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P02463

- CO4A1_MOUSE

UniProt

P02463 - CO4A1_MOUSE

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
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 4 (20 Feb 2007)
      Previous versions | rss
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    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: 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

    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

    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.
    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.

    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:
    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

    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: October 1, 2014
    This is version 142 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