CODA1_HUMAN » Collagen alpha-1(XIII) chain

CODA1_HUMAN » Collagen alpha-1(XIII) chain
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
CODA1_HUMAN » Collagen alpha-1(XIII) chain » COLXIIIA1;
Hydrophobic Thickness 30.8 ± 3.1 Å
Tilt Angle 1 ± 1°
ΔGtransfer -15.4 kcal/mol
ΔGfold -9.2 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, HMDB
Topology In
TM Segments 44-65 (44-65)
Pathways

Extracellular matrix organization (Reactome)

Protein digestion and absorption (KEGG)

PDB none
OPM none
Complexes none
Interactions

ITA1, Complex: CODA1:ITA1, PubMed

Domains

AA: 156-216, PDBID: 2JG8, Subunit B, Seq Identity:46%, Collagen triple helix repeat (20 copies)

AA: 257-322, PDBID: 2JG8, Subunit C, Seq Identity:42%, Collagen triple helix repeat (20 copies)

AA: 285-340, PDBID: 2JG8, Subunit B, Seq Identity:43%, Collagen triple helix repeat (20 copies)

AA: 318-383, PDBID: 2JG8, Subunit B, Seq Identity:45%, Collagen triple helix repeat (20 copies)

AA: 382-441, PDBID: 1M7L, Subunit A, Seq Identity:47%, Collagen triple helix repeat (20 copies)

AA: 463-522, PDBID: 3GXE, Subunit F, Seq Identity:51%, Collagen triple helix repeat (20 copies)

AA: 506-567, PDBID: 3GXE, Subunit F, Seq Identity:42%, Collagen triple helix repeat (20 copies)

AA: 566-625, PDBID: 3GXE, Subunit F, Seq Identity:43%, Collagen triple helix repeat (20 copies)

AA: 643-712, PDBID: 1M7L, Subunit A, Seq Identity:37%, Collagen triple helix repeat (20 copies)

UniProt annotation for CODA1_HUMAN » Collagen alpha-1(XIII) chain
FUNCTION: Involved in cell-matrix and cell-cell adhesion interactions that are required for normal development. May participate in the linkage between muscle fiber and basement membrane. May play a role in endochondral ossification of bone and branching morphogenesis of lung. Binds heparin.

SUBUNIT: Homotrimer; disulfide-linked. Nucleation of the type XIII collagen triple helix is likely to occur at the N-terminal region with triple helix formation proceeding from the N- to the C- terminus. Interacts with FN1, perlecan/HSPG2 and NID2.

TISSUE SPECIFICITY: Widely expressed in both fetal and adult ocular tissues (at protein level). In the eye, expression is accentuated in the ciliary muscle, optic nerve and the neural retina. In early placenta, localized to fibroblastoid stromal cells of the placental villi, to endothelial cells of developing capillaries and to cells of the cytotrophoblastic columns. Also detected in large decidual cells of the decidual membrane and to stromal cells of the gestational endometrium, but not in the epithelial cells in the endometrial glands.

UniProt features for CODA1_HUMAN » Collagen alpha-1(XIII) chain
CHAIN 1 717 Collagen alpha-1(XIII) chain.
REGION 1 121 Nonhelical region 1 (NC1).
REGION 122 216 Triple-helical region 1 (COL1).
REGION 217 269 Nonhelical region 2 (NC2).
REGION 270 441 Triple-helical region 2 (COL2).
REGION 442 463 Nonhelical region 3 (NC3).
REGION 464 699 Triple-helical region 3 (COL3).
REGION 700 717 Nonhelical region 4 (NC4).
Amino Acid Sequence for CODA1_HUMAN » Collagen alpha-1(XIII) chain
MVAERTHKAA ATGARGPGEL GAPGTVALVA ARAERGARLP SPGSCGLLTL ALCSLALSLL AHFRTAELQA RVLRLEAERG EQQMETAILG RVNQLLDEKW KLHSRRRREA PKTSPGCNCP PGPPGPTGRP GLPGDKGAIG MPGRVGSPGD AGLSIIGPRG PPGQPGTRGF PGFPGPIGLD GKPGHPGPKG DMGLTGPPGQ PGPQGQKGEK GQCGEYPHRE CLSSMPAALR SSQIIALKLL PLLNSVRLAP PPVIKRRTFQ GEQSQASIQG PPGPPGPPGP SGPLGHPGLP GPMGPPGLPG PPGPKGDPGI QGYHGRKGER GMPGMPGKHG AKGAPGIAVA GMKGEPGIPG TKGEKGAEGS PGLPGLLGQK GEKGDAGNSI GGGRGEPGPP GLPGPPGPKG EAGVDGQVGP PGQPGDKGER GAAGEQGPDG PKGSKGEPGK GEMVDYNGNI NEALQEIRTL ALMGPPGLPG QIGPPGAPGI PGQKGEIGLP GPPGHDGEKG PRGKPGDMGP PGPQGPPGKD GPPGVKGENG HPGSPGEKGE KGETGQAGSP GEKGEAGEKG NPGAEVPGLP GPEGPPGPPG LQGVPGPKGE AGLDGAKGEK GFQGEKGDRG PLGLPGASGL DGRPGPPGTP GPIGVPGPAG PKGERGSKGD PGMTGPTGAA GLPGLHGPPG DKGNRGERGK KGSRGPKGDK GDQGAPGLDA PCPLGEDGLP VQGCWNK