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Protein

Collagen alpha-1(XIV) chain

Gene

COL14A1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(XIV) chain
Alternative name(s):
Undulin
Gene namesi
Name:COL14A1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Chaini29 – 18881860Collagen alpha-1(XIV) chainPRO_0000005787Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi138 – 1381N-linked (GlcNAc...)Sequence analysis
Glycosylationi1398 – 13981N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Lysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in all cases and bind carbohydrates.
Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
May contain numerous cysteine residues involved in inter- and intramolecular disulfide bonding.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiP32018.
PRIDEiP32018.

Expressioni

Tissue specificityi

Wide tissue distribution; high presence in dense connective tissue in skeletal muscle.

Interactioni

Subunit structurei

Homotrimer.Curated

Protein-protein interaction databases

STRINGi9031.ENSGALP00000026422.

Structurei

Secondary structure

1
1888
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1854 – 18574Combined sources
Turni1859 – 18613Combined sources
Helixi1862 – 188019Combined sources
Beta strandi1881 – 18833Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B9PNMR-A1852-1885[»]
1B9QNMR-A1852-1885[»]
ProteinModelPortaliP32018.
SMRiP32018. Positions 1853-1885.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32018.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 12392Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini158 – 330173VWFA 1PROSITE-ProRule annotationAdd
BLAST
Domaini355 – 44490Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini445 – 53692Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini537 – 62791Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini628 – 71689Fibronectin type-III 5PROSITE-ProRule annotationAdd
BLAST
Domaini744 – 83390Fibronectin type-III 6PROSITE-ProRule annotationAdd
BLAST
Domaini835 – 92591Fibronectin type-III 7PROSITE-ProRule annotationAdd
BLAST
Domaini926 – 101792Fibronectin type-III 8PROSITE-ProRule annotationAdd
BLAST
Domaini1042 – 1215174VWFA 2PROSITE-ProRule annotationAdd
BLAST
Domaini1239 – 1434196Laminin G-likeAdd
BLAST
Domaini1468 – 152053Collagen-like 1Add
BLAST
Domaini1524 – 157956Collagen-like 2Add
BLAST
Domaini1580 – 161839Collagen-like 3Add
BLAST
Domaini1664 – 171552Collagen-like 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1227 – 1468242Nonhelical region (NC4)Add
BLAST
Regioni1469 – 1620152Triple-helical region 1 (COL2)Add
BLAST
Regioni1664 – 1786123Triple-helical region 2 (COL1)Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1489 – 14913Cell attachment siteSequence analysis
Motifi1617 – 16193Cell attachment siteSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi721 – 73313Poly-ThrAdd
BLAST

Sequence similaritiesi

Contains 4 collagen-like domains.Curated
Contains 8 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 laminin G-like domain.Curated
Contains 2 VWFA domains.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG1217. Eukaryota.
KOG3544. Eukaryota.
ENOG410Y01G. LUCA.
HOVERGENiHBG051060.
InParanoidiP32018.
KOiK08133.
PhylomeDBiP32018.

Family and domain databases

Gene3Di2.60.40.10. 8 hits.
3.40.50.410. 2 hits.
InterProiIPR008160. Collagen.
IPR013320. ConA-like_dom.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR001791. Laminin_G.
IPR002035. VWF_A.
[Graphical view]
PfamiPF01391. Collagen. 4 hits.
PF00041. fn3. 7 hits.
PF00092. VWA. 2 hits.
[Graphical view]
SMARTiSM00060. FN3. 8 hits.
SM00210. TSPN. 1 hit.
SM00327. VWA. 2 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 7 hits.
SSF49899. SSF49899. 1 hit.
SSF53300. SSF53300. 2 hits.
PROSITEiPS50853. FN3. 8 hits.
PS50234. VWFA. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32018-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLCWNEVQSC FLLAFLAVAA YSVSDAQGQV SPPTRLRYNV VNPDSVQISW
60 70 80 90 100
KAPKGQFSGY KLLVTPSSGG KTNQLILQNT ATKAIIQGLI PDQNYALQII
110 120 130 140 150
AFSDDKESKP AQGQFRIKDI ERRKETSKSK VKDPEKTNAS KPTPEGNLFT
160 170 180 190 200
CKTPAIADIV ILVDGSWSIG RFNFRLVRLF LENLVSAFNV GSEKTRVGLA
210 220 230 240 250
QYSGDPRIEW HLNAYGTKDA VLDAVRNLPY KGGNTLTGLA LTYILENSFK
260 270 280 290 300
PEAGARPGVS KIGILITDGK SQDDVIPPAK NLRDAGIELF AIGVKNADIN
310 320 330 340 350
ELKEIASEPD STHVYNVADF NFMNSIVEGL TRTVCSRVEE QEKEIKGTIA
360 370 380 390 400
ASLGAPTDLV TSDITARGFR VSWTHSPGKV EKYRVVYYPT RGGQPEEVVV
410 420 430 440 450
DGSSSTAVLK NLMSLTEYQI AVFAIYSNAA SEGLRGTETT LALPMASDLK
460 470 480 490 500
LYDVSHSSMR AKWNGVAGAT GYMILYAPLT EGLAADEKEI KIGEASTELE
510 520 530 540 550
LDGLLPNTEY TVTVYAMFGE EASDPLTGQE TTLPLSPPSN LKFSDVGHNS
560 570 580 590 600
AKLTWDPASK NVKGYRIMYV KTDGTETNEV EVGPVSTHTL KSLTALTEYT
610 620 630 640 650
VAIFSLYDEG QSEPLTGSFT TRKVPPPQHL EVDEASTDSF RVSWKPTSSD
660 670 680 690 700
IAFYRLAWIP LDGGESEEVV LSGDADSYVI EGLLPNTEYE VSLLAVFDDE
710 720 730 740 750
TESEVVAVLG ATIVGTTAIP TTVTTTTTTT ATTPKPTIAV FRTGVRNLVI
760 770 780 790 800
DDETTSSLRV VWDISDHNAQ QFRVTYLTAK GDRAEEAIMV PGRQNTLLLQ
810 820 830 840 850
PLLPDTEYKV TITPIYADGE GVSVSAPGKT LPLSAPRNLR VSDEWYNRLR
860 870 880 890 900
ISWDAPPSPT MGYRIVYKSI NVPGPALETF VGDDINTILI LNLFSGTEYS
910 920 930 940 950
VKVFASYSTG FSDALTGVAK TLYLGVTNLD TYQVRMTSLC AQWQLHRHAT
960 970 980 990 1000
AYRVVIESLV DGKKQEVNLG GGVPRHCFFE LMPGTEYKIS VHAQLQEIEG
1010 1020 1030 1040 1050
PAVSIMETTL PFPTQPPTSP STTLPPPTIP PAKEVCKAAK ADLVFLVDGS
1060 1070 1080 1090 1100
WSIGDDNFNK IISFLYSTVG ALDKIGPDGT QVAIIQFSDD PRTEFKLNAY
1110 1120 1130 1140 1150
KTKETLLEAI QQIAYKGGNT KTGKAIKHAR EVLFTGEAGM RKGIPKVLVV
1160 1170 1180 1190 1200
ITDGRSQDDV NKVSREMQLD GFSFFAIGVA DADYSELVNI GSKPSERHVF
1210 1220 1230 1240 1250
FVDDFDAFTK IEDELITFVC ETASATCPLV FKDGDKLAGF KMMEMFGLVE
1260 1270 1280 1290 1300
KEFSAIDGVS MEPGTFNVYP CYRLHKDALV SQPTKYLHPE GLPSDYTITF
1310 1320 1330 1340 1350
LFRILPDTPQ EPFALWEILN EQYEPLVGVI LDNGGKTLTF FNYDYKGDFQ
1360 1370 1380 1390 1400
TVTFEGPEIR KIFYGSFHKL HVVISKTTAK IIIDCKEAGE KTINAAGNIS
1410 1420 1430 1440 1450
SDGIEVLGRM VRSRGPRDNS APLQLQMFDI VCATSWANRD KCCELPGLRD
1460 1470 1480 1490 1500
EENCPALPHA CSCSEANKGP LGPPGPPGGP GVRGAKGHRG DPGPKGPDGP
1510 1520 1530 1540 1550
RGEIGVPGPQ GPPGPQGPSG LSIQGLPGPP GEKGEKGDLG FPGLQGVPGA
1560 1570 1580 1590 1600
SGSPGRDGAQ GQRGLPGKDG PTGPQGPPGP VGIPGAPGVP GITGSQGPQG
1610 1620 1630 1640 1650
DVGAPGAPGP KGERGERGDL QSQAMVRAVA RQVCEQLIQG HMARYNSILN
1660 1670 1680 1690 1700
QIPSQSVSTR TIAGPPGEPG RPGAPGPQGE QGSPGMQGFP GNPGQPGRPG
1710 1720 1730 1740 1750
ERGLPGEKGD RGNPGVGTQG PRGPPGSTGP PGESRTGSPG PPGSPGPRGP
1760 1770 1780 1790 1800
AGHTGPPGSQ GPAGPPGYCD PSSCAGYGMG GGYGEPTDQD IPVVQLPHNS
1810 1820 1830 1840 1850
YQIYDPEDLY DGEQQPYVVH GSYPLPSPYS QSSYPSPHLA QPEFTPVREE
1860 1870 1880
MEAVELRSPG ISRFRRKIAK RSIKTLEHKR ENAKEPSQ
Length:1,888
Mass (Da):202,668
Last modified:October 1, 1996 - v2
Checksum:i39915BB9F46DD873
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70793 mRNA. Translation: CAA50064.1.
X70792 mRNA. Translation: CAA50063.1.
X66138 mRNA. Translation: CAA46928.2.
X65122 mRNA. Translation: CAA46238.1.
PIRiA45974.
S31212.
S78476.
RefSeqiNP_990665.1. NM_205334.1.
UniGeneiGga.13901.
Gga.5089.

Genome annotation databases

GeneIDi396276.
KEGGigga:396276.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70793 mRNA. Translation: CAA50064.1.
X70792 mRNA. Translation: CAA50063.1.
X66138 mRNA. Translation: CAA46928.2.
X65122 mRNA. Translation: CAA46238.1.
PIRiA45974.
S31212.
S78476.
RefSeqiNP_990665.1. NM_205334.1.
UniGeneiGga.13901.
Gga.5089.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B9PNMR-A1852-1885[»]
1B9QNMR-A1852-1885[»]
ProteinModelPortaliP32018.
SMRiP32018. Positions 1853-1885.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000026422.

Proteomic databases

PaxDbiP32018.
PRIDEiP32018.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396276.
KEGGigga:396276.

Organism-specific databases

CTDi7373.

Phylogenomic databases

eggNOGiKOG1217. Eukaryota.
KOG3544. Eukaryota.
ENOG410Y01G. LUCA.
HOVERGENiHBG051060.
InParanoidiP32018.
KOiK08133.
PhylomeDBiP32018.

Miscellaneous databases

EvolutionaryTraceiP32018.
NextBioi20816327.
PROiP32018.

Family and domain databases

Gene3Di2.60.40.10. 8 hits.
3.40.50.410. 2 hits.
InterProiIPR008160. Collagen.
IPR013320. ConA-like_dom.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR001791. Laminin_G.
IPR002035. VWF_A.
[Graphical view]
PfamiPF01391. Collagen. 4 hits.
PF00041. fn3. 7 hits.
PF00092. VWA. 2 hits.
[Graphical view]
SMARTiSM00060. FN3. 8 hits.
SM00210. TSPN. 1 hit.
SM00327. VWA. 2 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 7 hits.
SSF49899. SSF49899. 1 hit.
SSF53300. SSF53300. 2 hits.
PROSITEiPS50853. FN3. 8 hits.
PS50234. VWFA. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryo.
  2. "Type XIV collagen is a variant of undulin."
    Trueb J., Trueb B.
    Eur. J. Biochem. 207:549-557(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 402-1549.
  3. "Cloning of the cDNA for a new member of the class of fibril-associated collagens with interrupted triple helices."
    Gordon M., Castagnola P., Dublet B., Linsenmayer T.F., van der Rest M., Mayne R., Olsen B.R.
    Eur. J. Biochem. 201:333-338(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1582-1770.
  4. Apte S.S.
    Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1582-1770.
  5. "Identification and characterization of a heparin binding site within the NC1 domain of chicken collagen XIV."
    Giry-Lozinguez C., Aubert-Foucher E., Penin F., Deleage G., Dublet B., van der Rest M.
    Matrix Biol. 17:145-149(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1853-1885.
  6. "Structural analysis of the heparin-binding site of the NC1 domain of collagen XIV by CD and NMR."
    Montserret R., Aubert-Foucher E., McLeish M.J., Hill J.M., Ficheux D., Jaquinod M., van der Rest M., Deleage G., Penin F.
    Biochemistry 38:6479-6488(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1852-1885.

Entry informationi

Entry nameiCOEA1_CHICK
AccessioniPrimary (citable) accession number: P32018
Secondary accession number(s): Q6LBL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 1, 1996
Last modified: April 13, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.