CO4A1_DROME
ID CO4A1_DROME Reviewed; 1779 AA.
AC P08120; A4V070; Q9VMV4;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Collagen alpha-1(IV) chain {ECO:0000303|PubMed:3142875};
DE AltName: Full=Collagen type IV alpha 1 {ECO:0000312|FlyBase:FBgn0000299};
DE Flags: Precursor;
GN Name=Col4a1 {ECO:0000312|FlyBase:FBgn0000299};
GN Synonyms=Cg25C {ECO:0000312|FlyBase:FBgn0000299},
GN DCg1 {ECO:0000303|PubMed:6210912};
GN ORFNames=CG4145 {ECO:0000312|FlyBase:FBgn0000299};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Oregon-R;
RX PubMed=3142875; DOI=10.1016/s0021-9258(19)81363-7;
RA Blumberg B., Mackrell A.J., Fessler J.H.;
RT "Drosophila basement membrane procollagen alpha 1(IV). II. Complete cDNA
RT sequence, genomic structure, and general implications for supramolecular
RT assemblies.";
RL J. Biol. Chem. 263:18328-18337(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Blumberg B.;
RL Thesis (1987), University of California Los Angeles, United States.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Mackrell A.J.;
RL Thesis (1992), University of California Los Angeles, United States.
RN [4]
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., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., 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., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., 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., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
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., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 762-1230.
RX PubMed=6210912; DOI=10.1073/pnas.79.6.1761;
RA Monson J.M., Natzle J.E., Friedman J., McCarthy B.J.;
RT "Expression and novel structure of a collagen gene in Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:1761-1765(1982).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1065-1779.
RX PubMed=3106346; DOI=10.1016/s0021-9258(18)45519-6;
RA Blumberg B., Mackrell A.J., Olson P.F., Kurkinen M., Monson J.M.,
RA Natzle J.E., Fessler J.H.;
RT "Basement membrane procollagen IV and its specialized carboxyl domain are
RT conserved in Drosophila, mouse, and human.";
RL J. Biol. Chem. 262:5947-5950(1987).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1356-1779.
RC TISSUE=Larva;
RX PubMed=3109906; DOI=10.1111/j.1432-1033.1987.tb11480.x;
RA Cecchini J.-P., Knibiehler B., Mirre C., le Parco Y.;
RT "Evidence for a type-IV-related collagen in Drosophila melanogaster.
RT Evolutionary constancy of the carboxyl-terminal noncollagenous domain.";
RL Eur. J. Biochem. 165:587-593(1987).
CC -!- FUNCTION: Collagen type IV is specific for basement membranes.
CC -!- SUBUNIT: Trimers of two alpha 1(IV) and one alpha 2(IV) chain. Type IV
CC collagen forms a mesh-like network linked through intermolecular
CC interactions between 7S domains and between NC1 domains.
CC -!- INTERACTION:
CC P08120; P07713: dpp; NbExp=3; IntAct=EBI-109669, EBI-499422;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane.
CC -!- DOMAIN: Alpha chains of type IV collagen have a non-collagenous domain
CC (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats
CC in the long central triple-helical domain (which may cause flexibility
CC in the triple helix), and a short N-terminal triple-helical 7S domain.
CC -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) are hydroxylated in some or all of the chains.
CC -!- PTM: Type IV collagens contain numerous cysteine residues which are
CC involved in inter- and intramolecular disulfide bonding. 12 of these,
CC located in the NC1 domain, are conserved in all known type IV
CC collagens.
CC -!- SIMILARITY: Belongs to the type IV collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00736}.
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DR EMBL; J02727; AAA28423.1; -; mRNA.
DR EMBL; M23704; AAA28404.1; -; mRNA.
DR EMBL; M96575; AAB59184.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF52204.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10519.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10520.1; -; Genomic_DNA.
DR EMBL; V00200; CAA23486.2; -; Genomic_DNA.
DR EMBL; M28334; AAA28422.1; -; mRNA.
DR PIR; A31893; A31893.
DR RefSeq; NP_723044.1; NM_164615.2.
DR RefSeq; NP_723045.1; NM_164616.2.
DR RefSeq; NP_723046.1; NM_164617.2.
DR AlphaFoldDB; P08120; -.
DR SMR; P08120; -.
DR BioGRID; 59908; 13.
DR DIP; DIP-59819N; -.
DR IntAct; P08120; 10.
DR STRING; 7227.FBpp0078641; -.
DR GlyGen; P08120; 1 site.
DR PaxDb; P08120; -.
DR PRIDE; P08120; -.
DR EnsemblMetazoa; FBtr0079001; FBpp0078640; FBgn0000299.
DR EnsemblMetazoa; FBtr0079002; FBpp0078641; FBgn0000299.
DR EnsemblMetazoa; FBtr0079003; FBpp0078642; FBgn0000299.
DR GeneID; 33727; -.
DR KEGG; dme:Dmel_CG4145; -.
DR CTD; 1282; -.
DR FlyBase; FBgn0000299; Col4a1.
DR VEuPathDB; VectorBase:FBgn0000299; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000164160; -.
DR HOGENOM; CLU_002023_1_0_1; -.
DR InParanoid; P08120; -.
DR OMA; NICNYAS; -.
DR OrthoDB; 63831at2759; -.
DR PhylomeDB; P08120; -.
DR Reactome; R-DME-1442490; Collagen degradation.
DR Reactome; R-DME-1474244; Extracellular matrix organization.
DR Reactome; R-DME-186797; Signaling by PDGF.
DR Reactome; R-DME-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-DME-216083; Integrin cell surface interactions.
DR Reactome; R-DME-2243919; Crosslinking of collagen fibrils.
DR Reactome; R-DME-3000157; Laminin interactions.
DR Reactome; R-DME-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-DME-419037; NCAM1 interactions.
DR SignaLink; P08120; -.
DR BioGRID-ORCS; 33727; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Cg25C; fly.
DR GenomeRNAi; 33727; -.
DR PRO; PR:P08120; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000299; Expressed in arthropod fat body and 18 other tissues.
DR ExpressionAtlas; P08120; baseline and differential.
DR Genevisible; P08120; DM.
DR GO; GO:0005604; C:basement membrane; IDA:FlyBase.
DR GO; GO:0005587; C:collagen type IV trimer; IBA:GO_Central.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IMP:FlyBase.
DR GO; GO:0071711; P:basement membrane organization; IMP:FlyBase.
DR GO; GO:0055013; P:cardiac muscle cell development; IMP:FlyBase.
DR GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007391; P:dorsal closure; TAS:FlyBase.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0060729; P:intestinal epithelial structure maintenance; IMP:FlyBase.
DR GO; GO:0035848; P:oviduct morphogenesis; IMP:FlyBase.
DR GO; GO:0048621; P:post-embryonic digestive tract morphogenesis; IMP:FlyBase.
DR Gene3D; 2.170.240.10; -; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR001442; Collagen_IV_NC.
DR InterPro; IPR036954; Collagen_IV_NC_sf.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF01413; C4; 2.
DR Pfam; PF01391; Collagen; 15.
DR SMART; SM00111; C4; 2.
DR SUPFAM; SSF56436; SSF56436; 2.
DR PROSITE; PS51403; NC1_IV; 1.
PE 1: Evidence at protein level;
KW Basement membrane; Collagen; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Hydroxylation; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT PROPEP 24..?
FT /note="N-terminal propeptide (7S domain)"
FT /id="PRO_0000005754"
FT CHAIN ?..1779
FT /note="Collagen alpha-1(IV) chain"
FT /id="PRO_0000005755"
FT DOMAIN 1555..1778
FT /note="Collagen IV NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT REGION 89..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1200..1285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1336..1530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION ?..1545
FT /note="Triple-helical region"
FT COMPBIAS 198..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..410
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1456..1471
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 1570..1659
FT /note="Or C-1570 with C-1656"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1603..1656
FT /note="Or C-1603 with C-1659"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1615..1621
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1678..1774
FT /note="Or C-1678 with C-1771"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1712..1771
FT /note="Or C-1712 with C-1774"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1724..1731
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT CONFLICT 383
FT /note="K -> E (in Ref. 1; AAA28404/AAA28423 and 2;
FT AAB59184)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="G -> D (in Ref. 1; AAA28404/AAA28423 and 2;
FT AAB59184)"
FT /evidence="ECO:0000305"
FT CONFLICT 948
FT /note="L -> S (in Ref. 6; CAA23486)"
FT /evidence="ECO:0000305"
FT CONFLICT 997
FT /note="T -> S (in Ref. 1; AAA28404/AAA28423 and 2;
FT AAB59184)"
FT /evidence="ECO:0000305"
FT CONFLICT 1329..1333
FT /note="AGEPG -> PESR (in Ref. 1; AAA28404/AAA28423 and 2;
FT AAB59184)"
FT /evidence="ECO:0000305"
FT CONFLICT 1358
FT /note="Q -> K (in Ref. 8; AAA28422)"
FT /evidence="ECO:0000305"
FT CONFLICT 1361
FT /note="Q -> K (in Ref. 8; AAA28422)"
FT /evidence="ECO:0000305"
FT CONFLICT 1374
FT /note="T -> I (in Ref. 8; AAA28422)"
FT /evidence="ECO:0000305"
FT CONFLICT 1424
FT /note="N -> T (in Ref. 8; AAA28422)"
FT /evidence="ECO:0000305"
FT CONFLICT 1497
FT /note="R -> L (in Ref. 1; AAA28404/AAA28423 and 2;
FT AAB59184)"
FT /evidence="ECO:0000305"
FT CONFLICT 1508..1512
FT /note="ETGNV -> RAGQR (in Ref. 8; AAA28422)"
FT /evidence="ECO:0000305"
FT CONFLICT 1530
FT /note="E -> K (in Ref. 8; AAA28422)"
FT /evidence="ECO:0000305"
FT CONFLICT 1600..1602
FT /note="Missing (in Ref. 1; AAA28404/AAA28423, 2; AAB59184
FT and 8; AAA28422)"
FT /evidence="ECO:0000305"
FT CONFLICT 1737
FT /note="M -> I (in Ref. 8; AAA28422)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1779 AA; 174300 MW; 6770F18AE40A313E CRC64;
MLPFWKRLLY AAVIAGALVG ADAQFWKTAG TAGSIQDSVK HYNRNEPKFP IDDSYDIVDS
AGVARGDLPP KNCTAGYAGC VPKCIAEKGN RGLPGPLGPT GLKGEMGFPG MEGPSGDKGQ
KGDPGPYGQR GDKGERGSPG LHGQAGVPGV QGPAGNPGAP GINGKDGCDG QDGIPGLEGL
SGMPGPRGYA GQLGSKGEKG EPAKENGDYA KGEKGEPGWR GTAGLAGPQG FPGEKGERGD
SGPYGAKGPR GEHGLKGEKG ASCYGPMKPG APGIKGEKGE PASSFPVKPT HTVMGPRGDM
GQKGEPGLVG RKGEPGPEGD TGLDGQKGEK GLPGGPGDRG RQGNFGPPGS TGQKGDRGEP
GLNGLPGNPG QKGEPGRAGA TGKPGLLGPP GPPGGGRGTP GPPGPKGPRG YVGAPGPQGL
NGVDGLPGPQ GYNGQKGGAG LPGRPGNEGP PGKKGEKGTA GLNGPKGSIG PIGHPGPPGP
EGQKGDAGLP GYGIQGSKGD AGIPGYPGLK GSKGERGFKG NAGAPGDSKL GRPGTPGAAG
APGQKGDAGR PGTPGQKGDM GIKGDVGGKC SSCRAGPKGD KGTSGLPGIP GKDGARGPPG
ERGYPGERGH DGINGQTGPP GEKGEDGRTG LPGATGEPGK PALCDLSLIE PLKGDKGYPG
APGAKGVQGF KGAEGLPGIP GPKGEFGFKG EKGLSGAPGN DGTPGRAGRD GYPGIPGQSI
KGEPGFHGRD GAKGDKGSFG RSGEKGEPGS CALDEIKMPA KGNKGEPGQT GMPGPPGEDG
SPGERGYTGL KGNTGPQGPP GVEGPRGLNG PRGEKGNQGA VGVPGNPGKD GLRGIPGRNG
QPGPRGEPGI SRPGPMGPPG LNGLQGEKGD RGPTGPIGFP GADGSVGYPG DRGDAGLPGV
SGRPGIVGEK GDVGPIGPAG VAGPPGVPGI DGVRGRDGAK GEPGSPGLVG MPGNKGDRGA
PGNDGPKGFA GVTGAPGKRG PAGIPGVSGA KGDKGATGLT GNDGPVGGRG PPGAPGLMGI
KGDQGLAGAP GQQGLDGMPG EKGNQGFPGL DGPPGLPGDA SEKGQKGEPG PSGLRGDTGP
AGTPGWPGEK GLPGLAVHGR AGPPGEKGDQ GRSGIDGRDG INGEKGEQGL QGVWGQPGEK
GSVGAPGIPG APGMDGLPGA AGAPGAVGYP GDRGDKGEPG LSGLPGLKGE TGPVGLQGFT
GAPGPKGERG IRGQPGLPAT VPDIRGDKGS QGERGYTGEK GEQGERGLTG PAGVAGAKGD
RGLQGPPGAS GLNGIPGAKG DIGPRGEIGY PGVTIKGEKG LPGRPGRNGR QGLIGAPGLI
GERGLPGLAG EPGLVGLPGP IGPAGSKGER GLAGSPGQPG QDGFPGAPGL KGDTGPQGFK
GERGLNGFEG QKGDKGDRGL QGPSGLPGLV GQKGDTGYPG LNGNDGPVGA PGERGFTGPK
GRDGRDGTPG LPGQKGEPGM LPPPGPKGEP GQPGRNGPKG EPGRPGERGL IGIQGERGEK
GERGLIGETG NVGRPGPKGD RGEPGERGYE GAIGLIGQKG EPGAPAPAAL DYLTGILITR
HSQSETVPAC SAGHTELWTG YSLLYVDGND YAHNQDLGSP GSCVPRFSTL PVLSCGQNNV
CNYASRNDKT FWLTTNAAIP MMPVENIEIR QYISRCVVCE APANVIAVHS QTIEVPDCPN
GWEGLWIGYS FLMHTAVGNG GGGQALQSPG SCLEDFRATP FIECNGAKGT CHFYETMTSF
WMYNLESSQP FERPQQQTIK AGERQSHVSR CQVCMKNSS
