CO4A1_CAEEL
ID CO4A1_CAEEL Reviewed; 1759 AA.
AC P17139; Q6LAD0;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 5.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Collagen alpha-1(IV) chain;
DE Flags: Precursor;
GN Name=emb-9 {ECO:0000312|WormBase:K04H4.1a};
GN Synonyms=clb-2 {ECO:0000312|WormBase:K04H4.1a};
GN ORFNames=K04H4.1 {ECO:0000312|WormBase:K04H4.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A), AND MUTAGENESIS OF GLY-403
RP AND GLY-409.
RC STRAIN=Bristol N2;
RX PubMed=1996137; DOI=10.1038/349707a0;
RA Guo X., Johnson J.J., Kramer J.M.;
RT "Embryonic lethality caused by mutations in basement membrane collagen of
RT C. elegans.";
RL Nature 349:707-709(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1447-1759 (ISOFORMS A/B).
RC STRAIN=Bristol N2;
RX PubMed=2793871; DOI=10.1016/s0021-9258(18)71530-5;
RA Guo X., Kramer J.M.;
RT "The two Caenorhabditis elegans basement membrane (type IV) collagen genes
RT are located on separate chromosomes.";
RL J. Biol. Chem. 264:17574-17582(1989).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF GLY-213 AND GLY-258.
RX PubMed=25080592; DOI=10.1523/jneurosci.5128-13.2014;
RA Qin J., Liang J., Ding M.;
RT "Perlecan antagonizes collagen IV and ADAMTS9/GON-1 in restricting the
RT growth of presynaptic boutons.";
RL J. Neurosci. 34:10311-10324(2014).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27984580; DOI=10.1371/journal.pgen.1006475;
RA Hisamoto N., Nagamori Y., Shimizu T., Pastuhov S.I., Matsumoto K.;
RT "The C. elegans discoidin domain receptor DDR-2 modulates the Met-like RTK-
RT JNK signaling pathway in axon regeneration.";
RL PLoS Genet. 12:E1006475-E1006475(2016).
RN [7]
RP MUTAGENESIS OF PRO-141 AND GLY-213.
RX PubMed=29440357; DOI=10.1534/genetics.118.300731;
RA Gotenstein J.R., Koo C.C., Ho T.W., Chisholm A.D.;
RT "Genetic Suppression of Basement Membrane Defects in Caenorhabditis elegans
RT by Gain of Function in Extracellular Matrix and Cell-Matrix Attachment
RT Genes.";
RL Genetics 208:1499-1512(2018).
CC -!- FUNCTION: Collagen type IV is specific for basement membranes
CC (Probable). Required to restrict presynaptic growth at the
CC neuromuscular junctions (NMJ) in late larval stage and in adult motor
CC neurons (PubMed:25080592). May play a role in axon regeneration in
CC embryos following injury in D-type motor neurons (PubMed:27984580).
CC {ECO:0000269|PubMed:25080592, ECO:0000269|PubMed:27984580,
CC ECO:0000305}.
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 -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=P17139-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P17139-2; Sequence=VSP_011573;
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 -!- PTM: The trimeric structure of the NC1 domains is stabilized by
CC covalent bonds between Lys and Met residues. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: At 20 degrees Celsius, there is reduced axon
CC regeneration following injury in D-type motor neurons in temperature-
CC sensitive mutant embryos. {ECO:0000269|PubMed:27984580}.
CC -!- SIMILARITY: Belongs to the type IV collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00736}.
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DR EMBL; X56979; CAA40299.1; -; Genomic_DNA.
DR EMBL; BX284603; CAA81584.5; -; Genomic_DNA.
DR EMBL; BX284603; CAE52901.2; -; Genomic_DNA.
DR EMBL; J05067; AAB59179.1; -; Genomic_DNA.
DR PIR; S40991; S40991.
DR RefSeq; NP_001022662.2; NM_001027491.4. [P17139-1]
DR RefSeq; NP_001022663.1; NM_001027492.4. [P17139-2]
DR AlphaFoldDB; P17139; -.
DR SMR; P17139; -.
DR BioGRID; 41512; 6.
DR IntAct; P17139; 7.
DR STRING; 6239.K04H4.1a; -.
DR EPD; P17139; -.
DR PaxDb; P17139; -.
DR PeptideAtlas; P17139; -.
DR EnsemblMetazoa; K04H4.1a.1; K04H4.1a.1; WBGene00001263. [P17139-1]
DR EnsemblMetazoa; K04H4.1b.1; K04H4.1b.1; WBGene00001263. [P17139-2]
DR GeneID; 176314; -.
DR KEGG; cel:CELE_K04H4.1; -.
DR UCSC; K04H4.1b; c. elegans. [P17139-1]
DR CTD; 176314; -.
DR WormBase; K04H4.1a; CE48054; WBGene00001263; emb-9. [P17139-1]
DR WormBase; K04H4.1b; CE36390; WBGene00001263; emb-9. [P17139-2]
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000153991; -.
DR InParanoid; P17139; -.
DR OMA; SCLMRFT; -.
DR OrthoDB; 63831at2759; -.
DR PhylomeDB; P17139; -.
DR Reactome; R-CEL-1442490; Collagen degradation.
DR Reactome; R-CEL-1474244; Extracellular matrix organization.
DR Reactome; R-CEL-186797; Signaling by PDGF.
DR Reactome; R-CEL-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-CEL-216083; Integrin cell surface interactions.
DR Reactome; R-CEL-2243919; Crosslinking of collagen fibrils.
DR Reactome; R-CEL-3000157; Laminin interactions.
DR Reactome; R-CEL-419037; NCAM1 interactions.
DR SignaLink; P17139; -.
DR PRO; PR:P17139; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001263; Expressed in larva and 4 other tissues.
DR GO; GO:0005604; C:basement membrane; IDA:WormBase.
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; IBA:GO_Central.
DR GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:WormBase.
DR GO; GO:0007517; P:muscle organ development; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0048680; P:positive regulation of axon regeneration; IMP:UniProtKB.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:WormBase.
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 Alternative splicing; Basement membrane; Collagen; Disulfide bond;
KW Extracellular matrix; Hydroxylation; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..?194
FT /note="N-terminal propeptide (7S domain)"
FT /id="PRO_0000005752"
FT CHAIN ?195..1759
FT /note="Collagen alpha-1(IV) chain"
FT /id="PRO_0000005753"
FT DOMAIN 1535..1759
FT /note="Collagen IV NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT REGION 51..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..1530
FT /note="Triple-helical region"
FT REGION 269..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..1522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1550..1641
FT /note="Or C-1550 with C-1638"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1583..1638
FT /note="Or C-1583 with C-1641"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1595..1601
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1660..1755
FT /note="Or C-1660 with C-1752"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1694..1752
FT /note="Or C-1694 with C-1755"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1706..1712
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT CROSSLNK 1623
FT /note="S-Lysyl-methionine sulfilimine (Met-Lys) (interchain
FT with K-1741)"
FT /evidence="ECO:0000250"
FT CROSSLNK 1741
FT /note="S-Lysyl-methionine sulfilimine (Lys-Met) (interchain
FT with M-1623)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 502..758
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_011573"
FT MUTAGEN 141
FT /note="P->L: In ju1197; suppresses the lethal phenotypes of
FT the pxn-2 tm3464 mutant."
FT /evidence="ECO:0000269|PubMed:29440357"
FT MUTAGEN 213
FT /note="G->E: In b189; temperature-sensitive mutant. At the
FT subrestrictive temperature of 22 degrees Celsius, causes
FT the formation of ectopic presynaptic boutons on the ventral
FT cord axons. Enhances the lethality of the pxn-2 ju436
FT mutant at 20 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:25080592,
FT ECO:0000269|PubMed:29440357"
FT MUTAGEN 258
FT /note="G->E: In xd51; formation of ectopic presynaptic
FT boutons on the ventral cord axons associated with a
FT disruption of synapse basement membrane."
FT /evidence="ECO:0000269|PubMed:25080592"
FT MUTAGEN 403
FT /note="G->E: In allele g34; temperature-sensitive lethality
FT during late embryogenesis."
FT /evidence="ECO:0000269|PubMed:1996137"
FT MUTAGEN 409
FT /note="G->E: In allele g23/hc70; temperature-sensitive
FT lethality during late embryogenesis."
FT /evidence="ECO:0000269|PubMed:1996137"
FT CONFLICT 302..305
FT /note="AGQR -> LDN (in Ref. 1; CAA40299)"
FT /evidence="ECO:0000305"
FT CONFLICT 769
FT /note="R -> P (in Ref. 1; CAA40299)"
FT /evidence="ECO:0000305"
FT CONFLICT 831
FT /note="V -> D (in Ref. 1; CAA40299)"
FT /evidence="ECO:0000305"
FT CONFLICT 1515
FT /note="P -> Q (in Ref. 4; AAB59179)"
FT /evidence="ECO:0000305"
FT CONFLICT 1723
FT /note="L -> P (in Ref. 1; CAA40299 and 4; AAB59179)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1759 AA; 170987 MW; 28BB24660E91BB7F CRC64;
MSRLSLLGLT AAVVLLSSFC QDRIHVDAAA ACKGCAPPCV CPGTKGERGN PGFGGEPGHP
GAPGQDGPEG APGAPGMFGA EGDFGDMGSK GARGDRGLPG SPGHPGLQGL DGLPGLKGEE
GIPGCNGTDG FPGMPGLAGP PGQSGQNGNP GRPGLSGPPG EGGVNSQGRK GVKGESGRSG
VPGLPGNSGY PGLKGAKGDP GPYGLPGFPG VSGLKGRMGV RTSGVKGEKG LPGPPGPPGQ
PGSYPWASKP IEMEVLQGPV GPAGVKGEKG RDGPVGPPGM LGLDGPPGYP GLKGQKGDLG
DAGQRGKRGK DGVPGNYGEK GSQGEQGLGG TPGYPGTKGG AGEPGYPGRP GFEGDCGPEG
PLGEGTGEAG PHGAQGFDGV QGGKGLPGHD GLPGPVGPRG PVGAPGAPGQ PGIDGMPGYT
EKGDRGEDGY PGFAGEPGLP GEPGDCGYPG EDGLPGYDIQ GPPGLDGQSG RDGFPGIPGD
IGDPGYSGEK GFPGTGVNKV GPPGMTGLPG EPGMPGRIGV DGYPGPPGNN GERGEDCGYC
PDGVPGNAGD PGFPGMNGYP GPPGPNGDHG DCGMPGAPGK PGSAGSDGLS GSPGLPGIPG
YPGMKGEAGE IVGPMENPAG IPGLKGDHGL PGLPGRPGSD GLPGYPGGPG QNGFPGLQGE
PGLAGIDGKR GRQGSLGIPG LQGPPGDSFP GQPGTPGYKG ERGADGLPGL PGAQGPRGIP
APLRIVNQVA GQPGVDGMPG LPGDRGADGL PGLPGPVGPD GYPGTPGERG MDGLPGFPGL
HGEPGMRGQQ GEVGFNGIDG DCGEPGLDGY PGAPGAPGAP GETGFGFPGQ VGYPGPNGDA
GAAGLPGPDG YPGRDGLPGT PGYPGEAGMN GQDGAPGQPG SRGESGLVGI DGKKGRDGTP
GTRGQDGGPG YSGEAGAPGQ NGMDGYPGAP GDQGYPGSPG QDGYPGPSGI PGEDGLVGFP
GLRGEHGDNG LPGLEGECGE EGSRGLDGVP GYPGEHGTDG LPGLPGADGQ PGFVGEAGEP
GTPGYRGQPG EPGNLAYPGQ PGDVGYPGPD GPPGLPGQDG LPGLNGERGD NGDSYPGNPG
LSGQPGDAGY DGLDGVPGPP GYPGITGMPG LKGESGLPGL PGRQGNDGIP GQPGLEGECG
EDGFPGSPGQ PGYPGQQGRE GEKGYPGIPG ENGLPGLRGQ DGQPGLKGEN GLDGQPGYPG
SAGQLGTPGD VGYPGAPGEN GDNGNQGRDG QPGLRGESGQ PGQPGLPGRD GQPGPVGPPG
DDGYPGAPGQ DIYGPPGQAG QDGYPGLDGL PGAPGLNGEP GSPGQYGMPG LPGGPGESGL
PGYPGERGLP GLDGKRGHDG LPGAPGVPGV EGVPGLEGDC GEDGYPGAPG APGSNGYPGE
RGLPGVPGQQ GRSGDNGYPG APGQPGIKGP RGDDGFPGRD GLDGLPGRPG REGLPGPMAM
AVRNPPGQPG ENGYPGEKGY PGLPGDNGLS GPPGKAGYPG APGTDGYPGP PGLSGMPGHG
GDQGFQGAAG RTGNPGLPGT PGYPGSPGGW APSRGFTFAK HSQTTAVPQC PPGASQLWEG
YSLLYVQGNG RASGQDLGQP GSCLSKFNTM PFMFCNMNSV CHVSSRNDYS FWLSTDEPMT
PMMNPVTGTA IRPYISRCAV CEVPTQIIAV HSQDTSVPQC PQGWSGMWTG YSFVMHTAAG
AEGTGQSLQS PGSCLEEFRA VPFIECHGRG TCNYYATNHG FWLSIVDQDK QFRKPMSQTL
KAGGLKDRVS RCQVCLKNR
