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P02463

- CO4A1_MOUSE

UniProt

P02463 - CO4A1_MOUSE

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Protein

Collagen alpha-1(IV) chain

Gene

Col4a1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.
Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation. Inhibits expression of hypoxia-inducible factor 1alpha and ERK1/2 and p38 MAPK activation. Ligand for alpha1/beta1 integrin (By similarity).By similarity

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: Ensembl

GO - Biological processi

  1. basement membrane organization Source: Ensembl
  2. brain development Source: Ensembl
  3. cellular response to amino acid stimulus Source: MGI
  4. epithelial cell differentiation Source: Ensembl
  5. neuromuscular junction development Source: MGI
  6. patterning of blood vessels Source: Ensembl
  7. renal tubule morphogenesis Source: Ensembl
  8. retinal blood vessel morphogenesis Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Angiogenesis

Enzyme and pathway databases

ReactomeiREACT_196581. Scavenging by Class A Receptors.
REACT_196595. Anchoring fibril formation.
REACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199055. Collagen degradation.
REACT_202342. Laminin interactions.
REACT_206066. Extracellular matrix organization.
REACT_216309. Integrin cell surface interactions.
REACT_236183. NCAM1 interactions.
REACT_263353. Signaling by PDGF.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(IV) chain
Cleaved into the following chain:
Gene namesi
Name:Col4a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:88454. Col4a1.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: UniProtKB
  2. collagen type IV trimer Source: MGI
  3. extracellular matrix Source: UniProtKB
  4. extracellular region Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Disruption phenotypei

Mice develop perinatal cerebral hemorrhage and porencephaly. The mutant protein inhibits the secretion of mutant and normal proteins into the basement membrane of embryonic origin. The mutation is semidominant.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Add
BLAST
Propeptidei28 – 172145N-terminal propeptide (7S domain)PRO_0000005750Add
BLAST
Chaini173 – 16691497Collagen alpha-1(IV) chainPRO_0000005751Add
BLAST
Chaini1445 – 1669225ArrestenPRO_0000390483Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1460 ↔ 1551Or C-1460 with C-1548PROSITE-ProRule annotation
Disulfide bondi1493 ↔ 1548Or C-1493 with C-1551PROSITE-ProRule annotation
Disulfide bondi1505 ↔ 1511PROSITE-ProRule annotation
Cross-linki1533 – 1533S-Lysyl-methionine sulfilimine (Met-Lys) (interchain with K-1651)By similarity
Disulfide bondi1570 ↔ 1665Or C-1570 with C-1662PROSITE-ProRule annotation
Disulfide bondi1604 ↔ 1662Or C-1604 with C-1665PROSITE-ProRule annotation
Disulfide bondi1616 ↔ 1622PROSITE-ProRule annotation
Cross-linki1651 – 1651S-Lysyl-methionine sulfilimine (Lys-Met) (interchain with M-1533)By similarity

Post-translational modificationi

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
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.
Proteolytic processing produces the C-terminal NC1 peptide, arresten.By similarity
The trimeric structure of the NC1 domains is stabilized by covalent bonds between Lys and Met residues.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

MaxQBiP02463.
PaxDbiP02463.
PRIDEiP02463.

PTM databases

PhosphoSiteiP02463.

Expressioni

Gene expression databases

BgeeiP02463.
CleanExiMM_COL4A1.
GenevestigatoriP02463.

Interactioni

Subunit structurei

There are six type IV collagen isoforms, alpha 1(IV)-alpha 6(IV), each of which can form a triple helix structure with 2 other chains to generate type IV collagen network.

Protein-protein interaction databases

BioGridi198816. 1 interaction.
IntActiP02463. 1 interaction.
MINTiMINT-4388747.

Structurei

3D structure databases

ProteinModelPortaliP02463.
SMRiP02463. Positions 1442-1669.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1445 – 1669225Collagen IV NC1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni173 – 14401268Triple-helical regionAdd
BLAST

Domaini

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.

Sequence similaritiesi

Belongs to the type IV collagen family.PROSITE-ProRule annotation
Contains 1 collagen IV NC1 (C-terminal non-collagenous) domain.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00770000120455.
HOVERGENiHBG004933.
InParanoidiP02463.
KOiK06237.
OMAiGVPGQKX.
OrthoDBiEOG7RZ5P3.
PhylomeDBiP02463.
TreeFamiTF316865.

Family and domain databases

Gene3Di2.170.240.10. 1 hit.
InterProiIPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR001442. Collagen_VI_NC.
[Graphical view]
PfamiPF01413. C4. 2 hits.
PF01391. Collagen. 20 hits.
[Graphical view]
SMARTiSM00111. C4. 2 hits.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 2 hits.
PROSITEiPS51403. NC1_IV. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02463-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGPRLSVWLL LLFAALLLHE ERSRAAAKGD CGGSGCGKCD CHGVKGQKGE
60 70 80 90 100
RGLPGLQGVI GFPGMQGPEG PHGPPGQKGD AGEPGLPGTK GTRGPPGAAG
110 120 130 140 150
YPGNPGLPGI PGQDGPPGPP GIPGCNGTKG ERGPLGPPGL PGFSGNPGPP
160 170 180 190 200
GLPGMKGDPG EILGHVPGTL LKGERGFPGI PGMPGSPGLP GLQGPVGPPG
210 220 230 240 250
FTGPPGPPGP PGPPGEKGQM GSSFQGPKGD KGEQGVSGPP GVPGQAQVKE
260 270 280 290 300
KGDFAPTGEK GQKGEPGFPG VPGYGEKGEP GKQGPRGKPG KDGEKGERGS
310 320 330 340 350
PGIPGDSGYP GLPGRQGPQG EKGEAGLPGP PGTVIGTMPL GEKGDRGYPG
360 370 380 390 400
APGLRGEPGP KGFPGTPGQP GPPGFPTPGQ AGAPGFPGER GEKGDQGFPG
410 420 430 440 450
VSLPGPSGRD GAPGPPGPPG PPGQPGHTNG IVECQPGPPG DQGPPGTPGQ
460 470 480 490 500
PGLTGEVGQK GQKGESCLAC DTEGLRGPPG PQGPPGEIGF PGQPGAKGDR
510 520 530 540 550
GLPGRDGLEG LPGPQGSPGL IGQPGAKGEP GEIFFDMRLK GDKGDPGFPG
560 570 580 590 600
QPGMPGRAGT PGRDGHPGLP GPKGSPGSIG LKGERGPPGG VGFPGSRGDI
610 620 630 640 650
GPPGPPGVGP IGPVGEKGQA GFPGGPGSPG LPGPKGEAGK VVPLPGPPGA
660 670 680 690 700
AGLPGSPGFP GPQGDRGFPG TPGRPGIPGE KGAVGQPGIG FPGLPGPKGV
710 720 730 740 750
DGLPGEIGRP GSPGRPGFNG LPGNPGPQGQ KGEPGIGLPG LKGQPGLPGI
760 770 780 790 800
PGTPGEKGSI GGPGVPGEQG LTGPPGLQGI RGDPGPPGVQ GPAGPPGVPG
810 820 830 840 850
IGPPGAMGPP GGQGPPGSSG PPGIKGEKGF PGFPGLDMPG PKGDKGSQGL
860 870 880 890 900
PGLTGQSGLP GLPGQQGTPG VPGFPGSKGE MGVMGTPGQP GSPGPAGTPG
910 920 930 940 950
LPGEKGDHGL PGSSGPRGDP GFKGDKGDVG LPGMPGSMEH VDMGSMKGQK
960 970 980 990 1000
GDQGEKGQIG PTGDKGSRGD PGTPGVPGKD GQAGHPGQPG PKGDPGLSGT
1010 1020 1030 1040 1050
PGSPGLPGPK GSVGGMGLPG SPGEKGVPGI PGSQGVPGSP GEKGAKGEKG
1060 1070 1080 1090 1100
QSGLPGIGIP GRPGDKGDQG LAGFPGSPGE KGEKGSAGTP GMPGSPGPRG
1110 1120 1130 1140 1150
SPGNIGHPGS PGLPGEKGDK GLPGLDGVPG VKGEAGLPGT PGPTGPAGQK
1160 1170 1180 1190 1200
GEPGSDGIPG SAGEKGEQGV PGRGFPGFPG SKGDKGSKGE VGFPGLAGSP
1210 1220 1230 1240 1250
GIPGVKGEQG FMGPPGPQGQ PGLPGTPGHP VEGPKGDRGP QGQPGLPGHP
1260 1270 1280 1290 1300
GPMGPPGFPG INGPKGDKGN QGWPGAPGVP GPKGDPGFQG MPGIGGSPGI
1310 1320 1330 1340 1350
TGSKGDMGLP GVPGFQGQKG LPGLQGVKGD QGDQGVPGPK GLQGPPGPPG
1360 1370 1380 1390 1400
PYDVIKGEPG LPGPEGPPGL KGLQGPPGPK GQQGVTGSVG LPGPPGVPGF
1410 1420 1430 1440 1450
DGAPGQKGET GPFGPPGPRG FPGPPGPDGL PGSMGPPGTP SVDHGFLVTR
1460 1470 1480 1490 1500
HSQTTDDPLC PPGTKILYHG YSLLYVQGNE RAHGQDLGTA GSCLRKFSTM
1510 1520 1530 1540 1550
PFLFCNINNV CNFASRNDYS YWLSTPEPMP MSMAPISGDN IRPFISRCAV
1560 1570 1580 1590 1600
CEAPAMVMAV HSQTIQIPQC PNGWSSLWIG YSFVMHTSAG AEGSGQALAS
1610 1620 1630 1640 1650
PGSCLEEFRS APFIECHGRG TCNYYANAYS FWLATIERSE MFKKPTPSTL
1660
KAGELRTHVS RCQVCMRRT
Length:1,669
Mass (Da):160,679
Last modified:February 20, 2007 - v4
Checksum:iEFEEC72AF301E5CF
GO

Sequence cautioni

The sequence AAH72650.1 differs from that shown. Reason: Insertion sequence.Curated
The sequence AAH72650.1 differs from that shown. Reason: Frameshift at position 1547. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261A → P in CAA29946. (PubMed:3338568)Curated
Sequence conflicti186 – 1861S → L in CAA29946. (PubMed:3338568)Curated
Sequence conflicti319 – 3191Q → S in CAA29946. (PubMed:3338568)Curated
Sequence conflicti369 – 3691Q → L in CAA29946. (PubMed:3338568)Curated
Sequence conflicti403 – 4031L → F in CAA29946. (PubMed:3338568)Curated
Sequence conflicti481 – 4811P → L in CAA29946. (PubMed:3338568)Curated
Sequence conflicti493 – 4931Q → H in CAA29946. (PubMed:3338568)Curated
Sequence conflicti621 – 6211G → S in BAE27208. (PubMed:16141072)Curated
Sequence conflicti712 – 7121S → I in CAA29946. (PubMed:3338568)Curated
Sequence conflicti813 – 8131Q → E in AAA50292. (PubMed:2703490)Curated
Sequence conflicti982 – 9821Q → H in CAA29946. (PubMed:3338568)Curated
Sequence conflicti1397 – 13971V → S in AAA37342. (PubMed:3755692)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04694 mRNA. Translation: AAA50292.1.
AK142097 mRNA. Translation: BAE24936.1.
AK146487 mRNA. Translation: BAE27208.1.
AK147284 mRNA. Translation: BAE27820.1.
AK147355 mRNA. Translation: BAE27863.1.
AK147661 mRNA. Translation: BAE28055.1.
BC002269 mRNA. Translation: AAH02269.1.
BC056620 mRNA. Translation: AAH56620.1.
BC072650 mRNA. Translation: AAH72650.1. Sequence problems.
X06777 mRNA. Translation: CAA29946.1.
J03758 mRNA. Translation: AAA37439.1.
J03944 Genomic DNA. Translation: AAA37442.1.
J04448 Genomic DNA. Translation: AAA37437.1.
M23333 Genomic DNA. Translation: AAA51625.1.
M12879 Genomic DNA. Translation: AAA37343.1.
M13024 Genomic DNA. No translation available.
M13025 Genomic DNA. No translation available.
M13026 Genomic DNA. Translation: AAA37344.1.
M13027 Genomic DNA. Translation: AAA37345.1.
M13043 Genomic DNA. Translation: AAA37346.1.
M14042 mRNA. Translation: AAA37342.1.
X02201 mRNA. Translation: CAA26132.1.
M15832 mRNA. Translation: AAA37340.1.
CCDSiCCDS40219.1.
PIRiA33525. CGMS4B.
RefSeqiNP_034061.2. NM_009931.2.
UniGeneiMm.738.

Genome annotation databases

EnsembliENSMUST00000033898; ENSMUSP00000033898; ENSMUSG00000031502.
GeneIDi12826.
KEGGimmu:12826.
UCSCiuc009kvb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04694 mRNA. Translation: AAA50292.1 .
AK142097 mRNA. Translation: BAE24936.1 .
AK146487 mRNA. Translation: BAE27208.1 .
AK147284 mRNA. Translation: BAE27820.1 .
AK147355 mRNA. Translation: BAE27863.1 .
AK147661 mRNA. Translation: BAE28055.1 .
BC002269 mRNA. Translation: AAH02269.1 .
BC056620 mRNA. Translation: AAH56620.1 .
BC072650 mRNA. Translation: AAH72650.1 . Sequence problems.
X06777 mRNA. Translation: CAA29946.1 .
J03758 mRNA. Translation: AAA37439.1 .
J03944 Genomic DNA. Translation: AAA37442.1 .
J04448 Genomic DNA. Translation: AAA37437.1 .
M23333 Genomic DNA. Translation: AAA51625.1 .
M12879 Genomic DNA. Translation: AAA37343.1 .
M13024 Genomic DNA. No translation available.
M13025 Genomic DNA. No translation available.
M13026 Genomic DNA. Translation: AAA37344.1 .
M13027 Genomic DNA. Translation: AAA37345.1 .
M13043 Genomic DNA. Translation: AAA37346.1 .
M14042 mRNA. Translation: AAA37342.1 .
X02201 mRNA. Translation: CAA26132.1 .
M15832 mRNA. Translation: AAA37340.1 .
CCDSi CCDS40219.1.
PIRi A33525. CGMS4B.
RefSeqi NP_034061.2. NM_009931.2.
UniGenei Mm.738.

3D structure databases

ProteinModelPortali P02463.
SMRi P02463. Positions 1442-1669.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198816. 1 interaction.
IntActi P02463. 1 interaction.
MINTi MINT-4388747.

PTM databases

PhosphoSitei P02463.

Proteomic databases

MaxQBi P02463.
PaxDbi P02463.
PRIDEi P02463.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000033898 ; ENSMUSP00000033898 ; ENSMUSG00000031502 .
GeneIDi 12826.
KEGGi mmu:12826.
UCSCi uc009kvb.2. mouse.

Organism-specific databases

CTDi 1282.
MGIi MGI:88454. Col4a1.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00770000120455.
HOVERGENi HBG004933.
InParanoidi P02463.
KOi K06237.
OMAi GVPGQKX.
OrthoDBi EOG7RZ5P3.
PhylomeDBi P02463.
TreeFami TF316865.

Enzyme and pathway databases

Reactomei REACT_196581. Scavenging by Class A Receptors.
REACT_196595. Anchoring fibril formation.
REACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199055. Collagen degradation.
REACT_202342. Laminin interactions.
REACT_206066. Extracellular matrix organization.
REACT_216309. Integrin cell surface interactions.
REACT_236183. NCAM1 interactions.
REACT_263353. Signaling by PDGF.

Miscellaneous databases

ChiTaRSi Col4a1. mouse.
NextBioi 282314.
PROi P02463.
SOURCEi Search...

Gene expression databases

Bgeei P02463.
CleanExi MM_COL4A1.
Genevestigatori P02463.

Family and domain databases

Gene3Di 2.170.240.10. 1 hit.
InterProi IPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR001442. Collagen_VI_NC.
[Graphical view ]
Pfami PF01413. C4. 2 hits.
PF01391. Collagen. 20 hits.
[Graphical view ]
SMARTi SM00111. C4. 2 hits.
[Graphical view ]
SUPFAMi SSF56436. SSF56436. 2 hits.
PROSITEi PS51403. NC1_IV. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The complete primary structure for the alpha 1-chain of mouse collagen IV. Differential evolution of collagen IV domains."
    Muthukumaran G., Blumberg B., Kurkinen M.
    J. Biol. Chem. 264:6310-6317(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6 and C57BL/6J.
    Tissue: Brain, Eye, Heart and Placenta.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6 and FVB/N.
    Tissue: Brain, Colon and Mammary gland.
  4. "cDNA clones completing the nucleotide and derived amino acid sequence of the alpha 1 chain of basement membrane (type IV) collagen from mouse."
    Wood L., Theriault N., Vogeli G.
    FEBS Lett. 227:5-8(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1154.
  5. "Structure of the amino-terminal portion of the murine alpha 1(IV) collagen chain and the corresponding region of the gene."
    Killen P.D., Burbelo P.D., Sakurai Y., Yamada Y.
    J. Biol. Chem. 263:8706-8709(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-129.
  6. "Characterization of the promoter for the alpha 1 (IV) collagen gene. DNA sequences within the first intron enhance transcription."
    Killen P.D., Burbelo P.D., Martin G.R., Yamada Y.
    J. Biol. Chem. 263:12310-12314(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
  7. "Head-to-head arrangement of murine type IV collagen genes."
    Kaytes P., Wood L., Theriault N., Kurkinen M., Vogeli G.
    J. Biol. Chem. 263:19274-19277(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
  8. "Alpha 1(IV) and alpha 2(IV) collagen genes are regulated by a bidirectional promoter and a shared enhancer."
    Burbelo P.D., Martin G.R., Yamada Y.
    Proc. Natl. Acad. Sci. U.S.A. 85:9679-9682(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
  9. "Alpha 1 type IV collagen gene evolved differently from fibrillar collagen genes."
    Sakurai Y., Sullivan M., Yamada Y.
    J. Biol. Chem. 261:6654-6657(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1110-1135.
  10. "Isolation of an alpha 1 type-IV collagen cDNA clone using a synthetic oligodeoxynucleotide."
    Nath P., Laurent M., Horn E., Sobel M.E., Zon G., Vogeli G.
    Gene 43:301-304(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1149-1424.
  11. "Amino acid sequence of the non-collagenous globular domain (NC1) of the alpha 1(IV) chain of basement membrane collagen as derived from complementary DNA."
    Oberbaeumer I., Laurent M., Schwarz U., Sakurai Y., Yamada Y., Vogeli G., Voss T., Siebold B., Glanville R.W., Kuhn K.
    Eur. J. Biochem. 147:217-224(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1276-1669.
  12. "Extensive homology between the carboxyl-terminal peptides of mouse alpha 1(IV) and alpha 2(IV) collagen."
    Kurkinen M., Condon M.R., Blumberg B., Barlow D., Quinones S., Saus J., Pihlajaniemi T.
    J. Biol. Chem. 262:8496-8499(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669.
  13. Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiCO4A1_MOUSE
AccessioniPrimary (citable) accession number: P02463
Secondary accession number(s): Q3UHJ4
, Q3UJE7, Q3UQV2, Q53X35, Q6GQS7, Q6PHB5, Q99LQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 20, 2007
Last modified: November 26, 2014
This is version 144 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3