COEA1_MOUSE
ID COEA1_MOUSE Reviewed; 1797 AA.
AC Q80X19; Q3UVS2; Q8C6X3; Q9WV05;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Collagen alpha-1(XIV) chain;
DE Flags: Precursor;
GN Name=Col14a1 {ECO:0000312|MGI:MGI:1341272};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAO64442.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=CD-1 {ECO:0000312|EMBL:AAO64442.1};
RC TISSUE=Tendon {ECO:0000269|PubMed:12853031};
RX PubMed=12853031; DOI=10.1016/s0945-053x(03)00021-0;
RA Gerecke D.R., Meng X., Liu B., Birk D.E.;
RT "Complete primary structure and genomic organization of the mouse Col14a1
RT gene.";
RL Matrix Biol. 22:209-216(2003).
RN [2]
RP ERRATUM OF PUBMED:12853031.
RX PubMed=15065570; DOI=10.1016/j.matbio.2003.11.005;
RA Gerecke D.R., Meng X., Liu B., Birk D.E.;
RL Matrix Biol. 22:595-601(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1047-1797 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1262-1797 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5] {ECO:0000305, ECO:0000312|EMBL:CAB44661.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1672-1797 (ISOFORM 1).
RC TISSUE=Heart {ECO:0000312|EMBL:CAB44661.1};
RX PubMed=10393435; DOI=10.1159/000015262;
RA Imhof M., Trueb B.;
RT "Comparative cytogenetic mapping of the gene for human and mouse collagen
RT XIV.";
RL Cytogenet. Cell Genet. 84:217-219(1999).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Plays 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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P32018}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P32018}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:12853031};
CC IsoId=Q80X19-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q80X19-2; Sequence=VSP_051652;
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 {ECO:0000250|UniProtKB:P32018}.
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 {ECO:0000250|UniProtKB:P32018}.
CC -!- PTM: May contain numerous cysteine residues involved in inter- and
CC intramolecular disulfide bonding. {ECO:0000250|UniProtKB:P32018}.
CC -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted
CC helices (FACIT) family. {ECO:0000255}.
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DR EMBL; AY221110; AAO64442.1; -; mRNA.
DR EMBL; AC131337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC133156; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK052963; BAC35222.1; -; mRNA.
DR EMBL; AK136987; BAE23197.1; -; mRNA.
DR EMBL; AJ131395; CAB44661.1; -; mRNA.
DR CCDS; CCDS88765.1; -. [Q80X19-1]
DR RefSeq; XP_006520447.1; XM_006520384.3.
DR RefSeq; XP_006520448.1; XM_006520385.3. [Q80X19-2]
DR AlphaFoldDB; Q80X19; -.
DR SMR; Q80X19; -.
DR BioGRID; 198809; 4.
DR ComplexPortal; CPX-2992; Collagen type XIV trimer.
DR STRING; 10090.ENSMUSP00000105846; -.
DR GlyGen; Q80X19; 5 sites.
DR iPTMnet; Q80X19; -.
DR PhosphoSitePlus; Q80X19; -.
DR jPOST; Q80X19; -.
DR MaxQB; Q80X19; -.
DR PaxDb; Q80X19; -.
DR PRIDE; Q80X19; -.
DR ProteomicsDB; 283484; -. [Q80X19-1]
DR ProteomicsDB; 283485; -. [Q80X19-2]
DR Antibodypedia; 13712; 117 antibodies from 24 providers.
DR DNASU; 12818; -.
DR Ensembl; ENSMUST00000023053; ENSMUSP00000023053; ENSMUSG00000022371. [Q80X19-1]
DR GeneID; 12818; -.
DR UCSC; uc007vsd.2; mouse. [Q80X19-1]
DR CTD; 7373; -.
DR MGI; MGI:1341272; Col14a1.
DR VEuPathDB; HostDB:ENSMUSG00000022371; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000153769; -.
DR InParanoid; Q80X19; -.
DR OrthoDB; 67372at2759; -.
DR PhylomeDB; Q80X19; -.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 12818; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Col14a1; mouse.
DR PRO; PR:Q80X19; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q80X19; protein.
DR Bgee; ENSMUSG00000022371; Expressed in efferent duct and 186 other tissues.
DR ExpressionAtlas; Q80X19; baseline and differential.
DR Genevisible; Q80X19; MM.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005614; C:interstitial matrix; IDA:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
DR GO; GO:0061050; P:regulation of cell growth involved in cardiac muscle cell development; IMP:MGI.
DR GO; GO:0003229; P:ventricular cardiac muscle tissue development; IMP:MGI.
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; 8.
DR Pfam; PF00092; VWA; 2.
DR SMART; SM00060; FN3; 8.
DR SMART; SM00210; TSPN; 1.
DR SMART; SM00327; VWA; 2.
DR SUPFAM; SSF49265; SSF49265; 5.
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 Alternative splicing; 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..1797
FT /note="Collagen alpha-1(XIV) chain"
FT /id="PRO_0000005786"
FT DOMAIN 32..122
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 159..331
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 356..445
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 446..537
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 538..625
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 627..716
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 738..830
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 832..922
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 923..1014
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1033..1206
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1230..1425
FT /note="Laminin G-like"
FT DOMAIN 1463..1511
FT /note="Collagen-like 1"
FT DOMAIN 1515..1571
FT /note="Collagen-like 2"
FT DOMAIN 1572..1610
FT /note="Collagen-like 3"
FT DOMAIN 1655..1706
FT /note="Collagen-like 4"
FT DOMAIN 1708..1758
FT /note="Collagen-like 5"
FT REGION 124..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1459
FT /note="Nonhelical region (NC4)"
FT REGION 1460..1611
FT /note="Triple-helical region 1 (COL2)"
FT REGION 1463..1611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1645..1797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1655..1780
FT /note="Triple-helical region 2 (COL1)"
FT MOTIF 1608..1610
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 1562..1576
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1659..1676
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1711..1748
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1772..1797
FT /note="VSHPDQPEFTPVQDEQEAMDLWSAGI -> DLIPYNDYQH (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_051652"
FT CONFLICT 406
FT /note="S -> F (in Ref. 1; AAO64442)"
FT /evidence="ECO:0000305"
FT CONFLICT 782..784
FT /note="VGT -> GKN (in Ref. 1; AAO64442)"
FT /evidence="ECO:0000305"
FT CONFLICT 1047
FT /note="D -> H (in Ref. 4; BAE23197)"
FT /evidence="ECO:0000305"
FT CONFLICT 1389
FT /note="N -> S (in Ref. 4; BAE23197)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1797 AA; 193013 MW; 67DAF37398EC49CC CRC64;
MMIWQCKMRD WLILAFLAAA CFCTIVRGQV APPTRLRYNV ISHDSIQISW KAPRGKFGGY
KLLVAPASGG KTNQMNLQNT ATKAIIQGLL PEQNYTVQLI AYYKDKESKP AQGQFRIKDL
EKRKDPTKPK VKVVDKGNGS KPTSPEEVKF FCETPAIADI VILVDGSWSI GRFNFRLVRN
FLENLVTAFN VGSEKTRIGL AQYSGDPRIE WHLNAFNTKD EVIDAVRSLP YKGGNTLTGL
ALNFIFENSF KPEAGSRSGV SKIGILITDG KSQDDIIPPS RNLRESGVEL FAIGVKNADL
SELQEIASEP DSTHVYNVAE FDLMHTVVES LTRTVCSRVE EQDKEIKASA LATIGPPTEL
ITSEVTARSF MVNWTQSPGK VEKYRVVYYP TRGGKPEEVV VDGSVSSTVL KNLMSSTEYQ
IAVFAVSAHT ASEGLRGAET TLALPMASDL ELYDVTENSM RVRWDAVPGA TGYLILYAPL
TEGLAGDEKE MKIGETHTDI ELSGLFPNTE YTVTVYAMFG EEASDPATGQ ETTLPLTPPR
NLRISNVGSN SARLTWDPAS GKISGYRIVY TSADGTEINE VEVDPITTFP LKGLTPLTEY
SIAIFSIYEE GQSLPLVGEF TTEEVPAQQY LEIDEVKTDS FRVTWHPLSA EEGQHKLMWI
PVYGGKTQEV DLKEEQDSYV IEGLDPGTEY EVSLLAVLDD GSESEVVTAV GTTLDDFWTE
APTAIEPTSP VTSVLQTGIR NLVVDDETAT SLRVSWDISD SNVEQFRVTY LKAQGDPMEE
VVGTVMVPGV QNSLLLKALL PDTEYKVTVT PVYTVGEGVS VSAPGKTLPS SGPQNLRVSE
EWYNRVRITW DPPSGPVKGY RIVYKPVSVP GQTLETFVGA DINTIVMTNL LSGMDYNVKI
FASQASGFSD ALTGLVQTLF LGVTDLQANQ VEMTSLCARW QIHRHATAYR IVLESLQDTQ
AQESTVGGGV NRHCFYGLQP DSEYKISVYT KLQELEGPSV SIMQKTQSLP TEPPTFPPTI
PPAKEVCKAA KADLVFMVDG SWSIGDDNFN KIINFLYSTV GALDKIGADG TQVAMVQFTD
DPRTEFKLDS YKTKETLLDA IRHISYKGGN TKTGKAIKHV RDTLFTSDSG TRRGIPKVIV
VITDGRSQDD VNKISREMQA DGFNIFAIGV ADADYSELVQ IGSKPSSRHV FFVDDFDAFK
KIEDELITFV CETASATCPM VHKDGVDLAG FKMMEMFGLV EKDFSAVEGV SMEPGTFNLF
PCYQIHKDAL VSQPTKYLHP EGLPSDYTMS FLFRILPDTP QEPFALWEIL NKNSEPLVGI
ILDNGGKTLT YFNYDYTGDF QTVTFEGPDI RKMFYGSFHK LHVVVSKTLA KVVVDCKEVG
QKAINASANI TSDGVEVLGR MVRSRGPNGN SAPFQLQMFD IVCSTSWASK DRCCELPGLR
DEESCPDLPR SCSCSETNEV ALGPAGPPGG PGLRGPKGQQ GEQGPKGPEG PRGETGPAGP
QGPPGPQGPS GLSIQGMPGM PGDKGDKGDA GLPGPQGVPG GVGSPGRDGS PGQRGFPGKD
GSSGPPGPPG PIGIPGAPGV PGITGSMGPQ GALGPPGVPG AKGERGERGD LQSQAMVRAV
ARQVCEQLIQ SHMARYTAIL NQIPSQSSSI RTIQGPPGEP GRPGSPGTPG EQGPPGTPGF
PGNAGVPGTP GERGLTGVKG EKGNPGIGTQ GPRGPPGPAG PSGESRPGSP GPPGSPGPRG
PPGHLGVPGP QGPSGQPGYC DPSSCSAYGV GVSHPDQPEF TPVQDEQEAM DLWSAGI
