PB0163
DATABASE


Click here to access PB0163 phyletic profile

PBID Uniprot Name Gene Alternative Organism Uniprot Description
PB0163 Q05707 Collagen alpha-1(XIV) chain COL14A1 UND, collagen type XIV alpha 1 chain Homo_sapiens 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).

DomainsGene Ontology
PF00041 (8_fn3)
PF00092 (2_VWA)
PF01391 (4_Collagen)
GO:0003723 (enables) RNA binding
GO:0005201 (enables) extracellular matrix structural constituent
GO:0005518 (enables) collagen binding
GO:0030020 (enables) extracellular matrix structural constituent conferring tensile strength
GO:0030674 (enables) protein-macromolecule adaptor activity
GO:0007155 (involved in) cell adhesion
GO:0030198 (involved in) extracellular matrix organization
GO:0030199 (involved in) collagen fibril organization
GO:0098609 (involved in) cell-cell adhesion
GO:0005614 (is active in) interstitial matrix
GO:0005615 (is active in) extracellular space
GO:0062023 (is active in) collagen-containing extracellular matrix
GO:0005576 (located in) extracellular region
GO:0005788 (located in) endoplasmic reticulum lumen
GO:0031012 (located in) extracellular matrix
GO:0005581 (part of) collagen trimer
GO:0005596 (part of) collagen type XIV trimer

External Links Description
Intact Open source database system and analysis tools for molecular interaction data.
Protein Atlas An open access resource for human proteins
InterPro (new pfam) InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites.

Seed proteins (Human and Zebrafish)

Selected proteins from model organisms

Mafft alignment of selected proteins

BMGE Cleaned alignment of selected proteins

PhyML tree of selected proteins

BLAST to find more sequences


Created by Puigbo and Nakamura @ University of Turku (2022)