 hit.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011993. PH_dom-like.
IPR001605. PH_dom-spectrin-type.
IPR001849. PH_domain.
IPR018159. Spectrin/alpha-actinin.
IPR016343. Spectrin_bsu.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamiPF00307. CH. 2 hits.
PF00435. Spectrin. 17 hits.
[Graphical view]
PIRSFiPIRSF002297. Spectrin_beta_subunit. 1 hit.
PRINTSiPR00683. SPECTRINPH.
SMARTiSM00033. CH. 2 hits.
SM00233. PH. 1 hit.
SM00150. SPEC. 17 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSPTCB_DROME
AccessioniPrimary (citable) accession number: Q00963
Secondary accession number(s): Q6NNX2, Q9VX30
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: June 1, 2001
Last modified: November 30, 2016
This is version 167 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.