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P13395 (SPTCA_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Spectrin alpha chain
Gene names
Name:alpha-Spec
Synonyms:SPEC-A
ORF Names:CG1977
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length2415 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Essential for larval survival and development. Stabilizes cell to cell interactions that are critical for the maintenance of cell shape and subcellular organization within embryonic tissues. Lva and spectrin may form a Golgi-based scaffold that mediates interaction of Golgi bodies with microtubules and facilitates Golgi-derived membrane secretion required for the formation of furrows during cellularization. Ref.5 Ref.7 Ref.8

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. Interacts with calmodulin in a calcium-dependent manner, interacts with F-actin and also interacts with Lva. Interacts with Ten-m. Ref.8 Ref.13

Subcellular location

Cytoplasmcytoskeleton. Golgi apparatus. Note: Near the inner surface of the plasma membrane of nearly all cells. Lva-alpha-spectrin complexes are found at the Golgi. Ref.8

Tissue specificity

A substantial pool of maternal protein in the egg undergoes dynamic changes in distribution early in embryogenesis. In gastrulated embryo, the highest level of protein is found in the respiratory tract cells and the lowest in parts of the forming gut. Ref.9

Developmental stage

Expressed both maternally and zygotically.

Miscellaneous

Its transcript shares the first untranslated exon with the dlt transcript, suggesting a common regulation.

Sequence similarities

Belongs to the spectrin family.

Contains 2 EF-hand domains.

Contains 1 SH3 domain.

Contains 22 spectrin repeats.

Sequence caution

The sequence AAL39886.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence ABA81823.1 differs from that shown. Reason: Frameshift at position 1549.

Ontologies

Keywords
   Biological processCell shape
   Cellular componentCytoplasm
Cytoskeleton
Golgi apparatus
   DomainRepeat
SH3 domain
   LigandActin-binding
Calcium
Calmodulin-binding
Metal-binding
   Molecular functionActin capping
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament capping

Inferred from electronic annotation. Source: UniProtKB-KW

axon midline choice point recognition

Inferred from genetic interaction PubMed 17121810. Source: FlyBase

central nervous system development

Inferred from mutant phenotype PubMed 10328928. Source: FlyBase

fusome organization

Traceable author statement PubMed 10370240PubMed 11131529. Source: FlyBase

germ-line cyst formation

Traceable author statement PubMed 10370240. Source: FlyBase

germarium-derived female germ-line cyst formation

Inferred from mutant phenotype PubMed 9012516. Source: FlyBase

germarium-derived oocyte fate determination

Inferred from mutant phenotype PubMed 9012516. Source: FlyBase

long-term strengthening of neuromuscular junction

Inferred from mutant phenotype PubMed 15916948. Source: FlyBase

maintenance of presynaptic active zone structure

Inferred from direct assay PubMed 17088429. Source: FlyBase

negative regulation of microtubule depolymerization

Inferred from mutant phenotype PubMed 15916948. Source: FlyBase

neuromuscular synaptic transmission

Inferred from mutant phenotype PubMed 11404407. Source: FlyBase

oocyte construction

Inferred from mutant phenotype PubMed 9012516. Source: FlyBase

ovarian follicle cell development

Traceable author statement PubMed 10822261. Source: FlyBase

plasma membrane organization

Traceable author statement Ref.8. Source: FlyBase

regulation of cell shape

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of synapse organization

Inferred from mutant phenotype PubMed 15916948. Source: FlyBase

spectrosome organization

Traceable author statement PubMed 11131529. Source: FlyBase

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.8. Source: FlyBase

basolateral plasma membrane

Inferred from direct assay PubMed 19672952. Source: FlyBase

cell cortex

Inferred from direct assay Ref.8. Source: FlyBase

fusome

Inferred from direct assay PubMed 9012516. Source: FlyBase

lipid particle

Inferred from direct assay PubMed 16543254. Source: FlyBase

neuromuscular junction

Inferred from direct assay PubMed 18070911. Source: FlyBase

plasma membrane

Inferred from direct assay Ref.8PubMed 19672952PubMed 20462449PubMed 9348534. Source: FlyBase

spectrin

Inferred from sequence or structural similarity PubMed 10908588. Source: FlyBase

spectrosome

Inferred from direct assay PubMed 9012516. Source: FlyBase

   Molecular_functionactin binding

Inferred from direct assay Ref.8. Source: FlyBase

calcium ion binding

Inferred from electronic annotation. Source: InterPro

cytoskeletal protein binding

Inferred from sequence or structural similarity PubMed 10908588. Source: FlyBase

microtubule binding

Inferred from direct assay Ref.8. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24152415Spectrin alpha chain
PRO_0000073467

Regions

Repeat18 – 122105Spectrin 1
Repeat123 – 228106Spectrin 2
Repeat229 – 334106Spectrin 3
Repeat335 – 440106Spectrin 4
Repeat441 – 546106Spectrin 5
Repeat547 – 651105Spectrin 6
Repeat652 – 757106Spectrin 7
Repeat758 – 863106Spectrin 8
Repeat864 – 969106Spectrin 9
Repeat970 – 104374Spectrin 10
Domain970 – 102960SH3
Repeat1044 – 1151108Spectrin 11
Repeat1152 – 1257106Spectrin 12
Repeat1258 – 1363106Spectrin 13
Repeat1364 – 1469106Spectrin 14
Repeat1470 – 1576107Spectrin 15
Repeat1577 – 1682106Spectrin 16
Repeat1683 – 1788106Spectrin 17
Repeat1789 – 1894106Spectrin 18
Repeat1895 – 2001107Spectrin 19
Repeat2002 – 2115114Spectrin 20
Repeat2116 – 2229114Spectrin 21
Repeat2230 – 2335106Spectrin 22
Domain2265 – 230036EF-hand 1
Domain2308 – 234336EF-hand 2
Calcium binding2278 – 2289121 Potential
Calcium binding2321 – 2332122 Potential

Amino acid modifications

Modified residue10321Phosphoserine Ref.12
Modified residue10341Phosphoserine Ref.11 Ref.12

Experimental info

Sequence conflict1101Q → D in AAB29441. Ref.5
Sequence conflict2121N → I in ABA81823. Ref.4
Sequence conflict3371D → G in ABA81823. Ref.4
Sequence conflict6511Q → L in ABA81823. Ref.4
Sequence conflict15551Q → H in AAL39886. Ref.6
Sequence conflict15621G → E in ABA81823. Ref.4
Sequence conflict16681Q → R in AAA28907. Ref.1
Sequence conflict19081N → S in ABA81823. Ref.4
Sequence conflict22031D → G in ABA81823. Ref.4

Secondary structure

..... 2415
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13395 [UniParc].

Last modified June 20, 2001. Version 2.
Checksum: F1F72FB990EB0A37

FASTA2,415278,303
        10         20         30         40         50         60 
MENFTPKEVK ILETVEDIQE RREQVLSRYN DFKIETRQKR EKLEDSRRFQ YFKRDADELE 

        70         80         90        100        110        120 
SWIHEKLQAA SEESYRDPTN LQAKIQKHQA FEAEVSAHSN AIVSLDNTGQ EMINQQHFAS 

       130        140        150        160        170        180 
ESIQVRLDEL HKLWELLLSR LAEKGLKLQQ ALVLVQFLRQ CEEVMFWIKD KETFVTADEF 

       190        200        210        220        230        240 
GQDLEHVEVL QRKFDEFQKD MASQEYRVTE VNQLADKLVQ DGHPERDTIT KRKEELNEAW 

       250        260        270        280        290        300 
QRLKQLAIVR QEKLFGAHEI QRFNRDADET VAWIAEKDVV LSSDDYGRDL ASVQALQRKH 

       310        320        330        340        350        360 
EGVERDLAAL EDKVSTLGAE AQRLCSIHAD HSDQIRDKQA EIANYWQSLT TKARERKQKL 

       370        380        390        400        410        420 
DESYYLHRFL ADFRDLVSWI NGMKAIISAD ELAKDVAGAE ALLERHQEHK GEIDAREDSF 

       430        440        450        460        470        480 
KLTTESGQKL LEREHYAAAE IQEKLAALEN DKSSLLSLWE DRRILYEQCM DLQLFYRDTE 

       490        500        510        520        530        540 
QADTWMAKQE AFLANEDLGD SLDSVEALIK KHEDFEKSLA AQEEKIKALD IFATKLIDGQ 

       550        560        570        580        590        600 
HYAADDVAQR RQMLLARRAA LQEKSSKRRQ LLEDSNRYQQ FERDCDETKG WISEKLKFAT 

       610        620        630        640        650        660 
DDSYLDPTNL NGKMQKHQNF EHELNANKSR IEDITNVGTE LIEKQHYAAD QINTRMQEIV 

       670        680        690        700        710        720 
VLWETLVQAS DKKGTKLNEA CQQQQFNRTI EDIELWLSEI EGQLLSEDHG KDLTSVQNLQ 

       730        740        750        760        770        780 
KKHALLEADV MAHQDRIESI KVAANKFIES GHFDADNIRN KEGNLSARYA ALAAPMGERK 

       790        800        810        820        830        840 
QHLLDSLQVQ QLFRDLEDEA AWIREKEPIA ASTNRGRDLI GVQNLIKKHQ AVLAEINNHE 

       850        860        870        880        890        900 
ARLLNVISSG ENMLKDQPFA SDDIRQRLEA LQEQWNTLKE KSSQRKQDLD DSLQAHQYFA 

       910        920        930        940        950        960 
DANEAESWMR EKEPIATGSD YGKDEDSSEA LLKKHEALVS DLEAFGNTIQ ALQEQAKNCR 

       970        980        990       1000       1010       1020 
QQETPVVDIT GKECVVALYD YTEKSPREVS MKKGDVLTLL NSNNKDWWKV EVNDRQGFVP 

      1030       1040       1050       1060       1070       1080 
AAYIKKIDAG LSASQQNLVD NHSIAKRQNQ INSQYDNLLA LARERQNKLN ETVKAYVLVR 

      1090       1100       1110       1120       1130       1140 
EAADLAQWIR DKENHAQIAD VVGEDLEEVE VLQKKFDDFN DDLKANEVRL ANMNEIAVQL 

      1150       1160       1170       1180       1190       1200 
TSLGQTEAAL KIQTQMQDLN EKWNNLQTLT AEKASQLGSA HEVQRFHRDI DETKDWIAEK 

      1210       1220       1230       1240       1250       1260 
ANALNNDDLG KDLRSVQTLQ RKHEGVERDL AALRDKIRQL DETANRLMQS HPDTAEQTYA 

      1270       1280       1290       1300       1310       1320 
KQKEINEMWD QIITKSTARK EKLLDSYDLQ RFLSDYRDLL AWINSMMSLV TSDELANDVT 

      1330       1340       1350       1360       1370       1380 
GAEALIERHQ EHRTEIDARA GTFGAFEQFG NELLQANHYA SPEIKEKIED LAKAREDLEK 

      1390       1400       1410       1420       1430       1440 
AWTERRLQLE QNLDLQLYMR DCELAESWMS AREAFLNADD DANAGGNVEA LIKKHEDFDK 

      1450       1460       1470       1480       1490       1500 
AINGHEQKIA ALQTVADQLI AQNHYASNLV DEKRKQVLER WRHLKEGLIE KRSRLGDEQT 

      1510       1520       1530       1540       1550       1560 
LQQFSRDADE IENWIAEKLQ LATEESYKDP ANIQSKHQKH QAFEAELAAN ADRIQSVLAM 

      1570       1580       1590       1600       1610       1620 
GGNLIDKKQC SGSEDAVQKR LTQIADQWEY LTHKTTEKSL KLKEANKQRT YIAAVKDLDF 

      1630       1640       1650       1660       1670       1680 
WLGEVESLLT TEDSGKDLAS VQNLMKKHQL VEADIVAHED RIKDMNNQAD SLVESGQFDT 

      1690       1700       1710       1720       1730       1740 
AGIQEKRQSI NERYERICNL AAHRQARLNE ALTLHQFFRD IADEESWIKE KKLLVGSDDY 

      1750       1760       1770       1780       1790       1800 
GRDLTGVQNL KKKHKRLEAE LGSHEPAIQA VQEAGEKLMD VSNLGVPEIE QRLKALNQAW 

      1810       1820       1830       1840       1850       1860 
AELKNLAATR GQKLDESLTY QQFLAQVEEE EAWITEKQQL LSVEDYGDSM AAVQGLLKKH 

      1870       1880       1890       1900       1910       1920 
DAFETDFTAH KDRCSLICDQ GSELVEAKNH HGESIAQRCQ QLRLKLDNLS ALAARRKGAL 

      1930       1940       1950       1960       1970       1980 
LDNSAYLQFM WKADVVESWI DDKENYVRSD EFGRDLSTVQ TLLTKQETFD AGLNAFEQEG 

      1990       2000       2010       2020       2030       2040 
IHNITALKDQ LINASHAQSP AILKRHGDVI ARWQKLRDAS NTRKDRLLAM QEQFRQIEEL 

      2050       2060       2070       2080       2090       2100 
YLTFAKKASA FNSWFENAEE DLTDPVRCNS IEEIRALRDA HAQFQASLSS AEADFKALAA 

      2110       2120       2130       2140       2150       2160 
LDQKIKSFNV GPNPYTWFTM EALEETWRNL QKIIEERDGE LAKEAKRQEE NDKLRKEFAK 

      2170       2180       2190       2200       2210       2220 
HANLFHQWLT ETRTSMMEGS GSLEQQLEAL RVKATEVRAR RVDLKKIEEL GALLEEHLIL 

      2230       2240       2250       2260       2270       2280 
DNRYTEHSTV GLAQQWDQLD QLSMRMQHNL EQQIQARNHS GVSEDSLKEF SMMFKHFDKD 

      2290       2300       2310       2320       2330       2340 
KSGKLNHQEF KSCLRALGYD LPMVEEGQPD PEFEAILDVV DPNRDGYVSL QEYIAFMISK 

      2350       2360       2370       2380       2390       2400 
ETENVQSYEE IENAFRAITA ADRPYVTKEE LYCNLTKDMA DYCVQRMKPF SEPRSGQPIK 

      2410 
DALDYIDFTR TLFQN 

« Hide

References

« Hide 'large scale' references
[1]"The complete sequence of Drosophila alpha-spectrin: conservation of structural domains between alpha-spectrins and alpha-actinin."
Dubreuil R.R., Byers T.J., Sillman A.L., Bar-Zvi D., Goldstein L.S.B., Branton D.
J. Cell Biol. 109:2197-2205(1989) [PubMed] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[5]"Cell shape and interaction defects in alpha-spectrin mutants of Drosophila melanogaster."
Lee J.K., Coyne R.S., Dubreuil R.R., Goldstein L.S.B., Branton D.
J. Cell Biol. 123:1797-1809(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-150 AND 2192-2415, FUNCTION.
[6]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1539-2415.
Strain: Berkeley.
Tissue: Larva and Pupae.
[7]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Lava lamp, a novel peripheral Golgi protein, is required for Drosophila melanogaster cellularization."
Sisson J.C., Field C., Ventura R., Royou A., Sullivan W.
J. Cell Biol. 151:905-918(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
[9]"Drosophila spectrin: the membrane skeleton during embryogenesis."
Pesacreta T.C., Byers T.J., Dubreuil R., Kiehart D.P., Branton D.
J. Cell Biol. 108:1697-1709(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[10]"The Drosophila cell survival gene discs lost encodes a cytoplasmic Codanin-1-like protein, not a homolog of tight junction PDZ protein Patj."
Pielage J., Stork T., Bunse I., Klaembt C.
Dev. Cell 5:841-851(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE STRUCTURE.
[11]"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1034, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1032 AND SER-1034, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
[13]"Trans-synaptic Teneurin signalling in neuromuscular synapse organization and target choice."
Mosca T.J., Hong W., Dani V.S., Favaloro V., Luo L.
Nature 484:237-241(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TEN-M.
[14]"Crystal structure of the repetitive segments of spectrin."
Yan Y., Winograd E., Viel A., Cronin T., Harrison S.C., Branton D.
Science 262:2027-2030(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1391-1497.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M26400 mRNA. Translation: AAA28907.1.
AE014296 Genomic DNA. Translation: AAF47569.1.
BT023889 mRNA. Translation: ABA81823.1. Frameshift.
S67762 Genomic DNA. Translation: AAB29441.2.
S67765 Genomic DNA. Translation: AAB29442.1.
AY069741 mRNA. Translation: AAL39886.1. Different initiation.
PIRA33733.
RefSeqNP_476739.1. NM_057391.4.
UniGeneDm.7397.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2SPCX-ray1.80A/B1391-1497[»]
ProteinModelPortalP13395.
SMRP13395. Positions 11-2258, 2260-2413.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid63763. 17 interactions.
DIPDIP-17516N.
IntActP13395. 2 interactions.
MINTMINT-950099.

Proteomic databases

PaxDbP13395.
PRIDEP13395.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0072789; FBpp0072672; FBgn0250789.
GeneID38231.
KEGGdme:Dmel_CG1977.

Organism-specific databases

CTD38231.
FlyBaseFBgn0250789. alpha-Spec.

Phylogenomic databases

eggNOGNOG237318.
GeneTreeENSGT00750000117361.
InParanoidP13395.
KOK06114.
OrthoDBEOG7GXP9K.
PhylomeDBP13395.

Enzyme and pathway databases

SignaLinkP13395.

Gene expression databases

BgeeP13395.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
InterProIPR011992. EF-hand-dom_pair.
IPR014837. EF-hand_Ca_insen.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001452. SH3_domain.
IPR018159. Spectrin/alpha-actinin.
IPR013315. Spectrin_alpha_SH3.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamPF13499. EF-hand_7. 1 hit.
PF08726. EFhand_Ca_insen. 1 hit.
PF00018. SH3_1. 1 hit.
PF00435. Spectrin. 20 hits.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.
SMARTSM00054. EFh. 2 hits.
SM00326. SH3. 1 hit.
SM00150. SPEC. 20 hits.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS50002. SH3. 1 hit.
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Other

EvolutionaryTraceP13395.
GenomeRNAi38231.
NextBio807649.
PROP13395.

Entry information

Entry nameSPTCA_DROME
AccessionPrimary (citable) accession number: P13395
Secondary accession number(s): Q26340 expand/collapse secondary AC list , Q3KN50, Q8SZW7, Q9W085
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: June 20, 2001
Last modified: April 16, 2014
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase