Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P39061 (COIA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(XVIII) chain

Cleaved into the following chain:

  1. Endostatin
Gene names
Name:Col18a1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1774 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Endostatin potently inhibits endothelial cell proliferation and angiogenesis. May inhibit angiogenesis by binding to the heparan sulfate proteoglycans involved in growth factor signaling.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Tissue specificity

Expressed in liver, kidney, lung, skeletal muscle and testis. Ref.7

Post-translational modification

Prolines at the third position of the tripeptide repeating unit (G-X-Y) of the triple-helical regions are hydroxylated.

Sequence similarities

Belongs to the multiplexin collagen family.

Contains 7 collagen-like domains.

Contains 1 FZ (frizzled) domain.

Contains 1 laminin G-like domain.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative promoter usage
Alternative splicing
   DomainCollagen
Repeat
Signal
   LigandMetal-binding
Zinc
   PTMDisulfide bond
Glycoprotein
Hydroxylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from direct assay PubMed 15188432. Source: MGI

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

endothelial cell morphogenesis

Inferred from direct assay PubMed 15188432. Source: MGI

extracellular matrix organization

Inferred from mutant phenotype PubMed 15254016. Source: MGI

positive regulation of cell migration

Inferred from direct assay PubMed 15188432. Source: MGI

positive regulation of cell proliferation

Inferred from direct assay PubMed 15188432. Source: MGI

positive regulation of endothelial cell apoptotic process

Inferred from direct assay PubMed 15188432. Source: MGI

response to drug

Inferred from electronic annotation. Source: Ensembl

response to hydrostatic pressure

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbasement membrane

Inferred from direct assay PubMed 12588956PubMed 15254016PubMed 18757743PubMed 19651211. Source: MGI

collagen trimer

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular space

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform 1 (identifier: P39061-3)

Also known as: NC1-764;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Produced by alternative promoter usage.
Isoform 2 (identifier: P39061-1)

Also known as: Long; NC1-517;

The sequence of this isoform differs from the canonical sequence as follows:
     240-486: Missing.
Note: Produced by alternative splicing of isoform 1.
Isoform 3 (identifier: P39061-2)

Also known as: Short; NC1-301;

The sequence of this isoform differs from the canonical sequence as follows:
     1-459: Missing.
     460-486: AGDRLPVVCASLPSQEDGYCVFIGPAA → MAPRWHLLDVLTSLVLLLVARVSWAEP
Note: Produced by alternative promoter usage.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 17741748Collagen alpha-1(XVIII) chain
PRO_0000005795
Chain1591 – 1774184Endostatin
PRO_0000005796

Regions

Domain365 – 482118FZ
Domain522 – 704183Laminin G-like
Domain823 – 87856Collagen-like 1
Domain953 – 100755Collagen-like 2
Domain1008 – 104134Collagen-like 3
Domain1066 – 111752Collagen-like 4
Domain1118 – 114730Collagen-like 5
Domain1162 – 120241Collagen-like 6
Domain1216 – 126449Collagen-like 7
Region27 – 785759Nonhelical region 1 (NC1)
Region786 – 81227Triple-helical region 1 (COL1)
Region813 – 82210Nonhelical region 2 (NC2)
Region823 – 89674Triple-helical region 2 (COL2)
Region897 – 92024Nonhelical region 3 (NC3)
Region921 – 1042122Triple-helical region 3 (COL3)
Region1043 – 106523Nonhelical region 4 (NC4)
Region1066 – 114883Triple-helical region 4 (COL4)
Region1149 – 116214Nonhelical region 5 (NC5)
Region1163 – 120442Triple-helical region 5 (COL5)
Region1205 – 121713Nonhelical region 6 (NC6)
Region1218 – 129073Triple-helical region 6 (COL6)
Region1291 – 130010Nonhelical region 7 (NC7)
Region1301 – 133333Triple-helical region 7 (COL7)
Region1334 – 134512Nonhelical region 8 (NC8)
Region1346 – 136924Triple-helical region 8 (COL8)
Region1370 – 13767Nonhelical region 9 (NC9)
Region1377 – 142852Triple-helical region 9 (COL9)
Region1429 – 144113Nonhelical region 10 (NC10)
Region1442 – 145918Triple-helical region 10 (COL10)
Region1460 – 1774315Nonhelical region 11 (NC11)
Motif1351 – 13533Cell attachment site Potential

Sites

Metal binding15911Zinc; alternate
Metal binding15931Zinc
Metal binding15951Zinc; alternate
Metal binding16011Zinc
Metal binding16661Zinc

Amino acid modifications

Glycosylation3541N-linked (GlcNAc...) Potential
Glycosylation3611N-linked (GlcNAc...) Potential
Glycosylation5851N-linked (GlcNAc...) Ref.12
Glycosylation9471N-linked (GlcNAc...) Potential
Disulfide bond370 ↔ 433 By similarity
Disulfide bond380 ↔ 426 By similarity
Disulfide bond417 ↔ 455 By similarity
Disulfide bond444 ↔ 479 By similarity
Disulfide bond448 ↔ 468 By similarity
Disulfide bond1623 ↔ 1763 Ref.14
Disulfide bond1725 ↔ 1755 Ref.14

Natural variations

Alternative sequence1 – 459459Missing in isoform 3.
VSP_001157
Alternative sequence240 – 486247Missing in isoform 2.
VSP_008303
Alternative sequence460 – 48627AGDRL…IGPAA → MAPRWHLLDVLTSLVLLLVA RVSWAEP in isoform 3.
VSP_001158

Experimental info

Mutagenesis15911H → A: No effect on zinc binding. Ref.14
Mutagenesis15931H → A: Reduces zinc binding by 60%. Abolishes zinc binding; when associated with A-1595. Ref.14
Mutagenesis15951D → A: No effect on zinc binding. Abolishes zinc binding; when associated with A-1593. Ref.14
Mutagenesis16661D → A: Abolishes zinc binding. Ref.14
Sequence conflict10461G → V in AAH66080. Ref.4
Sequence conflict11471P → L in AAA19787. Ref.8
Sequence conflict11941P → F in AAA19787. Ref.8
Sequence conflict12111A → R in AAA19787. Ref.8
Sequence conflict13471D → V in BAC27554. Ref.6
Sequence conflict14041P → R in AAA20657. Ref.1
Sequence conflict14041P → R in AAC52901. Ref.2
Sequence conflict14041P → R in AAC52902. Ref.2
Sequence conflict14041P → R in AAC52903. Ref.2
Sequence conflict14041P → R in AAA19787. Ref.8
Sequence conflict15131P → L in AAA19787. Ref.8
Sequence conflict15231L → F in AAA19787. Ref.8
Sequence conflict16841L → V in AAA19787. Ref.8

Secondary structure

.................................. 1774
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (NC1-764) [UniParc].

Last modified May 1, 2007. Version 4.
Checksum: BEA79BADD1E34407

FASTA1,774182,172
        10         20         30         40         50         60 
MAPDPSRRLC LLLLLLLSCR LVPASADGNS LSPLNPLVWL WPPKTSDSLE GPVSKPQNSS 

        70         80         90        100        110        120 
PVQSTENPTT HVVPQDGLTE QQTTPASSEL PPEEEEEEDQ KAGQGGSPAT PAVPIPLVAP 

       130        140        150        160        170        180 
AASPDMKEEN VAGVGAKILN VAQGIRSFVQ LWDEDSTIGH SAGTEVPDSS IPTVLPSPAE 

       190        200        210        220        230        240 
LSSAPQGSKT TLWLSSAIPS SPDAQTTEAG TLAVPTQLPP FQSNLQAPLG RPSAPPDFPG 

       250        260        270        280        290        300 
RAFLSSSTDQ GSSWGNQEPP RQPQHLEGKG FLPMTARSSQ QHRHSDVHSD IHGHVPLLPL 

       310        320        330        340        350        360 
VTGPLVTASL SVHGLLSVPS SDPSGQLSQV AALPGFPGTW VSHVAPSSGT GLSNDSALAG 

       370        380        390        400        410        420 
NGSLTSTSRC LPLPPTLTLC SRLGIGHFWL PNHLHHTDSV EVEATVQAWG RFLHTNCHPF 

       430        440        450        460        470        480 
LAWFFCLLLA PSCGPGPPPP LPPCRQFCEA LEDECWNYLA GDRLPVVCAS LPSQEDGYCV 

       490        500        510        520        530        540 
FIGPAAENVA EEVGLLQLLG DPLPEKISQI DDPHVGPAYI FGPDSNSGQV AQYHFPKLFF 

       550        560        570        580        590        600 
RDFSLLFHVR PATEAAGVLF AITDAAQVVV SLGVKLSEVR DGQQNISLLY TEPGASQTQT 

       610        620        630        640        650        660 
GASFRLPAFV GQWTHFALSV DGGSVALYVD CEEFQRVPFA RASQGLELER GAGLFVGQAG 

       670        680        690        700        710        720 
TADPDKFQGM ISELKVRKTP RVSPVHCLDE EDDDEDRASG DFGSGFEESS KSHKEDTSLL 

       730        740        750        760        770        780 
PGLPQPPPVT SPPLAGGSTT EDPRTEETEE DAAVDSIGAE TLPGTGSSGA WDEAIQNPGR 

       790        800        810        820        830        840 
GLIKGGMKGQ KGEPGAQGPP GPAGPQGPAG PVVQSPNSQP VPGAQGPPGP QGPPGKDGTP 

       850        860        870        880        890        900 
GRDGEPGDPG EDGRPGDTGP QGFPGTPGDV GPKGEKGDPG IGPRGPPGPP GPPGPSFRQD 

       910        920        930        940        950        960 
KLTFIDMEGS GFSGDIESLR GPRGFPGPPG PPGVPGLPGE PGRFGINGSY APGPAGLPGV 

       970        980        990       1000       1010       1020 
PGKEGPPGFP GPPGPPGPPG KEGPPGVAGQ KGSVGDVGIP GPKGSKGDLG PIGMPGKSGL 

      1030       1040       1050       1060       1070       1080 
AGSPGPVGPP GPPGPPGPPG PGFAAGFDDM EGSGIPLWTT ARSSDGLQGP PGSPGLKGDP 

      1090       1100       1110       1120       1130       1140 
GVAGLPGAKG EVGADGAQGI PGPPGREGAA GSPGPKGEKG MPGEKGNPGK DGVGRPGLPG 

      1150       1160       1170       1180       1190       1200 
PPGPPGPVIY VSSEDKAIVS TPGPEGKPGY AGFPGPAGPK GDLGSKGEQG LPGPKGEKGE 

      1210       1220       1230       1240       1250       1260 
PGTIFSPDGR ALGHPQKGAK GEPGFRGPPG PYGRPGHKGE IGFPGRPGRP GTNGLKGEKG 

      1270       1280       1290       1300       1310       1320 
EPGDASLGFS MRGLPGPPGP PGPPGPPGMP IYDSNAFVES GRPGLPGQQG VQGPSGPKGD 

      1330       1340       1350       1360       1370       1380 
KGEVGPPGPP GQFPIDLFHL EAEMKGDKGD RGDAGQKGER GEPGAPGGGF FSSSVPGPPG 

      1390       1400       1410       1420       1430       1440 
PPGYPGIPGP KGESIRGPPG PPGPQGPPGI GYEGRQGPPG PPGPPGPPSF PGPHRQTVSV 

      1450       1460       1470       1480       1490       1500 
PGPPGPPGPP GPPGAMGASA GQVRIWATYQ TMLDKIREVP EGWLIFVAER EELYVRVRNG 

      1510       1520       1530       1540       1550       1560 
FRKVLLEART ALPRGTGNEV AALQPPLVQL HEGSPYTRRE YSYSTARPWR ADDILANPPR 

      1570       1580       1590       1600       1610       1620 
LPDRQPYPGV PHHHSSYVHL PPARPTLSLA HTHQDFQPVL HLVALNTPLS GGMRGIRGAD 

      1630       1640       1650       1660       1670       1680 
FQCFQQARAV GLSGTFRAFL SSRLQDLYSI VRRADRGSVP IVNLKDEVLS PSWDSLFSGS 

      1690       1700       1710       1720       1730       1740 
QGQLQPGARI FSFDGRDVLR HPAWPQKSVW HGSDPSGRRL MESYCETWRT ETTGATGQAS 

      1750       1760       1770 
SLLSGRLLEQ KAASCHNSYI VLCIENSFMT SFSK 

« Hide

Isoform 2 (Long) (NC1-517) [UniParc].

Checksum: E7AF043EC82D0326
Show »

FASTA1,527155,950
Isoform 3 (Short) (NC1-301) [UniParc].

Checksum: B8215602ACE7AD1F
Show »

FASTA1,315134,204

References

« Hide 'large scale' references
[1]"Primary structure of the alpha 1 chain of mouse type XVIII collagen, partial structure of the corresponding gene, and comparison of the alpha 1(XVIII) chain with its homologue, the alpha 1(XV) collagen chain."
Rehn M.V., Hintikka E., Pihlajaniemi T.
J. Biol. Chem. 269:13929-13935(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3).
Strain: BALB/c.
Tissue: Liver.
[2]"Characterization of the mouse gene for the alpha-1 chain of type XVIII collagen (COL18A1) reveals that the three variant N-terminal polypeptide forms are transcribed from two widely separated promoters."
Rehn M., Hintikka E., Pihlajaniemi T.
Genomics 32:436-446(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"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] (ISOFORM 3).
Strain: C57BL/6.
Tissue: Brain and Embryo.
[5]"Alpha 1(XVIII), a collagen chain with frequent interruptions in the collagenous sequence, a distinct tissue distribution, and homology with type XV collagen."
Rehn M.V., Pihlajaniemi T.
Proc. Natl. Acad. Sci. U.S.A. 91:4234-4238(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1387 (ISOFORM 3).
[6]"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. expand/collapse author list , 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] OF 1-1347 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1615-1774.
Strain: C57BL/6J.
Tissue: Head.
[7]"Identification of three N-terminal ends of type XVIII collagen chains and tissue-specific differences in the expression of the corresponding transcripts. The longest form contains a novel motif homologous to rat and Drosophila frizzled proteins."
Rehn M., Pihlajaniemi T.
J. Biol. Chem. 270:4705-4711(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-562 (ISOFORMS 1 AND 3), TISSUE SPECIFICITY.
[8]"Isolation and sequencing of cDNAs for proteins with multiple domains of Gly-Xaa-Yaa repeats identify a distinct family of collagenous proteins."
Oh S.P., Kamagata Y., Muragaki Y., Timmons S., Ooshima A., Olsen B.R.
Proc. Natl. Acad. Sci. U.S.A. 91:4229-4233(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 487-1774.
Tissue: Liver.
[9]"Identification of a novel collagen chain represented by extensive interruptions in the triple-helical region."
Abe N., Muragaki Y., Yoshioka H., Inoue H., Ninomiya Y.
Biochem. Biophys. Res. Commun. 196:576-582(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 635-1774.
Tissue: Embryo.
[10]"Anticancer treatment of endostatin gene therapy by targeting tumor neovasculature in C57/BL mice."
Jia S., Zhu F., Li H., He F., Xiu R.-J.
Clin. Hemorheol. Microcirc. 23:251-257(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1591-1774.
[11]"Endostatin: an endogenous inhibitor of angiogenesis and tumor growth."
O'Reilly M.S., Boehm T., Shing Y., Fukai N., Vasios G., Lane W.S., Flynn E., Birkhead J.R., Olsen B.R., Folkman J.
Cell 88:277-285(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF ENDOSTATIN, PROTEIN SEQUENCE OF 1591-1610.
[12]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-585.
[13]"Crystal structure of the angiogenesis inhibitor endostatin at 1.5-A resolution."
Hohenester E., Sasaki T., Olsen B.R., Timpl R.
EMBO J. 17:1656-1664(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF ENDOSTATIN.
[14]"Variable zinc coordination in endostatin."
Hohenester E., Sasaki T., Mann K., Timpl R.
J. Mol. Biol. 297:1-6(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1589-1774, DISULFIDE BONDS, MUTAGENESIS OF HIS-1591; HIS-1593; ASP-1595 AND ASP-1666, ZINC-BINDING SITES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U03714 mRNA. Translation: AAA20657.1.
U03715 expand/collapse EMBL AC list , U34606, U34608, U34609, U34610, U34611, U34612, U34613, U03716, U03718 Genomic DNA. Translation: AAC52901.1.
U03715 expand/collapse EMBL AC list , U34607, U34608, U34609, U34610, U34611, U34612, U34613, U03716, U03718 Genomic DNA. Translation: AAC52902.1.
U03715 expand/collapse EMBL AC list , U03716, U03718, U34607, U34608, U34609, U34610, U34611, U34612, U34613 Genomic DNA. Translation: AAC52903.1.
AC055777 Genomic DNA. No translation available.
AC159334 Genomic DNA. No translation available.
BC064817 mRNA. Translation: AAH64817.1.
BC066080 mRNA. Translation: AAH66080.1.
L16898 mRNA. Translation: AAA37434.1.
AK031798 mRNA. Translation: BAC27554.1.
AK014292 mRNA. Translation: BAB29249.1.
U11636 mRNA. Translation: AAC52178.1.
U11637 mRNA. Translation: AAC52179.1.
L22545 mRNA. Translation: AAA19787.1.
D17546 mRNA. Translation: BAA04483.1.
AF257775 mRNA. Translation: AAF69009.1.
CCDSCCDS23953.1. [P39061-2]
CCDS48604.1. [P39061-1]
PIRA56101.
B56101.
RefSeqNP_001103461.1. NM_001109991.1. [P39061-1]
NP_034059.2. NM_009929.3. [P39061-2]
UniGeneMm.4352.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DY0X-ray2.20A1587-1774[»]
1DY1X-ray2.20A1587-1774[»]
1KOEX-ray1.50A1597-1768[»]
ProteinModelPortalP39061.
SMRP39061. Positions 376-474, 1463-1514, 1597-1768.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198812. 1 interaction.

PTM databases

PhosphoSiteP39061.

Proteomic databases

MaxQBP39061.
PaxDbP39061.
PRIDEP39061.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000081654; ENSMUSP00000080358; ENSMUSG00000001435. [P39061-2]
ENSMUST00000105409; ENSMUSP00000101049; ENSMUSG00000001435. [P39061-1]
GeneID12822.
KEGGmmu:12822.
UCSCuc007fvg.1. mouse. [P39061-1]
uc007fvh.2. mouse. [P39061-2]

Organism-specific databases

CTD80781.
MGIMGI:88451. Col18a1.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00710000106713.
HOVERGENHBG053241.
InParanoidP39061.
KOK06823.
OrthoDBEOG7NSB2B.
PhylomeDBP39061.
TreeFamTF315821.

Gene expression databases

ArrayExpressP39061.
BgeeP39061.
CleanExMM_COL18A1.
GenevestigatorP39061.

Family and domain databases

Gene3D1.10.2000.10. 1 hit.
2.60.120.200. 1 hit.
3.10.100.10. 1 hit.
InterProIPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR026917. COL18A1.
IPR008160. Collagen.
IPR010515. Collagenase_NC10/endostatin.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR010363. DUF959_COL18_N.
IPR020067. Frizzled_dom.
IPR001791. Laminin_G.
[Graphical view]
PANTHERPTHR24023:SF390. PTHR24023:SF390. 1 hit.
PfamPF01391. Collagen. 7 hits.
PF06121. DUF959. 1 hit.
PF06482. Endostatin. 1 hit.
PF01392. Fz. 1 hit.
[Graphical view]
SMARTSM00063. FRI. 1 hit.
SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
SSF56436. SSF56436. 1 hit.
SSF63501. SSF63501. 1 hit.
PROSITEPS50038. FZ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOL18A1. mouse.
EvolutionaryTraceP39061.
NextBio282298.
PMAP-CutDBP39061.
PROP39061.
SOURCESearch...

Entry information

Entry nameCOIA1_MOUSE
AccessionPrimary (citable) accession number: P39061
Secondary accession number(s): Q60672 expand/collapse secondary AC list , Q61434, Q61437, Q62001, Q62002, Q6NZK9, Q6P1Y4, Q8CCZ8, Q9CRT2, Q9JK63
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: May 1, 2007
Last modified: July 9, 2014
This is version 147 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot