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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND FUNCTION.
STRAIN=Bristol N2;
DOI=10.1083/jcb.123.1.255; PubMed=7691828 [NCBI, ExPASy, EBI, Israel, Japan]
Sibley M.H.,
Johnson J.J.,
Mello C.C.,
Kramer J.M.;
"Genetic identification, sequence, and alternative splicing of the Caenorhabditis elegans alpha 2(IV) collagen gene.";
J. Cell Biol. 123:255-264(1993).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
STRAIN=Bristol N2;
DOI=10.1126/science.282.5396.2012; PubMed=9851916 [NCBI, ExPASy, EBI, Israel, Japan]
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for investigating biology.";
Science 282:2012-2018(1998).
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[3]
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PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1495-1758.
STRAIN=Bristol N2;
PubMed=2793871 [NCBI, ExPASy, EBI, Israel, Japan]
Guo X.,
Kramer J.M.;
"The two Caenorhabditis elegans basement membrane (type IV) collagen genes are located on separate chromosomes.";
J. Biol. Chem. 264:17574-17582(1989).
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[4]
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MUTAGENESIS.
PubMed=8045258 [NCBI, ExPASy, EBI, Israel, Japan]
Sibley M.H.,
Graham P.L.,
von Mende N.,
Kramer J.M.;
"Mutations in the alpha 2(IV) basement membrane collagen gene of Caenorhabditis elegans produce phenotypes of differing severities.";
EMBO J. 13:3278-3285(1994).
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- FUNCTION: Collagen type IV is specific for basement membranes. Vital for embryonic development.
- SUBUNIT: Trimers of two alpha 1(IV) and one alpha 2(IV) chain. Type IV collagen forms a mesh-like network linked through intermolecular interactions between 7S domains and between NC1 domains.
- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane.
- ALTERNATIVE PRODUCTS:
2 named isoforms [FASTA] produced by alternative splicing.
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| Name | II |
| Synonyms | b |
| Isoform ID | P17140-2 |
| Features which should be applied to build the isoform sequence: VSP_001160. |
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- DEVELOPMENTAL STAGE: Isoform I is predominant in embryos and isoform II is predominant in the larvae and adults.
- DOMAIN: Alpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain.
- PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
- PTM: Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens.
- SIMILARITY: Belongs to the type IV collagen family.
- SIMILARITY: Contains 1 collagen IV NC1 (C-terminal non-collagenous) domain.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 1758 AA [This is the length of the unprocessed precursor] |
Molecular weight: 167751 Da [This is the MW of the unprocessed precursor] |
CRC64: 97EE3F3DBB2D2AC5 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MKQRAALGPV LRLAILALLA VSYVQSQATC RDCSNRGCFC VGEKGSMGAP GPQGPPGTQG
70 80 90 100 110 120
IRGFPGPEGL AGPKGLKGAQ GPPGPVGIKG DRGAVGVPGF PGNDGGNGRP GEPGPPGAPG
130 140 150 160 170 180
WDGCNGTDGA PGIPGRPGPP GMPGFPGPPG MDGLKGEPAI GYAGAPGEKG DGGMPGMPGL
190 200 210 220 230 240
PGPSGRDGYP GEKGDRGDTG NAGPRGPPGE AGSPGNPGIG SIGPKGDPGD LGSVGPPGPP
250 260 270 280 290 300
GPREFTGSGS IVGPRGNPGE KGDKGEPGEG GQRGYPGNGG LSGQPGLPGM KGEKGLSGPA
310 320 330 340 350 360
GPRGKEGRPG NAGPPGFKGD RGLDGLGGIP GLPGQKGEAG YPGRDGPKGN SGPPGPPGGG
370 380 390 400 410 420
TFNDGAPGPP GLPGRPGNPG PPGTDGYPGA PGPAGPIGNT GGPGLPGYPG NEGLPGPKGD
430 440 450 460 470 480
KGDGGIPGAP GVSGPSGIPG LPGPKGEPGY RGTPGQSIPG LPGKDGKPGL DGAPGRKGEN
490 500 510 520 530 540
GLPGVRGPPG DSLNGLPGAP GQRGAPGPNG YDGRDGVNGL PGAPGTKGDR GGTCSACAPG
550 560 570 580 590 600
TKGEKGLPGY SGQPGPQGDR GLPGMPGPVG DAGDDGLPGP AGRPGSPGPP GQDGFPGLPG
610 620 630 640 650 660
QKGEPTQLTL RPGPPGYPGL KGENGFPGQP GVDGLPGPSG PVGPPGAPGY PGEKGDAGLP
670 680 690 700 710 720
GLSGKPGQDG LPGLPGNKGE AGYGQPGQPG FPGAKGDGGL PGLPGTPGLQ GMPGEPAPEN
730 740 750 760 770 780
QVNPAPPGQP GLPGLPGTKG EGGYPGRPGE VGQPGFPGLP GMKGDSGLPG PPGLPGHPGV
790 800 810 820 830 840
PGDKGFGGVP GLPGIPGPKG DVGNPGLPGL NGQKGEPGVG VPGQPGSPGF PGLKGDAGLP
850 860 870 880 890 900
GLPGTPGLEG QRGFPGAPGL KGGDGLPGLS GQPGYPGEKG DAGLPGVPGR EGSPGFPGQD
910 920 930 940 950 960
GLPGVPGMKG EDGLPGLPGV TGLKGDLGAP GQSGAPGLPG APGYPGMKGN AGIPGVPGFK
970 980 990 1000 1010 1020
GDGGLPGLPG LNGPKGEPGV PGMPGTPGMK GNGGLPGLPG RDGLSGVPGM KGDRGFNGLP
1030 1040 1050 1060 1070 1080
GEKGEAGPAA RDGQKGDAGL PGQPGLRGPQ GPSGLPGVPG FKGETGLPGY GQPGQPGEKG
1090 1100 1110 1120 1130 1140
LPGIPGKAGR QGAPGSPGQD GLPGFPGMKG ESGYPGQDGL PGRDGLPGVP GQKGDLGQSG
1150 1160 1170 1180 1190 1200
QPGLSGAPGL DGQPGVPGIR GDKGQGGLPG IPGDRGMDGY PGQKGENGYP GQPGLPGLGG
1210 1220 1230 1240 1250 1260
EKGFAGTPGF PGLKGSPGYP GQDGLPGIPG LKGDSGFPGQ PGQEGLPGLS GEKGMGGLPG
1270 1280 1290 1300 1310 1320
MPGQPGQSIA GPVGPPGAPG LQGKDGFPGL PGQKGESGLS GLPGAPGLKG ESGMPGFPGA
1330 1340 1350 1360 1370 1380
KGDLGANGIP GKRGEDGLPG VPGRDGQPGI PGLKGEVGGA GLPGQPGFPG IPGLKGEGGL
1390 1400 1410 1420 1430 1440
PGFPGAKGEA GFPGTPGVPG YAGEKGDGGL PGLPGRDGLP GADGPVGPPG PSGPQNLVEP
1450 1460 1470 1480 1490 1500
GEKGLPGLPG APGLRGEKGM PGLDGPPGND GPPGLPGQRG NDGYPGAPGL SGEKGMGGLP
1510 1520 1530 1540 1550 1560
GFPGLDGQPG GPGAPGLPGA PGAAGPAYRD GFVLVKHSQT TEVPRCPEGQ TKLWDGYSLL
1570 1580 1590 1600 1610 1620
YIEGNEKSHN QDLGHAGSCL QRFSTMPFLF CDFNNVCNYA SRNEKSYWLS TSEAIPMMPV
1630 1640 1650 1660 1670 1680
NEREIEPYIS RCAVCEAPAN TIAVHSQTIQ IPNCPAGWSS LWIGYSFAMH TGAGAEGGGQ
1690 1700 1710 1720 1730 1740
SPSSPGSCLE DFRATPFIEC NGARGSCHYF ANKFSFWLTT IDNDSEFKVP ESQTLKSGNL
1750
RTRVSRCQVC VKSTDGRH
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P17140 in FASTA format |
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ExPASy Home page
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