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 01-MAY-2013, entry version 110.
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;
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;
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 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 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.
DR RefSeq; NP_725864.1; NM_166336.1.
DR RefSeq; NP_725865.1; NM_166337.1.
DR RefSeq; NP_725866.1; NM_166338.2.
DR UniGene; Dm.4694; -.
DR ProteinModelPortal; Q9V8R9; -.
DR SMR; Q9V8R9; 30-313.
DR DIP; DIP-20283N; -.
DR IntAct; Q9V8R9; 2.
DR MINT; MINT-1330152; -.
DR PaxDb; Q9V8R9; -.
DR PRIDE; Q9V8R9; -.
DR EnsemblMetazoa; FBtr0086509; FBpp0085697; FBgn0010434.
DR GeneID; 37205; -.
DR KEGG; dme:Dmel_CG11949; -.
DR UCSC; CG11949-RA; d. melanogaster.
DR CTD; 37205; -.
DR FlyBase; FBgn0010434; cora.
DR eggNOG; NOG242913; -.
DR GeneTree; ENSGT00700000104349; -.
DR InParanoid; Q9V8R9; -.
DR KO; K06107; -.
DR OMA; TGRIKSE; -.
DR OrthoDB; EOG466T2H; -.
DR PhylomeDB; Q9V8R9; -.
DR ChiTaRS; cora; drosophila.
DR GenomeRNAi; 37205; -.
DR NextBio; 802505; -.
DR Bgee; Q9V8R9; -.
DR GermOnline; CG11949; Drosophila melanogaster.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
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:0008362; P:chitin-based embryonic cuticle biosynthetic process; TAS:FlyBase.
DR GO; GO:0007391; P:dorsal closure; NAS:FlyBase.
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: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 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; FERM_3-hlx; 1.
DR PROSITE; PS00660; FERM_1; FALSE_NEG.
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
//
