GenomeNet

Database: UniProt
Entry: Q9V8R9
LinkDB: Q9V8R9
Original site: Q9V8R9 
ID   41_DROME                Reviewed;        1698 AA.
AC   Q9V8R9; A1ZBI0; Q1WWD0; Q24440; Q24441; Q24442; Q9V8R8; Q9V8S0;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   09-JUL-2014, entry version 120.
DE   RecName: Full=Protein 4.1 homolog;
DE   AltName: Full=Protein coracle;
GN   Name=cora; ORFNames=CG11949;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF
RP   278-1698 (ISOFORMS 2 AND 3), AND FUNCTION.
RC   STRAIN=Oregon-R; TISSUE=Embryo;
RX   PubMed=8162854;
RA   Fehon R.G., Dawson I.A., Artavanis-Tsakonas S.;
RT   "A Drosophila homologue of membrane-skeleton protein 4.1 is associated
RT   with septate junctions and is encoded by the coracle gene.";
RL   Development 120:545-557(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   STRAIN=Berkeley;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=Berkeley;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A.,
RA   Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-659 AND SER-1590, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17372656; DOI=10.1039/b617545g;
RA   Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,
RA   Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
RT   "An integrated chemical, mass spectrometric and computational strategy
RT   for (quantitative) phosphoproteomics: application to Drosophila
RT   melanogaster Kc167 cells.";
RL   Mol. Biosyst. 3:275-286(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471; SER-474; SER-478;
RP   SER-566; SER-687; THR-689; SER-697; SER-1398; SER-1401; SER-1402 AND
RP   THR-1407, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: An integral component of the septate junction. May play
CC       a role in cell-cell interactions that are necessary for proper
CC       development. Vital for embryonic development.
CC   -!- SUBCELLULAR LOCATION: Cell junction, septate junction.
CC       Note=Septate junction in the apical-lateral domain of epithelial
CC       cells during embryonic and imaginal disk development.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1; Synonyms=A;
CC         IsoId=Q9V8R9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9V8R9-2; Sequence=VSP_000476, VSP_000477, VSP_000479,
CC                                  VSP_000480, VSP_000481;
CC       Name=3; Synonyms=C;
CC         IsoId=Q9V8R9-3; Sequence=VSP_000475, VSP_000478, VSP_000479;
CC       Name=4; Synonyms=B;
CC         IsoId=Q9V8R9-4; Sequence=VSP_000476, VSP_000477, VSP_000479;
CC       Name=5;
CC         IsoId=Q9V8R9-5; Sequence=VSP_000474, VSP_000478;
CC         Note=No experimental confirmation available;
CC       Name=6; Synonyms=D;
CC         IsoId=Q9V8R9-6; Sequence=VSP_000478;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: At onset of germ band retraction, expression
CC       is seen in epidermis, hindgut and foregut. During retraction,
CC       expression extends to tracheal branches and salivary glands.
CC   -!- DEVELOPMENTAL STAGE: Expressed weakly in 4-8 hours embryos, more
CC       abundant expression in 8-12 hours and remains throughout later
CC       embryonic and larval stages.
CC   -!- SIMILARITY: Contains 1 FERM domain.
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DR   EMBL; L27467; AAB59187.1; -; mRNA.
DR   EMBL; L27468; AAA28742.1; -; mRNA.
DR   EMBL; L27469; AAA28743.1; -; mRNA.
DR   EMBL; AE013599; AAF57591.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAF57592.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAF57593.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAM70846.1; -; Genomic_DNA.
DR   EMBL; AY070992; AAL48614.1; -; mRNA.
DR   EMBL; BT024976; ABE01206.1; -; mRNA.
DR   PIR; T13800; T13800.
DR   RefSeq; NP_523791.2; NM_079067.3. [Q9V8R9-1]
DR   RefSeq; NP_725864.1; NM_166336.1. [Q9V8R9-3]
DR   RefSeq; NP_725865.1; NM_166337.1. [Q9V8R9-4]
DR   RefSeq; NP_725866.1; NM_166338.2. [Q9V8R9-6]
DR   UniGene; Dm.4694; -.
DR   ProteinModelPortal; Q9V8R9; -.
DR   SMR; Q9V8R9; 30-313.
DR   BioGrid; 62870; 7.
DR   DIP; DIP-20283N; -.
DR   IntAct; Q9V8R9; 2.
DR   MINT; MINT-1330152; -.
DR   PaxDb; Q9V8R9; -.
DR   PRIDE; Q9V8R9; -.
DR   EnsemblMetazoa; FBtr0086509; FBpp0085697; FBgn0010434. [Q9V8R9-1]
DR   GeneID; 37205; -.
DR   KEGG; dme:Dmel_CG11949; -.
DR   UCSC; CG11949-RA; d. melanogaster. [Q9V8R9-1]
DR   CTD; 37205; -.
DR   FlyBase; FBgn0010434; cora.
DR   eggNOG; NOG242913; -.
DR   GeneTree; ENSGT00750000117241; -.
DR   InParanoid; Q9V8R9; -.
DR   KO; K06107; -.
DR   OMA; VITIYGY; -.
DR   OrthoDB; EOG7Z69BP; -.
DR   PhylomeDB; Q9V8R9; -.
DR   ChiTaRS; cora; drosophila.
DR   GenomeRNAi; 37205; -.
DR   NextBio; 802505; -.
DR   Bgee; Q9V8R9; -.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR   GO; GO:0005918; C:septate junction; IDA:UniProtKB.
DR   GO; GO:0005920; C:smooth septate junction; IDA:FlyBase.
DR   GO; GO:0008092; F:cytoskeletal protein binding; ISS:FlyBase.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0007527; P:adult somatic muscle development; IMP:FlyBase.
DR   GO; GO:0061343; P:cell adhesion involved in heart morphogenesis; IMP:FlyBase.
DR   GO; GO:0045216; P:cell-cell junction organization; TAS:FlyBase.
DR   GO; GO:0008362; P:chitin-based embryonic cuticle biosynthetic process; TAS:FlyBase.
DR   GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR   GO; GO:0009790; P:embryo development; IMP:UniProtKB.
DR   GO; GO:0060857; P:establishment of glial blood-brain barrier; IMP:FlyBase.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; NAS:FlyBase.
DR   GO; GO:0003015; P:heart process; IMP:FlyBase.
DR   GO; GO:0035321; P:maintenance of imaginal disc-derived wing hair orientation; IMP:FlyBase.
DR   GO; GO:0006612; P:protein targeting to membrane; TAS:FlyBase.
DR   GO; GO:0035151; P:regulation of tube size, open tracheal system; IMP:FlyBase.
DR   GO; GO:0007435; P:salivary gland morphogenesis; TAS:FlyBase.
DR   GO; GO:0019991; P:septate junction assembly; TAS:FlyBase.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR008379; Band_4.1_C.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR014847; FERM-adjacent.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH_like_dom.
DR   InterPro; IPR029071; Ubiquitin-rel_dom.
DR   Pfam; PF05902; 4_1_CTD; 1.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   PRINTS; PR00935; BAND41.
DR   SMART; SM00295; B41; 1.
DR   SUPFAM; SSF47031; SSF47031; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Complete proteome;
KW   Developmental protein; Phosphoprotein; Reference proteome.
FT   CHAIN         1   1698       Protein 4.1 homolog.
FT                                /FTId=PRO_0000219394.
FT   DOMAIN       32    314       FERM.
FT   REGION      317    434       Hydrophilic.
FT   REGION     1286   1698       C-terminal (CTD).
FT   COMPBIAS    404    449       Lys-rich.
FT   COMPBIAS    731    775       Ala-rich.
FT   COMPBIAS   1437   1643       Thr-rich.
FT   MOD_RES     471    471       Phosphoserine.
FT   MOD_RES     474    474       Phosphoserine.
FT   MOD_RES     478    478       Phosphoserine.
FT   MOD_RES     566    566       Phosphoserine.
FT   MOD_RES     659    659       Phosphoserine.
FT   MOD_RES     687    687       Phosphoserine.
FT   MOD_RES     689    689       Phosphothreonine.
FT   MOD_RES     697    697       Phosphoserine.
FT   MOD_RES    1398   1398       Phosphoserine.
FT   MOD_RES    1401   1401       Phosphoserine.
FT   MOD_RES    1402   1402       Phosphoserine.
FT   MOD_RES    1407   1407       Phosphothreonine.
FT   MOD_RES    1590   1590       Phosphoserine.
FT   VAR_SEQ       1    312       Missing (in isoform 5).
FT                                /FTId=VSP_000474.
FT   VAR_SEQ     409    409       K -> KSSTGTASASSQSSLEGDYETNLEIEAIEAEPPVQ
FT                                (in isoform 2 and isoform 4).
FT                                /FTId=VSP_000476.
FT   VAR_SEQ     409    409       K -> KLMRQSSTGTASASSQSSLEGDYETNLEIEAIEAEP
FT                                PVQ (in isoform 3).
FT                                /FTId=VSP_000475.
FT   VAR_SEQ     482   1480       Missing (in isoform 3, isoform 5 and
FT                                isoform 6).
FT                                /FTId=VSP_000478.
FT   VAR_SEQ     482   1290       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_000477.
FT   VAR_SEQ    1554   1587       Missing (in isoform 2, isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_000479.
FT   VAR_SEQ    1629   1635       VSSKTRT -> GGGGGGI (in isoform 2).
FT                                /FTId=VSP_000480.
FT   VAR_SEQ    1636   1698       Missing (in isoform 2).
FT                                /FTId=VSP_000481.
FT   CONFLICT    970    970       I -> V (in Ref. 1; AAB59187).
SQ   SEQUENCE   1698 AA;  184168 MW;  93940FC4F1ACEB83 CRC64;
     MPAEIKPSAP AEPETPTKSK PKSSSSSHGK PALARVTLLD GSLLDVSIDR KAIGRDVINS
     ICAGLNLIEK DYFGLTYETP TDPRTWLDLE KPVSKFFRTD TWPLTFAVKF YPPEPSQLKE
     DITRYHLCLQ VRNDILEGRL PCTFVTHALL GSYLVQSEMG DYDAEEMPTR AYLKDFKIAP
     NQTAELEDKV MDLHKTHKGQ SPAEAELHYL ENAKKLAMYG VDLHPAKDSE GVDIMLGVCA
     SGLLVYRDKL RINRFAWPKI LKISYKRHHF YIKIRPGEFE QYESTIGFKL ANHRAAKKLW
     KSCVEHHTFF RLMTPEPVSK SKMFPVFGST YRYKGRTQAE STNTPVDRTP PKFNRTLSGA
     RLTSRSMDAL ALAEKEKVAR KSSTLDHRGD RNADGDAHSR SPIKNKKEKD ADKEAKLREK
     KQKEKEEKER KEREKRELEE KKKAEKAAKA ALAAGAAAGA AVNGNDELND SNKSDKSSGR
     RGVGIFSSGR KSKSGSPSKD GKDKSGKDKD KEVGRLGLVV TSGLGDNQQD QNLDEAARNA
     AKNRGSTTPG VTRQYEYAVD NDGNTSPTRK SYTPGGFRYD QDPNSRKSGA DGQEQLSPTS
     QQKKIGLAFN YAPGNENALK ETAEKLKAGQ LSPRTQDKLN RGQLSPKSRA KLLQDPLLSP
     TTRAKLQGSA VDAAAVPLSD SQKRSYSPTK GPQGYSSGAP GSYKPISDPT ADFLESQRYN
     KEPGYVGPSK ADVAAGLAGA AGSKKPGSPT KTGKGAPGAA AAAAAGAAGA AAAAAKPKKR
     RVKIMVITSK FDPSTKRIDA ENGSIEHSTG ILDPATGLID TKYGVIDPKK GTLEALNTKT
     GKKEVFQGDV DGKTGNLHLV SGVADPKTGR LDDTLGQIVC ITPQDNPVVE LTVITSRIDP
     ATGKIDTVNG DVERSLGVLN LDTGLLDTKY GEINTRTGEL KAIDPKSGKI VVSKNVKVDP
     GTGQITILGI VDPKTNKIDP NQGRLIEVGQ QIDPIVEVTS LAGKFDSKRN IIDPKTAQVE
     TSGGQFDPKA GKIDTKYGQI DLVKHTITFN DPKSGKTVTR DIKIEPTTGQ IVLKNQVNPK
     NNKPDKDYAR IISLRIVQQR VDPATKAPIT EVSASKDKDI VVDPKSNQIW VPTGATDPAT
     KEQQYISSSV DPKTGYVITI YGYLDPKTNE IKKQTKLDPN TIKIEPTSGK IYTATGEVDQ
     ATGEPLYAAT QVDPESGEVY TKLARVDPKT GKIVIVRILL ISKTDERGRP EEIDPSTCEI
     DPVSGRVLKF FNKTVYVYNM IDPVTGEIVQ VDPNDPRFAG ARTTVTHTMT LTGEIDPVTG
     RIKSEYGDID PNTGDIDPAT AVTDPVTGKL ILNYAQIDPS HFGKQAQVQT TTETVPITRQ
     QFFDGVKHIS KGALRRDSEG SSDDDMTAQY GADQVNEILI GSPAGQAGGK LGKPVSTPTV
     VKTTTKQVLT KNIDGVTHNV EEEVRNLGTG EVTYSTQEHK ADATPTDLSG AYVTATAVTT
     RTATTHEDLG KNAKTEQLEE KTVATTRTHD PNKQQQRVVT QEVKTTATVT SGDQYQRRDS
     VSSTSSGDSG TPIDGPYDGA SVVRTDNQKS PLFTTSATTG PHVESTRVVL GEDTPGFSGH
     GEIISTQTVS SKTRTVETIT YKTERDGIVE TRVEQKITIQ SDGDPIDHDK ALAEAIQEAT
     AMNPDMTVEK IEIQQQTQ
//
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