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P13395

- SPTCA_DROME

UniProt

P13395 - SPTCA_DROME

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
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 2 (20 Jun 2001)
      Previous versions | rss
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    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

    Keywords - Molecular functioni

    Actin capping

    Keywords - Biological processi

    Cell shape

    Keywords - Ligandi

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

    Enzyme and pathway databases

    ReactomeiREACT_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

    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 – 142230
    Helixi1428 – 149467

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2SPCX-ray1.80A/B1391-1497[»]
    ProteinModelPortaliP13395.
    SMRiP13395. Positions 11-2258, 2260-2413.
    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.
    GeneTreeiENSGT00750000117361.
    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

    MENFTPKEVK ILETVEDIQE RREQVLSRYN DFKIETRQKR EKLEDSRRFQ     50
    YFKRDADELE SWIHEKLQAA SEESYRDPTN LQAKIQKHQA FEAEVSAHSN 100
    AIVSLDNTGQ EMINQQHFAS ESIQVRLDEL HKLWELLLSR LAEKGLKLQQ 150
    ALVLVQFLRQ CEEVMFWIKD KETFVTADEF GQDLEHVEVL QRKFDEFQKD 200
    MASQEYRVTE VNQLADKLVQ DGHPERDTIT KRKEELNEAW QRLKQLAIVR 250
    QEKLFGAHEI QRFNRDADET VAWIAEKDVV LSSDDYGRDL ASVQALQRKH 300
    EGVERDLAAL EDKVSTLGAE AQRLCSIHAD HSDQIRDKQA EIANYWQSLT 350
    TKARERKQKL DESYYLHRFL ADFRDLVSWI NGMKAIISAD ELAKDVAGAE 400
    ALLERHQEHK GEIDAREDSF KLTTESGQKL LEREHYAAAE IQEKLAALEN 450
    DKSSLLSLWE DRRILYEQCM DLQLFYRDTE QADTWMAKQE AFLANEDLGD 500
    SLDSVEALIK KHEDFEKSLA AQEEKIKALD IFATKLIDGQ HYAADDVAQR 550
    RQMLLARRAA LQEKSSKRRQ LLEDSNRYQQ FERDCDETKG WISEKLKFAT 600
    DDSYLDPTNL NGKMQKHQNF EHELNANKSR IEDITNVGTE LIEKQHYAAD 650
    QINTRMQEIV VLWETLVQAS DKKGTKLNEA CQQQQFNRTI EDIELWLSEI 700
    EGQLLSEDHG KDLTSVQNLQ KKHALLEADV MAHQDRIESI KVAANKFIES 750
    GHFDADNIRN KEGNLSARYA ALAAPMGERK QHLLDSLQVQ QLFRDLEDEA 800
    AWIREKEPIA ASTNRGRDLI GVQNLIKKHQ AVLAEINNHE ARLLNVISSG 850
    ENMLKDQPFA SDDIRQRLEA LQEQWNTLKE KSSQRKQDLD DSLQAHQYFA 900
    DANEAESWMR EKEPIATGSD YGKDEDSSEA LLKKHEALVS DLEAFGNTIQ 950
    ALQEQAKNCR QQETPVVDIT GKECVVALYD YTEKSPREVS MKKGDVLTLL 1000
    NSNNKDWWKV EVNDRQGFVP AAYIKKIDAG LSASQQNLVD NHSIAKRQNQ 1050
    INSQYDNLLA LARERQNKLN ETVKAYVLVR EAADLAQWIR DKENHAQIAD 1100
    VVGEDLEEVE VLQKKFDDFN DDLKANEVRL ANMNEIAVQL TSLGQTEAAL 1150
    KIQTQMQDLN EKWNNLQTLT AEKASQLGSA HEVQRFHRDI DETKDWIAEK 1200
    ANALNNDDLG KDLRSVQTLQ RKHEGVERDL AALRDKIRQL DETANRLMQS 1250
    HPDTAEQTYA KQKEINEMWD QIITKSTARK EKLLDSYDLQ RFLSDYRDLL 1300
    AWINSMMSLV TSDELANDVT GAEALIERHQ EHRTEIDARA GTFGAFEQFG 1350
    NELLQANHYA SPEIKEKIED LAKAREDLEK AWTERRLQLE QNLDLQLYMR 1400
    DCELAESWMS AREAFLNADD DANAGGNVEA LIKKHEDFDK AINGHEQKIA 1450
    ALQTVADQLI AQNHYASNLV DEKRKQVLER WRHLKEGLIE KRSRLGDEQT 1500
    LQQFSRDADE IENWIAEKLQ LATEESYKDP ANIQSKHQKH QAFEAELAAN 1550
    ADRIQSVLAM GGNLIDKKQC SGSEDAVQKR LTQIADQWEY LTHKTTEKSL 1600
    KLKEANKQRT YIAAVKDLDF WLGEVESLLT TEDSGKDLAS VQNLMKKHQL 1650
    VEADIVAHED RIKDMNNQAD SLVESGQFDT AGIQEKRQSI NERYERICNL 1700
    AAHRQARLNE ALTLHQFFRD IADEESWIKE KKLLVGSDDY GRDLTGVQNL 1750
    KKKHKRLEAE LGSHEPAIQA VQEAGEKLMD VSNLGVPEIE QRLKALNQAW 1800
    AELKNLAATR GQKLDESLTY QQFLAQVEEE EAWITEKQQL LSVEDYGDSM 1850
    AAVQGLLKKH DAFETDFTAH KDRCSLICDQ GSELVEAKNH HGESIAQRCQ 1900
    QLRLKLDNLS ALAARRKGAL LDNSAYLQFM WKADVVESWI DDKENYVRSD 1950
    EFGRDLSTVQ TLLTKQETFD AGLNAFEQEG IHNITALKDQ LINASHAQSP 2000
    AILKRHGDVI ARWQKLRDAS NTRKDRLLAM QEQFRQIEEL YLTFAKKASA 2050
    FNSWFENAEE DLTDPVRCNS IEEIRALRDA HAQFQASLSS AEADFKALAA 2100
    LDQKIKSFNV GPNPYTWFTM EALEETWRNL QKIIEERDGE LAKEAKRQEE 2150
    NDKLRKEFAK HANLFHQWLT ETRTSMMEGS GSLEQQLEAL RVKATEVRAR 2200
    RVDLKKIEEL GALLEEHLIL DNRYTEHSTV GLAQQWDQLD QLSMRMQHNL 2250
    EQQIQARNHS GVSEDSLKEF SMMFKHFDKD KSGKLNHQEF KSCLRALGYD 2300
    LPMVEEGQPD PEFEAILDVV DPNRDGYVSL QEYIAFMISK ETENVQSYEE 2350
    IENAFRAITA ADRPYVTKEE LYCNLTKDMA DYCVQRMKPF SEPRSGQPIK 2400
    DALDYIDFTR TLFQN 2415
    Length:2,415
    Mass (Da):278,303
    Last modified:June 20, 2001 - v2
    Checksum:iF1F72FB990EB0A37
    GO

    Sequence cautioni

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

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2SPC X-ray 1.80 A/B 1391-1497 [» ]
    ProteinModelPortali P13395.
    SMRi P13395. Positions 11-2258, 2260-2413.
    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 ENSGT00750000117361.
    InParanoidi P13395.
    KOi K06114.
    OrthoDBi EOG7GXP9K.
    PhylomeDBi P13395.

    Enzyme and pathway databases

    Reactomei 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

    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: October 1, 2014
    This is version 161 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