P13395 (SPTCA_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Spectrin alpha chain

Gene names

Name:	alpha-Spec
Synonyms:	SPEC-A
ORF Names:	CG1977

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	2415 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. 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	Cytoplasm › cytoskeleton. 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.
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 process	Cell shape
Cellular component	Cytoplasm Cytoskeleton Golgi apparatus
Domain	Repeat SH3 domain
Ligand	Actin-binding Calcium Calmodulin-binding Metal-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 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 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 spectrosome organization Traceable author statement PubMed 11131529. Source: FlyBase
Cellular_component	Golgi apparatus Inferred from direct assay Ref.8. Source: FlyBase basolateral plasma membrane Inferred from direct assay PubMed 19672952. 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 spectrin Inferred from sequence or structural similarity PubMed 10908588. Source: FlyBase spectrosome Inferred from direct assay PubMed 9012516. Source: FlyBase
Molecular_function	actin binding Inferred from direct assay Ref.8. Source: FlyBase calcium ion binding Inferred from electronic annotation. Source: InterPro microtubule binding Inferred from direct assay Ref.8. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2415

2415

Spectrin alpha chain

PRO_0000073467

Regions

Repeat

18 – 122

105

Spectrin 1

Repeat

123 – 228

106

Spectrin 2

Repeat

229 – 334

106

Spectrin 3

Repeat

335 – 440

106

Spectrin 4

Repeat

441 – 546

106

Spectrin 5

Repeat

547 – 651

105

Spectrin 6

Repeat

652 – 757

106

Spectrin 7

Repeat

758 – 863

106

Spectrin 8

Repeat

864 – 969

106

Spectrin 9

Repeat

970 – 1043

74

Spectrin 10

Domain

970 – 1029

60

SH3

Repeat

1044 – 1151

108

Spectrin 11

Repeat

1152 – 1257

106

Spectrin 12

Repeat

1258 – 1363

106

Spectrin 13

Repeat

1364 – 1469

106

Spectrin 14

Repeat

1470 – 1576

107

Spectrin 15

Repeat

1577 – 1682

106

Spectrin 16

Repeat

1683 – 1788

106

Spectrin 17

Repeat

1789 – 1894

106

Spectrin 18

Repeat

1895 – 2001

107

Spectrin 19

Repeat

2002 – 2115

114

Spectrin 20

Repeat

2116 – 2229

114

Spectrin 21

Repeat

2230 – 2335

106

Spectrin 22

Domain

2265 – 2300

36

EF-hand 1

Domain

2308 – 2343

36

EF-hand 2

Calcium binding

2278 – 2289

12

1 Potential

Calcium binding

2321 – 2332

12

2 Potential

Amino acid modifications

Modified residue

1032

1

Phosphoserine Ref.12

Modified residue

1034

1

Phosphoserine Ref.11 Ref.12

Experimental info

Sequence conflict

110

1

Q → D in AAB29441. Ref.5

Sequence conflict

212

1

N → I in ABA81823. Ref.4

Sequence conflict

337

1

D → G in ABA81823. Ref.4

Sequence conflict

651

1

Q → L in ABA81823. Ref.4

Sequence conflict

1555

1

Q → H in AAL39886. Ref.6

Sequence conflict

1562

1

G → E in ABA81823. Ref.4

Sequence conflict

1668

1

Q → R in AAA28907. Ref.1

Sequence conflict

1908

1

N → S in ABA81823. Ref.4

Sequence conflict

2203

1

D → G in ABA81823. Ref.4

Secondary structure

1

.

.

.

.

.

2415

Helix Strand Turn

Details...

Helix

1393 – 1422

30

Helix

1428 – 1494

67

Sequences

	Sequence		Length	Mass (Da)
	P13395 [UniParc]. Last modified June 20, 2001. Version 2. Checksum: F1F72FB990EB0A37	FASTA	2,415	278,303
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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: EMBRYONIC LOCALIZATION.
[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, 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, 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.

PIR

A33733.

RefSeq

NP_476739.1. NM_057391.4.

UniGene

Dm.7397.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2SPC	X-ray	1.80	A/B	1391-1497	[»]

ProteinModelPortal

P13395.

SMR

P13395. Positions 11-2258, 2263-2413.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-17516N.

IntAct

P13395. 2 interactions.

MINT

MINT-950099.

Proteomic databases

PaxDb

P13395.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0072789; FBpp0072672; FBgn0250789.

GeneID

38231.

KEGG

dme:Dmel_CG1977.

Organism-specific databases

CTD

38231.

FlyBase

FBgn0250789. alpha-Spec.

Phylogenomic databases

eggNOG

NOG237318.

GeneTree

ENSGT00700000104022.

InParanoid

P13395.

KO

K06114.

OMA

MELHRQW.

OrthoDB

EOG4B5MKX.

PhylomeDB

P13395.

Gene expression databases

Bgee

P13395.

GermOnline

CG1977. Drosophila melanogaster.

Family and domain databases

Gene3D

1.10.238.10. 2 hits.

InterPro

IPR011992. EF-hand-like_dom.
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]

Pfam

PF13499. EF_hand_5. 1 hit.
PF08726. efhand_Ca_insen. 1 hit.
PF00018. SH3_1. 1 hit.
PF00435. Spectrin. 20 hits.
[Graphical view]

PRINTS

PR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.

SMART

SM00054. EFh. 2 hits.
SM00326. SH3. 1 hit.
SM00150. SPEC. 20 hits.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P13395.

GenomeRNAi

38231.

NextBio

807649.

Entry information

Entry name

SPTCA_DROME

Accession

Primary (citable) accession number: P13395
Secondary accession number(s): Q26340 , Q3KN50, Q8SZW7, Q9W085

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	June 20, 2001
Last modified:	May 1, 2013
This is version 151 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project