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P13395

- SPTCA_DROME

UniProt

P13395 - SPTCA_DROME

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Protein

Spectrin alpha chain

Gene

alpha-Spec

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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. 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.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi2278 – 2289121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi2321 – 2332122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. actin binding Source: FlyBase
  2. calcium ion binding Source: InterPro
  3. cytoskeletal protein binding Source: FlyBase
  4. microtubule binding Source: FlyBase

GO - Biological processi

  1. actin filament capping Source: UniProtKB-KW
  2. axon midline choice point recognition Source: FlyBase
  3. central nervous system development Source: FlyBase
  4. fusome organization Source: FlyBase
  5. germarium-derived female germ-line cyst formation Source: FlyBase
  6. germarium-derived oocyte fate determination Source: FlyBase
  7. germ-line cyst formation Source: FlyBase
  8. long-term strengthening of neuromuscular junction Source: FlyBase
  9. maintenance of presynaptic active zone structure Source: FlyBase
  10. negative regulation of microtubule depolymerization Source: FlyBase
  11. neuromuscular synaptic transmission Source: FlyBase
  12. oocyte construction Source: FlyBase
  13. ovarian follicle cell development Source: FlyBase
  14. plasma membrane organization Source: FlyBase
  15. regulation of cell shape Source: UniProtKB-KW
  16. regulation of synapse organization Source: FlyBase
  17. spectrosome organization Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Biological processi

Cell shape

Keywords - Ligandi

Actin-binding, Calcium, Calmodulin-binding, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_214284. NCAM signaling for neurite out-growth.
REACT_236010. Caspase-mediated cleavage of cytoskeletal proteins.
REACT_256915. Nephrin interactions.
REACT_79920. Interaction between L1 and Ankyrins.
SignaLinkiP13395.

Names & Taxonomyi

Protein namesi
Recommended name:
Spectrin alpha chain
Gene namesi
Name:alpha-Spec
Synonyms:SPEC-A
ORF Names:CG1977
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0250789. alpha-Spec.

Subcellular locationi

Cytoplasmcytoskeleton 1 Publication. Golgi apparatus 1 Publication
Note: Near the inner surface of the plasma membrane of nearly all cells. Lva-alpha-spectrin complexes are found at the Golgi.

GO - Cellular componenti

  1. basolateral plasma membrane Source: FlyBase
  2. cell cortex Source: FlyBase
  3. fusome Source: FlyBase
  4. Golgi apparatus Source: FlyBase
  5. lipid particle Source: FlyBase
  6. neuromuscular junction Source: FlyBase
  7. plasma membrane Source: FlyBase
  8. spectrin Source: FlyBase
  9. spectrosome Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Golgi apparatus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24152415Spectrin alpha chainPRO_0000073467Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1032 – 10321Phosphoserine1 Publication
Modified residuei1034 – 10341Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP13395.
PRIDEiP13395.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

Expressed both maternally and zygotically.

Gene expression databases

BgeeiP13395.

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. Interacts with calmodulin in a calcium-dependent manner, interacts with F-actin and also interacts with Lva. Interacts with Ten-m.2 Publications

Protein-protein interaction databases

BioGridi63763. 17 interactions.
DIPiDIP-17516N.
IntActiP13395. 2 interactions.
MINTiMINT-950099.

Structurei

Secondary structure

1
2415
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1393 – 142230Combined sources
Helixi1428 – 149467Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2SPCX-ray1.80A/B1391-1497[»]
ProteinModelPortaliP13395.
SMRiP13395. Positions 11-2413.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13395.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati18 – 122105Spectrin 1Add
BLAST
Repeati123 – 228106Spectrin 2Add
BLAST
Repeati229 – 334106Spectrin 3Add
BLAST
Repeati335 – 440106Spectrin 4Add
BLAST
Repeati441 – 546106Spectrin 5Add
BLAST
Repeati547 – 651105Spectrin 6Add
BLAST
Repeati652 – 757106Spectrin 7Add
BLAST
Repeati758 – 863106Spectrin 8Add
BLAST
Repeati864 – 969106Spectrin 9Add
BLAST
Repeati970 – 104374Spectrin 10Add
BLAST
Domaini970 – 102960SH3PROSITE-ProRule annotationAdd
BLAST
Repeati1044 – 1151108Spectrin 11Add
BLAST
Repeati1152 – 1257106Spectrin 12Add
BLAST
Repeati1258 – 1363106Spectrin 13Add
BLAST
Repeati1364 – 1469106Spectrin 14Add
BLAST
Repeati1470 – 1576107Spectrin 15Add
BLAST
Repeati1577 – 1682106Spectrin 16Add
BLAST
Repeati1683 – 1788106Spectrin 17Add
BLAST
Repeati1789 – 1894106Spectrin 18Add
BLAST
Repeati1895 – 2001107Spectrin 19Add
BLAST
Repeati2002 – 2115114Spectrin 20Add
BLAST
Repeati2116 – 2229114Spectrin 21Add
BLAST
Repeati2230 – 2335106Spectrin 22Add
BLAST
Domaini2265 – 230036EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini2308 – 234336EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the spectrin family.Curated
Contains 2 EF-hand domains.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation
Contains 22 spectrin repeats.Curated

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiNOG237318.
GeneTreeiENSGT00760000118813.
InParanoidiP13395.
KOiK06114.
OrthoDBiEOG7GXP9K.
PhylomeDBiP13395.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. 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]
PfamiPF13499. EF-hand_7. 1 hit.
PF08726. EFhand_Ca_insen. 1 hit.
PF00018. SH3_1. 1 hit.
PF00435. Spectrin. 20 hits.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.
SMARTiSM00054. EFh. 2 hits.
SM00326. SH3. 1 hit.
SM00150. SPEC. 20 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13395-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MENFTPKEVK ILETVEDIQE RREQVLSRYN DFKIETRQKR EKLEDSRRFQ
60 70 80 90 100
YFKRDADELE SWIHEKLQAA SEESYRDPTN LQAKIQKHQA FEAEVSAHSN
110 120 130 140 150
AIVSLDNTGQ EMINQQHFAS ESIQVRLDEL HKLWELLLSR LAEKGLKLQQ
160 170 180 190 200
ALVLVQFLRQ CEEVMFWIKD KETFVTADEF GQDLEHVEVL QRKFDEFQKD
210 220 230 240 250
MASQEYRVTE VNQLADKLVQ DGHPERDTIT KRKEELNEAW QRLKQLAIVR
260 270 280 290 300
QEKLFGAHEI QRFNRDADET VAWIAEKDVV LSSDDYGRDL ASVQALQRKH
310 320 330 340 350
EGVERDLAAL EDKVSTLGAE AQRLCSIHAD HSDQIRDKQA EIANYWQSLT
360 370 380 390 400
TKARERKQKL DESYYLHRFL ADFRDLVSWI NGMKAIISAD ELAKDVAGAE
410 420 430 440 450
ALLERHQEHK GEIDAREDSF KLTTESGQKL LEREHYAAAE IQEKLAALEN
460 470 480 490 500
DKSSLLSLWE DRRILYEQCM DLQLFYRDTE QADTWMAKQE AFLANEDLGD
510 520 530 540 550
SLDSVEALIK KHEDFEKSLA AQEEKIKALD IFATKLIDGQ HYAADDVAQR
560 570 580 590 600
RQMLLARRAA LQEKSSKRRQ LLEDSNRYQQ FERDCDETKG WISEKLKFAT
610 620 630 640 650
DDSYLDPTNL NGKMQKHQNF EHELNANKSR IEDITNVGTE LIEKQHYAAD
660 670 680 690 700
QINTRMQEIV VLWETLVQAS DKKGTKLNEA CQQQQFNRTI EDIELWLSEI
710 720 730 740 750
EGQLLSEDHG KDLTSVQNLQ KKHALLEADV MAHQDRIESI KVAANKFIES
760 770 780 790 800
GHFDADNIRN KEGNLSARYA ALAAPMGERK QHLLDSLQVQ QLFRDLEDEA
810 820 830 840 850
AWIREKEPIA ASTNRGRDLI GVQNLIKKHQ AVLAEINNHE ARLLNVISSG
860 870 880 890 900
ENMLKDQPFA SDDIRQRLEA LQEQWNTLKE KSSQRKQDLD DSLQAHQYFA
910 920 930 940 950
DANEAESWMR EKEPIATGSD YGKDEDSSEA LLKKHEALVS DLEAFGNTIQ
960 970 980 990 1000
ALQEQAKNCR QQETPVVDIT GKECVVALYD YTEKSPREVS MKKGDVLTLL
1010 1020 1030 1040 1050
NSNNKDWWKV EVNDRQGFVP AAYIKKIDAG LSASQQNLVD NHSIAKRQNQ
1060 1070 1080 1090 1100
INSQYDNLLA LARERQNKLN ETVKAYVLVR EAADLAQWIR DKENHAQIAD
1110 1120 1130 1140 1150
VVGEDLEEVE VLQKKFDDFN DDLKANEVRL ANMNEIAVQL TSLGQTEAAL
1160 1170 1180 1190 1200
KIQTQMQDLN EKWNNLQTLT AEKASQLGSA HEVQRFHRDI DETKDWIAEK
1210 1220 1230 1240 1250
ANALNNDDLG KDLRSVQTLQ RKHEGVERDL AALRDKIRQL DETANRLMQS
1260 1270 1280 1290 1300
HPDTAEQTYA KQKEINEMWD QIITKSTARK EKLLDSYDLQ RFLSDYRDLL
1310 1320 1330 1340 1350
AWINSMMSLV TSDELANDVT GAEALIERHQ EHRTEIDARA GTFGAFEQFG
1360 1370 1380 1390 1400
NELLQANHYA SPEIKEKIED LAKAREDLEK AWTERRLQLE QNLDLQLYMR
1410 1420 1430 1440 1450
DCELAESWMS AREAFLNADD DANAGGNVEA LIKKHEDFDK AINGHEQKIA
1460 1470 1480 1490 1500
ALQTVADQLI AQNHYASNLV DEKRKQVLER WRHLKEGLIE KRSRLGDEQT
1510 1520 1530 1540 1550
LQQFSRDADE IENWIAEKLQ LATEESYKDP ANIQSKHQKH QAFEAELAAN
1560 1570 1580 1590 1600
ADRIQSVLAM GGNLIDKKQC SGSEDAVQKR LTQIADQWEY LTHKTTEKSL
1610 1620 1630 1640 1650
KLKEANKQRT YIAAVKDLDF WLGEVESLLT TEDSGKDLAS VQNLMKKHQL
1660 1670 1680 1690 1700
VEADIVAHED RIKDMNNQAD SLVESGQFDT AGIQEKRQSI NERYERICNL
1710 1720 1730 1740 1750
AAHRQARLNE ALTLHQFFRD IADEESWIKE KKLLVGSDDY GRDLTGVQNL
1760 1770 1780 1790 1800
KKKHKRLEAE LGSHEPAIQA VQEAGEKLMD VSNLGVPEIE QRLKALNQAW
1810 1820 1830 1840 1850
AELKNLAATR GQKLDESLTY QQFLAQVEEE EAWITEKQQL LSVEDYGDSM
1860 1870 1880 1890 1900
AAVQGLLKKH DAFETDFTAH KDRCSLICDQ GSELVEAKNH HGESIAQRCQ
1910 1920 1930 1940 1950
QLRLKLDNLS ALAARRKGAL LDNSAYLQFM WKADVVESWI DDKENYVRSD
1960 1970 1980 1990 2000
EFGRDLSTVQ TLLTKQETFD AGLNAFEQEG IHNITALKDQ LINASHAQSP
2010 2020 2030 2040 2050
AILKRHGDVI ARWQKLRDAS NTRKDRLLAM QEQFRQIEEL YLTFAKKASA
2060 2070 2080 2090 2100
FNSWFENAEE DLTDPVRCNS IEEIRALRDA HAQFQASLSS AEADFKALAA
2110 2120 2130 2140 2150
LDQKIKSFNV GPNPYTWFTM EALEETWRNL QKIIEERDGE LAKEAKRQEE
2160 2170 2180 2190 2200
NDKLRKEFAK HANLFHQWLT ETRTSMMEGS GSLEQQLEAL RVKATEVRAR
2210 2220 2230 2240 2250
RVDLKKIEEL GALLEEHLIL DNRYTEHSTV GLAQQWDQLD QLSMRMQHNL
2260 2270 2280 2290 2300
EQQIQARNHS GVSEDSLKEF SMMFKHFDKD KSGKLNHQEF KSCLRALGYD
2310 2320 2330 2340 2350
LPMVEEGQPD PEFEAILDVV DPNRDGYVSL QEYIAFMISK ETENVQSYEE
2360 2370 2380 2390 2400
IENAFRAITA ADRPYVTKEE LYCNLTKDMA DYCVQRMKPF SEPRSGQPIK
2410
DALDYIDFTR TLFQN
Length:2,415
Mass (Da):278,303
Last modified:June 20, 2001 - v2
Checksum:iF1F72FB990EB0A37
GO

Sequence cautioni

The sequence AAL39886.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence ABA81823.1 differs from that shown. Reason: Frameshift at position 1549. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 1101Q → D in AAB29441. (PubMed:8276898)Curated
Sequence conflicti212 – 2121N → I in ABA81823. 1 PublicationCurated
Sequence conflicti337 – 3371D → G in ABA81823. 1 PublicationCurated
Sequence conflicti651 – 6511Q → L in ABA81823. 1 PublicationCurated
Sequence conflicti1555 – 15551Q → H in AAL39886. (PubMed:12537569)Curated
Sequence conflicti1562 – 15621G → E in ABA81823. 1 PublicationCurated
Sequence conflicti1668 – 16681Q → R in AAA28907. (PubMed:2808524)Curated
Sequence conflicti1908 – 19081N → S in ABA81823. 1 PublicationCurated
Sequence conflicti2203 – 22031D → G in ABA81823. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA33733.
RefSeqiNP_476739.1. NM_057391.4.
UniGeneiDm.7397.

Genome annotation databases

EnsemblMetazoaiFBtr0072789; FBpp0072672; FBgn0250789.
GeneIDi38231.
KEGGidme:Dmel_CG1977.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRi A33733.
RefSeqi NP_476739.1. NM_057391.4.
UniGenei Dm.7397.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2SPC X-ray 1.80 A/B 1391-1497 [» ]
ProteinModelPortali P13395.
SMRi P13395. Positions 11-2413.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 63763. 17 interactions.
DIPi DIP-17516N.
IntActi P13395. 2 interactions.
MINTi MINT-950099.

Proteomic databases

PaxDbi P13395.
PRIDEi P13395.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0072789 ; FBpp0072672 ; FBgn0250789 .
GeneIDi 38231.
KEGGi dme:Dmel_CG1977.

Organism-specific databases

CTDi 38231.
FlyBasei FBgn0250789. alpha-Spec.

Phylogenomic databases

eggNOGi NOG237318.
GeneTreei ENSGT00760000118813.
InParanoidi P13395.
KOi K06114.
OrthoDBi EOG7GXP9K.
PhylomeDBi P13395.

Enzyme and pathway databases

Reactomei REACT_214284. NCAM signaling for neurite out-growth.
REACT_236010. Caspase-mediated cleavage of cytoskeletal proteins.
REACT_256915. Nephrin interactions.
REACT_79920. Interaction between L1 and Ankyrins.
SignaLinki P13395.

Miscellaneous databases

EvolutionaryTracei P13395.
GenomeRNAii 38231.
NextBioi 807649.
PROi P13395.

Gene expression databases

Bgeei P13395.

Family and domain databases

Gene3Di 1.10.238.10. 2 hits.
InterProi IPR011992. 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 ]
Pfami PF13499. EF-hand_7. 1 hit.
PF08726. EFhand_Ca_insen. 1 hit.
PF00018. SH3_1. 1 hit.
PF00435. Spectrin. 20 hits.
[Graphical view ]
PRINTSi PR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.
SMARTi SM00054. EFh. 2 hits.
SM00326. SH3. 1 hit.
SM00150. SPEC. 20 hits.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiSPTCA_DROME
AccessioniPrimary (citable) accession number: P13395
Secondary accession number(s): Q26340
, Q3KN50, Q8SZW7, Q9W085
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: June 20, 2001
Last modified: November 26, 2014
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

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

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

External Data

Dasty 3