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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.

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: InterPro

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. cellular response to amino acid stimulus Source: MGI
  3. epithelial cell differentiation Source: Ensembl
  4. neuromuscular junction development Source: MGI
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_209041. Scavenging by Class A Receptors.
REACT_216309. Integrin cell surface interactions.

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 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 – 2727
Add
BLAST
Propeptidei28 – 172145N-terminal propeptide (7S domain)
PRO_0000005750Add
BLAST
Chaini173 – 16691497Collagen alpha-1(IV) chain
PRO_0000005751Add
BLAST
Chaini1445 – 1669225Arresten
PRO_0000390483Add
BLAST

Amino acid modifications

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1445 – 1669225Collagen IV NC1
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni173 – 14401268Triple-helical region
Add
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.

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00720000108691.
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

MGPRLSVWLL LLFAALLLHE ERSRAAAKGD CGGSGCGKCD CHGVKGQKGE     50
RGLPGLQGVI GFPGMQGPEG PHGPPGQKGD AGEPGLPGTK GTRGPPGAAG 100
YPGNPGLPGI PGQDGPPGPP GIPGCNGTKG ERGPLGPPGL PGFSGNPGPP 150
GLPGMKGDPG EILGHVPGTL LKGERGFPGI PGMPGSPGLP GLQGPVGPPG 200
FTGPPGPPGP PGPPGEKGQM GSSFQGPKGD KGEQGVSGPP GVPGQAQVKE 250
KGDFAPTGEK GQKGEPGFPG VPGYGEKGEP GKQGPRGKPG KDGEKGERGS 300
PGIPGDSGYP GLPGRQGPQG EKGEAGLPGP PGTVIGTMPL GEKGDRGYPG 350
APGLRGEPGP KGFPGTPGQP GPPGFPTPGQ AGAPGFPGER GEKGDQGFPG 400
VSLPGPSGRD GAPGPPGPPG PPGQPGHTNG IVECQPGPPG DQGPPGTPGQ 450
PGLTGEVGQK GQKGESCLAC DTEGLRGPPG PQGPPGEIGF PGQPGAKGDR 500
GLPGRDGLEG LPGPQGSPGL IGQPGAKGEP GEIFFDMRLK GDKGDPGFPG 550
QPGMPGRAGT PGRDGHPGLP GPKGSPGSIG LKGERGPPGG VGFPGSRGDI 600
GPPGPPGVGP IGPVGEKGQA GFPGGPGSPG LPGPKGEAGK VVPLPGPPGA 650
AGLPGSPGFP GPQGDRGFPG TPGRPGIPGE KGAVGQPGIG FPGLPGPKGV 700
DGLPGEIGRP GSPGRPGFNG LPGNPGPQGQ KGEPGIGLPG LKGQPGLPGI 750
PGTPGEKGSI GGPGVPGEQG LTGPPGLQGI RGDPGPPGVQ GPAGPPGVPG 800
IGPPGAMGPP GGQGPPGSSG PPGIKGEKGF PGFPGLDMPG PKGDKGSQGL 850
PGLTGQSGLP GLPGQQGTPG VPGFPGSKGE MGVMGTPGQP GSPGPAGTPG 900
LPGEKGDHGL PGSSGPRGDP GFKGDKGDVG LPGMPGSMEH VDMGSMKGQK 950
GDQGEKGQIG PTGDKGSRGD PGTPGVPGKD GQAGHPGQPG PKGDPGLSGT 1000
PGSPGLPGPK GSVGGMGLPG SPGEKGVPGI PGSQGVPGSP GEKGAKGEKG 1050
QSGLPGIGIP GRPGDKGDQG LAGFPGSPGE KGEKGSAGTP GMPGSPGPRG 1100
SPGNIGHPGS PGLPGEKGDK GLPGLDGVPG VKGEAGLPGT PGPTGPAGQK 1150
GEPGSDGIPG SAGEKGEQGV PGRGFPGFPG SKGDKGSKGE VGFPGLAGSP 1200
GIPGVKGEQG FMGPPGPQGQ PGLPGTPGHP VEGPKGDRGP QGQPGLPGHP 1250
GPMGPPGFPG INGPKGDKGN QGWPGAPGVP GPKGDPGFQG MPGIGGSPGI 1300
TGSKGDMGLP GVPGFQGQKG LPGLQGVKGD QGDQGVPGPK GLQGPPGPPG 1350
PYDVIKGEPG LPGPEGPPGL KGLQGPPGPK GQQGVTGSVG LPGPPGVPGF 1400
DGAPGQKGET GPFGPPGPRG FPGPPGPDGL PGSMGPPGTP SVDHGFLVTR 1450
HSQTTDDPLC PPGTKILYHG YSLLYVQGNE RAHGQDLGTA GSCLRKFSTM 1500
PFLFCNINNV CNFASRNDYS YWLSTPEPMP MSMAPISGDN IRPFISRCAV 1550
CEAPAMVMAV HSQTIQIPQC PNGWSSLWIG YSFVMHTSAG AEGSGQALAS 1600
PGSCLEEFRS APFIECHGRG TCNYYANAYS FWLATIERSE MFKKPTPSTL 1650
KAGELRTHVS RCQVCMRRT 1669
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.
The sequence AAH72650.1 differs from that shown. Reason: Frameshift at position 1547.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261A → P in CAA29946. 1 Publication
Sequence conflicti186 – 1861S → L in CAA29946. 1 Publication
Sequence conflicti319 – 3191Q → S in CAA29946. 1 Publication
Sequence conflicti369 – 3691Q → L in CAA29946. 1 Publication
Sequence conflicti403 – 4031L → F in CAA29946. 1 Publication
Sequence conflicti481 – 4811P → L in CAA29946. 1 Publication
Sequence conflicti493 – 4931Q → H in CAA29946. 1 Publication
Sequence conflicti621 – 6211G → S in BAE27208. 1 Publication
Sequence conflicti712 – 7121S → I in CAA29946. 1 Publication
Sequence conflicti813 – 8131Q → E in AAA50292. 1 Publication
Sequence conflicti982 – 9821Q → H in CAA29946. 1 Publication
Sequence conflicti1397 – 13971V → S in AAA37342. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 ENSGT00720000108691.
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_209041. Scavenging by Class A Receptors.
REACT_216309. Integrin cell surface interactions.

Miscellaneous databases

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: September 3, 2014
This is version 141 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

Similar proteinsi