COEA1_CHICK
ID COEA1_CHICK Reviewed; 1888 AA.
AC P32018; Q6LBL0;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Collagen alpha-1(XIV) chain;
DE AltName: Full=Undulin;
DE Flags: Precursor;
GN Name=COL14A1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=8444186; DOI=10.1111/j.1432-1033.1993.tb17685.x;
RA Waelchli C., Trueb J., Kessler B., Winterhalter K.H., Trueb B.;
RT "Complete primary structure of chicken collagen XIV.";
RL Eur. J. Biochem. 212:483-490(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 402-1549.
RX PubMed=1339349; DOI=10.1111/j.1432-1033.1992.tb17081.x;
RA Trueb J., Trueb B.;
RT "Type XIV collagen is a variant of undulin.";
RL Eur. J. Biochem. 207:549-557(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1582-1770.
RX PubMed=1935930; DOI=10.1111/j.1432-1033.1991.tb16290.x;
RA Gordon M., Castagnola P., Dublet B., Linsenmayer T.F., van der Rest M.,
RA Mayne R., Olsen B.R.;
RT "Cloning of the cDNA for a new member of the class of fibril-associated
RT collagens with interrupted triple helices.";
RL Eur. J. Biochem. 201:333-338(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1582-1770.
RA Apte S.S.;
RL Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP STRUCTURE BY NMR OF 1853-1885.
RX PubMed=9694594; DOI=10.1016/s0945-053x(98)90027-0;
RA Giry-Lozinguez C., Aubert-Foucher E., Penin F., Deleage G., Dublet B.,
RA van der Rest M.;
RT "Identification and characterization of a heparin binding site within the
RT NC1 domain of chicken collagen XIV.";
RL Matrix Biol. 17:145-149(1998).
RN [6]
RP STRUCTURE BY NMR OF 1852-1885.
RX PubMed=10350466; DOI=10.1021/bi9900222;
RA Montserret R., Aubert-Foucher E., McLeish M.J., Hill J.M., Ficheux D.,
RA Jaquinod M., van der Rest M., Deleage G., Penin F.;
RT "Structural analysis of the heparin-binding site of the NC1 domain of
RT collagen XIV by CD and NMR.";
RL Biochemistry 38:6479-6488(1999).
CC -!- FUNCTION: An adhesive role by integrating collagen bundles. It is
CC probably associated with the surface of interstitial collagen fibrils
CC via COL1. The COL2 domain may then serve as a rigid arm which sticks
CC out from the fibril and protrudes the large N-terminal globular domain
CC into the extracellular space, where it might interact with other matrix
CC molecules or cell surface receptors.
CC -!- SUBUNIT: Homotrimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: Wide tissue distribution; high presence in dense
CC connective tissue in skeletal muscle.
CC -!- PTM: Lysines at the third position of the tripeptide repeating unit (G-
CC X-Y) are hydroxylated in all cases and bind carbohydrates.
CC -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) are hydroxylated in some or all of the chains.
CC -!- PTM: May contain numerous cysteine residues involved in inter- and
CC intramolecular disulfide bonding.
CC -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted
CC helices (FACIT) family. {ECO:0000305}.
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DR EMBL; X70793; CAA50064.1; -; mRNA.
DR EMBL; X70792; CAA50063.1; -; mRNA.
DR EMBL; X66138; CAA46928.2; -; mRNA.
DR EMBL; X65122; CAA46238.1; -; mRNA.
DR PIR; A45974; A45974.
DR PIR; S31212; S31212.
DR PIR; S78476; S78476.
DR RefSeq; NP_990665.1; NM_205334.1.
DR PDB; 1B9P; NMR; -; A=1852-1885.
DR PDB; 1B9Q; NMR; -; A=1852-1885.
DR PDBsum; 1B9P; -.
DR PDBsum; 1B9Q; -.
DR AlphaFoldDB; P32018; -.
DR SMR; P32018; -.
DR ComplexPortal; CPX-3110; Collagen type XIV trimer.
DR STRING; 9031.ENSGALP00000026419; -.
DR PaxDb; P32018; -.
DR GeneID; 396276; -.
DR KEGG; gga:396276; -.
DR CTD; 7373; -.
DR VEuPathDB; HostDB:geneid_396276; -.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; P32018; -.
DR OrthoDB; 67372at2759; -.
DR PhylomeDB; P32018; -.
DR EvolutionaryTrace; P32018; -.
DR PRO; PR:P32018; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 7.
DR Gene3D; 2.60.40.10; -; 8.
DR Gene3D; 3.40.50.410; -; 2.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF00041; fn3; 7.
DR Pfam; PF00092; VWA; 2.
DR SMART; SM00060; FN3; 8.
DR SMART; SM00210; TSPN; 1.
DR SMART; SM00327; VWA; 2.
DR SUPFAM; SSF49265; SSF49265; 7.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF53300; SSF53300; 2.
DR PROSITE; PS50853; FN3; 8.
DR PROSITE; PS50234; VWFA; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Collagen; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydroxylation; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1888
FT /note="Collagen alpha-1(XIV) chain"
FT /id="PRO_0000005787"
FT DOMAIN 32..123
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 158..330
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 355..444
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 445..536
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 537..627
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 628..716
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 744..833
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 835..925
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 926..1017
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1042..1215
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1239..1434
FT /note="Laminin G-like"
FT DOMAIN 1468..1520
FT /note="Collagen-like 1"
FT DOMAIN 1524..1579
FT /note="Collagen-like 2"
FT DOMAIN 1580..1618
FT /note="Collagen-like 3"
FT DOMAIN 1664..1715
FT /note="Collagen-like 4"
FT REGION 110..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1227..1468
FT /note="Nonhelical region (NC4)"
FT REGION 1469..1620
FT /note="Triple-helical region 1 (COL2)"
FT REGION 1472..1620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1654..1767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1664..1786
FT /note="Triple-helical region 2 (COL1)"
FT REGION 1817..1841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1489..1491
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1617..1619
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 110..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1571..1585
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1735..1752
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1825..1839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 1854..1857
FT /evidence="ECO:0007829|PDB:1B9Q"
FT TURN 1859..1861
FT /evidence="ECO:0007829|PDB:1B9P"
FT HELIX 1862..1880
FT /evidence="ECO:0007829|PDB:1B9P"
FT STRAND 1881..1883
FT /evidence="ECO:0007829|PDB:1B9Q"
SQ SEQUENCE 1888 AA; 202668 MW; 39915BB9F46DD873 CRC64;
MLCWNEVQSC FLLAFLAVAA YSVSDAQGQV SPPTRLRYNV VNPDSVQISW KAPKGQFSGY
KLLVTPSSGG KTNQLILQNT ATKAIIQGLI PDQNYALQII AFSDDKESKP AQGQFRIKDI
ERRKETSKSK VKDPEKTNAS KPTPEGNLFT CKTPAIADIV ILVDGSWSIG RFNFRLVRLF
LENLVSAFNV GSEKTRVGLA QYSGDPRIEW HLNAYGTKDA VLDAVRNLPY KGGNTLTGLA
LTYILENSFK PEAGARPGVS KIGILITDGK SQDDVIPPAK NLRDAGIELF AIGVKNADIN
ELKEIASEPD STHVYNVADF NFMNSIVEGL TRTVCSRVEE QEKEIKGTIA ASLGAPTDLV
TSDITARGFR VSWTHSPGKV EKYRVVYYPT RGGQPEEVVV DGSSSTAVLK NLMSLTEYQI
AVFAIYSNAA SEGLRGTETT LALPMASDLK LYDVSHSSMR AKWNGVAGAT GYMILYAPLT
EGLAADEKEI KIGEASTELE LDGLLPNTEY TVTVYAMFGE EASDPLTGQE TTLPLSPPSN
LKFSDVGHNS AKLTWDPASK NVKGYRIMYV KTDGTETNEV EVGPVSTHTL KSLTALTEYT
VAIFSLYDEG QSEPLTGSFT TRKVPPPQHL EVDEASTDSF RVSWKPTSSD IAFYRLAWIP
LDGGESEEVV LSGDADSYVI EGLLPNTEYE VSLLAVFDDE TESEVVAVLG ATIVGTTAIP
TTVTTTTTTT ATTPKPTIAV FRTGVRNLVI DDETTSSLRV VWDISDHNAQ QFRVTYLTAK
GDRAEEAIMV PGRQNTLLLQ PLLPDTEYKV TITPIYADGE GVSVSAPGKT LPLSAPRNLR
VSDEWYNRLR ISWDAPPSPT MGYRIVYKSI NVPGPALETF VGDDINTILI LNLFSGTEYS
VKVFASYSTG FSDALTGVAK TLYLGVTNLD TYQVRMTSLC AQWQLHRHAT AYRVVIESLV
DGKKQEVNLG GGVPRHCFFE LMPGTEYKIS VHAQLQEIEG PAVSIMETTL PFPTQPPTSP
STTLPPPTIP PAKEVCKAAK ADLVFLVDGS WSIGDDNFNK IISFLYSTVG ALDKIGPDGT
QVAIIQFSDD PRTEFKLNAY KTKETLLEAI QQIAYKGGNT KTGKAIKHAR EVLFTGEAGM
RKGIPKVLVV ITDGRSQDDV NKVSREMQLD GFSFFAIGVA DADYSELVNI GSKPSERHVF
FVDDFDAFTK IEDELITFVC ETASATCPLV FKDGDKLAGF KMMEMFGLVE KEFSAIDGVS
MEPGTFNVYP CYRLHKDALV SQPTKYLHPE GLPSDYTITF LFRILPDTPQ EPFALWEILN
EQYEPLVGVI LDNGGKTLTF FNYDYKGDFQ TVTFEGPEIR KIFYGSFHKL HVVISKTTAK
IIIDCKEAGE KTINAAGNIS SDGIEVLGRM VRSRGPRDNS APLQLQMFDI VCATSWANRD
KCCELPGLRD EENCPALPHA CSCSEANKGP LGPPGPPGGP GVRGAKGHRG DPGPKGPDGP
RGEIGVPGPQ GPPGPQGPSG LSIQGLPGPP GEKGEKGDLG FPGLQGVPGA SGSPGRDGAQ
GQRGLPGKDG PTGPQGPPGP VGIPGAPGVP GITGSQGPQG DVGAPGAPGP KGERGERGDL
QSQAMVRAVA RQVCEQLIQG HMARYNSILN QIPSQSVSTR TIAGPPGEPG RPGAPGPQGE
QGSPGMQGFP GNPGQPGRPG ERGLPGEKGD RGNPGVGTQG PRGPPGSTGP PGESRTGSPG
PPGSPGPRGP AGHTGPPGSQ GPAGPPGYCD PSSCAGYGMG GGYGEPTDQD IPVVQLPHNS
YQIYDPEDLY DGEQQPYVVH GSYPLPSPYS QSSYPSPHLA QPEFTPVREE MEAVELRSPG
ISRFRRKIAK RSIKTLEHKR ENAKEPSQ
