Q05707 (COEA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 104.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Collagen alpha-1(XIV) chain Alternative name(s): Undulin | ||||
| Gene names |
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| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 1796 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Plays an adhesive role by integrating collagen bundles. It is probably associated with the surface of interstitial collagen fibrils via COL1. The COL2 domain may then serve as a rigid arm which sticks out from the fibril and protrudes the large N-terminal globular domain into the extracellular space, where it might interact with other matrix molecules or cell surface receptors By similarity. Ref.6 |
| Subunit structure | Homotrimer By similarity. UniProtKB P32018 |
| Subcellular location | Secreted › extracellular space › extracellular matrix By similarity. |
| Post-translational modification | Lysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in all cases and bind carbohydrates By similarity. UniProtKB P32018 Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains By similarity. UniProtKB P32018 May contain numerous cysteine residues involved in inter- and intramolecular disulfide bonding By similarity. UniProtKB P32018 |
| Sequence similarities | Belongs to the fibril-associated collagens with interrupted helices (FACIT) family. Contains 4 collagen-like domains. Contains 8 fibronectin type-III domains. Contains 1 laminin G-like domain. Contains 2 VWFA domains. |
| Sequence caution | The sequence AAA36795.1 differs from that shown. Reason: The sequence AAH14640.1 differs from that shown. Reason: Frameshift at position 1047. |
Ontologies
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 Ref.3 (identifier: Q05707-1) Also known as: Undulin 1; Un1; 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. | ||||||
| Isoform 2 Ref.3 (identifier: Q05707-2) The sequence of this isoform differs from the canonical sequence as follows: 1771-1796: APHPDQPEFTPVQDELEAMELWGPGV → DLIPYNDYQH | ||||||
| Isoform 3 Ref.4 (identifier: Q05707-3) Also known as: Undulin 2; Un2; The sequence of this isoform differs from the canonical sequence as follows: 197-291: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 28 | 28 | Potential | ||||||
| Chain | 29 – 1796 | 1768 | Collagen alpha-1(XIV) chain | PRO_0000005785 | |||||
Regions | |||||||||
| Domain | 29 – 117 | 89 | Fibronectin type-III 1 | ||||||
| Domain | 158 – 330 | 173 | VWFA 1 | ||||||
| Domain | 352 – 440 | 89 | Fibronectin type-III 2 | ||||||
| Domain | 442 – 532 | 91 | Fibronectin type-III 3 | ||||||
| Domain | 534 – 621 | 88 | Fibronectin type-III 4 | ||||||
| Domain | 623 – 712 | 90 | Fibronectin type-III 5 | ||||||
| Domain | 735 – 826 | 92 | Fibronectin type-III 6 | ||||||
| Domain | 828 – 917 | 90 | Fibronectin type-III 7 | ||||||
| Domain | 921 – 1005 | 85 | Fibronectin type-III 8 | ||||||
| Domain | 1032 – 1205 | 174 | VWFA 2 | ||||||
| Domain | 1229 – 1424 | 196 | Laminin G-like | ||||||
| Domain | 1462 – 1510 | 49 | Collagen-like 1 | ||||||
| Domain | 1514 – 1570 | 57 | Collagen-like 2 | ||||||
| Domain | 1571 – 1609 | 39 | Collagen-like 3 | ||||||
| Domain | 1653 – 1705 | 53 | Collagen-like 4 | ||||||
| Region | 1217 – 1458 | 242 | Nonhelical region (NC4) | ||||||
| Region | 1459 – 1610 | 152 | Triple-helical region 1 (COL2) | ||||||
| Region | 1654 – 1779 | 126 | Triple-helical region 2 (COL1) | ||||||
| Motif | 1607 – 1609 | 3 | Cell attachment site Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1467 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1470 | 1 | 4-hydroxyproline; partial Ref.5 | ||||||
| Modified residue | 1476 | 1 | 5-hydroxylysine Ref.5 | ||||||
| Modified residue | 1482 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1485 | 1 | 5-hydroxylysine; partial Ref.5 | ||||||
| Modified residue | 1497 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1503 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1517 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1520 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1523 | 1 | 5-hydroxylysine; partial Ref.5 | ||||||
| Modified residue | 1526 | 1 | 5-hydroxylysine; partial Ref.5 | ||||||
| Modified residue | 1532 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1538 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1544 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1550 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1556 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1565 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1568 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1574 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1577 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1580 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1595 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1598 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1601 | 1 | 5-hydroxylysine Ref.5 | ||||||
| Modified residue | 1643 | 1 | 4-hydroxyproline; partial Ref.5 | ||||||
| Modified residue | 1656 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1659 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1662 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1665 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1668 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1674 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1677 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1680 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1686 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1689 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1698 | 1 | 5-hydroxylysine Ref.5 | ||||||
| Modified residue | 1701 | 1 | 5-hydroxylysine Ref.5 | ||||||
| Modified residue | 1704 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1715 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1726 | 1 | 4-hydroxyproline; partial Ref.5 | ||||||
| Modified residue | 1729 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1732 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1735 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1741 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1747 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Modified residue | 1756 | 1 | 4-hydroxyproline Ref.5 | ||||||
| Glycosylation | 94 | 1 | N-linked (GlcNAc...) Ref.7 | ||||||
| Glycosylation | 137 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 372 | 1 | N-linked (GlcNAc...) Ref.7 | ||||||
| Glycosylation | 1384 | 1 | N-linked (GlcNAc...) Ref.7 | ||||||
| Glycosylation | 1388 | 1 | N-linked (GlcNAc...) Ref.7 | ||||||
| Glycosylation | 1476 | 1 | O-linked (Gal...) Ref.5 | ||||||
| Glycosylation | 1485 | 1 | O-linked (Gal...); partial Ref.5 | ||||||
| Glycosylation | 1523 | 1 | O-linked (Gal...); partial Ref.5 | ||||||
| Glycosylation | 1526 | 1 | O-linked (Gal...); partial Ref.5 | ||||||
| Glycosylation | 1601 | 1 | O-linked (Gal...) Ref.5 | ||||||
| Glycosylation | 1698 | 1 | O-linked (Gal...) Ref.5 | ||||||
| Glycosylation | 1701 | 1 | O-linked (Gal...); partial Ref.5 | ||||||
Natural variations | |||||||||
| Alternative sequence | 197 – 291 | 95 | Missing in isoform 3. Ref.4 | VSP_051653 | |||||
| Alternative sequence | 1771 – 1796 | 26 | APHPD…WGPGV → DLIPYNDYQH in isoform 2. Ref.3 | VSP_051654 | |||||
| Natural variant | 563 | 1 | N → H. Corresponds to variant rs4870723 [ dbSNP | Ensembl ]. | VAR_048772 | |||||
| Natural variant | 636 | 1 | T → A. Corresponds to variant rs56815167 [ dbSNP | Ensembl ]. | VAR_061113 | |||||
| Natural variant | 855 | 1 | P → L. Corresponds to variant rs2305606 [ dbSNP | Ensembl ]. | VAR_048773 | |||||
| Natural variant | 922 | 1 | V → I. Corresponds to variant rs11774228 [ dbSNP | Ensembl ]. | VAR_048774 | |||||
| Natural variant | 1342 | 1 | V → L. Ref.2 Corresponds to variant rs17833992 [ dbSNP | Ensembl ]. | VAR_048775 | |||||
Experimental info | |||||||||
| Sequence conflict | 616 | 1 | T → I in AAA36794. Ref.2 | ||||||
| Sequence conflict | 1025 | 1 | V → G in AAA36794. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "DNA sequence and analysis of human chromosome 8." Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. Lander E.S.Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [2] | "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 1), VARIANT LEU-1342. Tissue: Brain, Muscle and PNS. |
| [3] | "Complete primary structure of human collagen type XIV (undulin)." Bauer M., Dieterich W., Ehnis T., Schuppan D. Biochim. Biophys. Acta 1354:183-188(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-165, NUCLEOTIDE SEQUENCE [MRNA] OF 1026-1796 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 1760-1796 (ISOFORM 2). |
| [4] | "Undulin is a novel member of the fibronectin-tenascin family of extracellular matrix glycoproteins." Just M., Herbst H., Hummel M., Duerkop H., Tripier D., Stein H., Schuppan D. J. Biol. Chem. 266:17326-17332(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 149-582 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 188-1030 (ISOFORM 1). |
| [5] | "Structure and stability of the triple-helical domains of human collagen XIV." Brown J.C., Golbik R., Mann K., Timpl R. Matrix Biol. 14:287-295(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1459-1635 AND 1640-1767, HYDROXYLATION AT PRO-1467; PRO-1470; LYS-1476; PRO-1482; LYS-1485; PRO-1497; PRO-1503; PRO-1517; PRO-1520; LYS-1523; LYS-1526; PRO-1532; PRO-1538; PRO-1544; PRO-1550; PRO-1556; PRO-1565; PRO-1568; PRO-1574; PRO-1577; PRO-1580; PRO-1595; PRO-1598; LYS-1601; PRO-1643; PRO-1656; PRO-1659; PRO-1662; PRO-1665; PRO-1668; PRO-1674; PRO-1677; PRO-1680; PRO-1686; PRO-1689; LYS-1698; LYS-1701; PRO-1704; PRO-1715; PRO-1726; PRO-1729; PRO-1732; PRO-1735; PRO-1741; PRO-1747 AND PRO-1756, GLYCOSYLATION AT LYS-1476; LYS-1485; LYS-1523; LYS-1526; LYS-1601; LYS-1698 AND LYS-1701. Tissue: Placenta. |
| [6] | "Undulin, an extracellular matrix glycoprotein associated with collagen fibrils." Schuppan D., Cantaluppi M., Becker J., Veit A., Bunte T., Troyer D., Schuppan F., Schmid M., Ackermann R., Hahn E. J. Biol. Chem. 265:8823-8832(1990) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. |
| [7] | "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-94; ASN-372; ASN-1384 AND ASN-1388, MASS SPECTROMETRY. Tissue: Liver. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AC020603 Genomic DNA. No translation available. AC090735 Genomic DNA. No translation available. AC107877 Genomic DNA. No translation available. BC014640 mRNA. Translation: AAH14640.1. Frameshift. BC083495 mRNA. Translation: AAH83495.1. BC140893 mRNA. Translation: AAI40894.1. Y11709 mRNA. Translation: CAA72401.1. Y11710 mRNA. Translation: CAA72402.1. Y11711 mRNA. Translation: CAA72403.1. M64108 mRNA. Translation: AAA36794.1. M64109 mRNA. Translation: AAA36795.1. Sequence problems. |
| IPI | IPI00176193. IPI00402215. IPI00550918. |
| PIR | A40970. B40970. S37749. S46657. |
| RefSeq | NP_066933.1. NM_021110.2. |
| UniGene | Hs.409662. |
3D structure databases | |
| ProteinModelPortal | Q05707. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q05707. 2 interactions. |
PTM databases | |
| PhosphoSite | Q05707. |
Polymorphism databases | |
| DMDM | 125987815. |
Proteomic databases | |
| PaxDb | Q05707. |
| PRIDE | Q05707. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000247781; ENSP00000247781; ENSG00000187955. ENST00000297848; ENSP00000297848; ENSG00000187955. ENST00000309791; ENSP00000311809; ENSG00000187955. |
| GeneID | 7373. |
| KEGG | hsa:7373. |
| UCSC | uc003yox.3. human. |
Organism-specific databases | |
| CTD | 7373. |
| GeneCards | GC08P121093. |
| H-InvDB | HIX0007753. |
| HGNC | HGNC:2191. COL14A1. |
| HPA | HPA023781. |
| MIM | 120324. gene. |
| neXtProt | NX_Q05707. |
| PharmGKB | PA26707. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | NOG307460. |
| HOVERGEN | HBG051060. |
| InParanoid | Q05707. |
| KO | K08133. |
| OMA | VYNVAEF. |
| OrthoDB | EOG4PC9R7. |
Enzyme and pathway databases | |
| Reactome | REACT_118779. Extracellular matrix organization. |
Gene expression databases | |
| ArrayExpress | Q05707. |
| Bgee | Q05707. |
| CleanEx | HS_COL14A1. |
| Genevestigator | Q05707. |
| GermOnline | ENSG00000187955. Homo sapiens. |
Family and domain databases | |
| Gene3D | 2.60.40.10. 8 hits. |
| InterPro | IPR008160. Collagen. IPR008985. ConA-like_lec_gl_sf. IPR003961. Fibronectin_type3. IPR013783. Ig-like_fold. IPR001791. Laminin_G. IPR002035. VWF_A. [Graphical view] |
| Pfam | PF01391. Collagen. 4 hits. PF00041. fn3. 8 hits. PF00092. VWA. 2 hits. [Graphical view] |
| SMART | SM00060. FN3. 8 hits. SM00210. TSPN. 1 hit. SM00327. VWA. 2 hits. [Graphical view] |
| SUPFAM | SSF49899. ConA_like_lec_gl. 1 hit. SSF49265. FN_III-like. 8 hits. |
| PROSITE | PS50853. FN3. 8 hits. PS50025. LAM_G_DOMAIN. False negative. PS50234. VWFA. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | COL14A1. human. |
| GenomeRNAi | 7373. |
| NextBio | 28870. |
| SOURCE | Search... |
Entry information
| Entry name | COEA1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q05707 Secondary accession number(s): B2RU07 Q9UDF6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 8 Human chromosome 8: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
