COGA1_MOUSE
ID COGA1_MOUSE Reviewed; 1580 AA.
AC Q8BLX7; A3KFV5; Q9CZS2;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Collagen alpha-1(XVI) chain;
DE Flags: Precursor;
GN Name=Col16a1 {ECO:0000312|MGI:MGI:1095396};
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:BAC30765.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC30765.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAB28100.1};
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [3] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8650669; DOI=10.1016/s0040-8166(96)80004-8;
RA Lai C.-H., Chu M.-L.;
RT "Tissue distribution and developmental expression of type XVI collagen in
RT the mouse.";
RL Tissue Cell 28:155-164(1996).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: Involved in mediating cell attachment and inducing integrin-
CC mediated cellular reactions, such as cell spreading and alterations in
CC cell morphology. {ECO:0000250|UniProtKB:Q07092}.
CC -!- SUBUNIT: Homotrimer. Interacts with FBN1, fibronectin and integrins
CC ITGA1/ITGB1 and ITGA2/ITGB1. Integrin ITGA1/ITGB1 binds to a unique
CC site within COL16A1 located close to its C-terminal end between
CC collagenous domains COL1-COL3 (By similarity).
CC {ECO:0000250|UniProtKB:Q07092}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:16141072};
CC IsoId=Q8BLX7-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16141072};
CC IsoId=Q8BLX7-2; Sequence=VSP_052375;
CC -!- TISSUE SPECIFICITY: Expressed in most tissues examined with highest
CC levels of expression observed in heart. Strongly expressed in cortical
CC and medullar regions of kidney and more weakly expressed in lung. Also
CC detected in the ciliary muscle of the eye, on the serosa layer lining
CC the muscularis externa of intestinal tissue, and in the perimysium
CC membrane lining both the cardiac muscle bundle and the smooth muscle
CC tissue of the small intestine. Strongly stained in particulate or
CC granular structures. Not detected in brain or skeletal muscle.
CC {ECO:0000269|PubMed:8650669}.
CC -!- DEVELOPMENTAL STAGE: At 8 dpc no significant expression of mRNA or
CC protein is observed, but strong signals are observed in placental
CC trophoblasts. By 11 dpc weak positive signals are observed in heart.
CC During later stages of development, stronger expression is observed in
CC a variety of tissues, particularly in the atrial and ventricular walls
CC of the developing heart, spinal root neural fibers and skin.
CC {ECO:0000269|PubMed:8650669}.
CC -!- DOMAIN: This sequence defines eighteen different domains, nine triple-
CC helical domains (COL9 to COL1) and ten non-triple-helical domains (NC10
CC to NC1). The numerous interruptions in the triple helix may make this
CC molecule either elastic or flexible. {ECO:0000255}.
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. {ECO:0000305}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q07092}.
CC -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted
CC helices (FACIT) family. {ECO:0000255}.
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DR EMBL; AK012212; BAB28100.1; -; mRNA.
DR EMBL; AK040971; BAC30765.1; -; mRNA.
DR EMBL; AL606925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS38889.1; -. [Q8BLX7-1]
DR RefSeq; NP_082542.3; NM_028266.5. [Q8BLX7-1]
DR AlphaFoldDB; Q8BLX7; -.
DR BioGRID; 223412; 3.
DR ComplexPortal; CPX-2994; Collagen type XVI trimer.
DR STRING; 10090.ENSMUSP00000035802; -.
DR GlyGen; Q8BLX7; 2 sites.
DR iPTMnet; Q8BLX7; -.
DR PhosphoSitePlus; Q8BLX7; -.
DR jPOST; Q8BLX7; -.
DR MaxQB; Q8BLX7; -.
DR PaxDb; Q8BLX7; -.
DR PRIDE; Q8BLX7; -.
DR ProteomicsDB; 283421; -. [Q8BLX7-1]
DR ProteomicsDB; 283422; -. [Q8BLX7-2]
DR Antibodypedia; 8436; 65 antibodies from 19 providers.
DR DNASU; 107581; -.
DR Ensembl; ENSMUST00000044565; ENSMUSP00000035802; ENSMUSG00000040690. [Q8BLX7-1]
DR GeneID; 107581; -.
DR KEGG; mmu:107581; -.
DR UCSC; uc008uyr.2; mouse. [Q8BLX7-1]
DR UCSC; uc008uyv.2; mouse. [Q8BLX7-2]
DR CTD; 1307; -.
DR MGI; MGI:1095396; Col16a1.
DR VEuPathDB; HostDB:ENSMUSG00000040690; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000161782; -.
DR HOGENOM; CLU_001074_2_2_1; -.
DR InParanoid; Q8BLX7; -.
DR OMA; MGNSWQP; -.
DR OrthoDB; 1295141at2759; -.
DR PhylomeDB; Q8BLX7; -.
DR TreeFam; TF332900; -.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 107581; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Col16a1; mouse.
DR PRO; PR:Q8BLX7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BLX7; protein.
DR Bgee; ENSMUSG00000040690; Expressed in humerus cartilage element and 247 other tissues.
DR ExpressionAtlas; Q8BLX7; baseline and differential.
DR Genevisible; Q8BLX7; MM.
DR GO; GO:0005588; C:collagen type V trimer; IBA:GO_Central.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; ISO:MGI.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0033622; P:integrin activation; ISO:MGI.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISO:MGI.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF01391; Collagen; 6.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Collagen; Extracellular matrix;
KW Glycoprotein; Hydroxylation; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1580
FT /note="Collagen alpha-1(XVI) chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000282960"
FT DOMAIN 50..231
FT /note="Laminin G-like"
FT DOMAIN 375..424
FT /note="Collagen-like 1"
FT DOMAIN 590..643
FT /note="Collagen-like 2"
FT DOMAIN 676..725
FT /note="Collagen-like 3"
FT DOMAIN 797..848
FT /note="Collagen-like 4"
FT DOMAIN 1006..1063
FT /note="Collagen-like 5"
FT DOMAIN 1210..1263
FT /note="Collagen-like 6"
FT DOMAIN 1350..1407
FT /note="Collagen-like 7"
FT DOMAIN 1448..1500
FT /note="Collagen-like 8"
FT DOMAIN 1504..1552
FT /note="Collagen-like 9"
FT REGION 232..374
FT /note="Nonhelical region 10 (NC10)"
FT /evidence="ECO:0000255"
FT REGION 324..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..509
FT /note="Triple-helical region 9 (COL9) with 3 imperfections"
FT /evidence="ECO:0000255"
FT REGION 510..524
FT /note="Nonhelical region 9 (NC9)"
FT /evidence="ECO:0000255"
FT REGION 525..570
FT /note="Triple-helical region 8 (COL8) with 1 imperfection"
FT /evidence="ECO:0000255"
FT REGION 571..586
FT /note="Nonhelical region 8 (NC8)"
FT /evidence="ECO:0000255"
FT REGION 585..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..640
FT /note="Triple-helical region 7 (COL7) with 1 imperfection"
FT /evidence="ECO:0000255"
FT REGION 641..661
FT /note="Nonhelical region 7 (NC7)"
FT /evidence="ECO:0000255"
FT REGION 662..732
FT /note="Triple-helical region 6 (COL6) with 1 imperfection"
FT /evidence="ECO:0000255"
FT REGION 733..747
FT /note="Nonhelical region 6 (NC6)"
FT /evidence="ECO:0000255"
FT REGION 748..870
FT /note="Triple-helical region 5 (COL5) with 3 imperfections"
FT /evidence="ECO:0000255"
FT REGION 871..881
FT /note="Nonhelical region 5 (NC5)"
FT /evidence="ECO:0000255"
FT REGION 882..933
FT /note="Triple-helical region 4 (COL4) with 2 imperfections"
FT /evidence="ECO:0000255"
FT REGION 934..967
FT /note="Nonhelical region 4 (NC4)"
FT /evidence="ECO:0000255"
FT REGION 968..982
FT /note="Triple-helical region 3 (COL3)"
FT /evidence="ECO:0000255"
FT REGION 983..1005
FT /note="Nonhelical region 3 (NC3)"
FT /evidence="ECO:0000255"
FT REGION 995..1405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1409
FT /note="Triple-helical region 2 (COL2) with 2 imperfections"
FT /evidence="ECO:0000255"
FT REGION 1410..1448
FT /note="Nonhelical region 2 (NC2)"
FT /evidence="ECO:0000255"
FT REGION 1445..1523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1449..1554
FT /note="Triple-helical region 1 (COL1) with 2 imperfections"
FT /evidence="ECO:0000255"
FT REGION 1555..1580
FT /note="Nonhelical region 1 (NC1)"
FT /evidence="ECO:0000255"
FT MOTIF 555..557
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1000..1002
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1206..1208
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 448..473
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..916
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1156
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1281
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..1430
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052375"
FT CONFLICT 726
FT /note="K -> R (in Ref. 1; BAC30765)"
FT /evidence="ECO:0000305"
FT CONFLICT 1119
FT /note="R -> Q (in Ref. 1; BAC30765)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1580 AA; 155805 MW; FC01635F6E410E3A CRC64;
MLTSWAPGLW VLGLWATFSH GTNIGERCPT SQQEGLKLEH SSDPSTNVTG FNLIRRLNLM
KTSAIKKIRN PKGPLILRLG AAPVTQPTRR VFPRGLPEEF ALVLTVLLKK HTFRNTWYLF
QVTDANGYPQ ISLEVNSQER SLELRAQGQD GDFVSCIFPV PQLFDLRWHK LMLSVAGRVA
SVHVDCVSAS SQPLGPRQSI RPGGHVFLGL DAEQGKPVSF DLQQAHIYCD PELVLEEGCC
EILPGGCPPE TSKSRRDTQS NELIEINPQT EGKVYTRCFC LEEPQNSKVD AQLMGRNIQK
AERGTKVHQG TGVNECPPCA HSARESNVTL GPSGLKGGKG ERGLTGPSGP KGEKGARGND
CVRVSPDAPL QCVEGPKGEK GESGDLGPPG LPGPTGQKGQ KGEKGDGGLK GLPGKPGRDG
RPGEICVIGP KGQKGDPGFV GPEGLAGEPG PPGLPGPPGI GLPGTPGDPG GPPGPKGEKG
SSGIPGKEGP GGKPGKPGVP GTKGEKGDPC EVCPTLPEGS QNFVGLPGKP GPKGEPGDPA
PAWEGLGTVG LKGDRGDPGI QGMKGEKGEP CSSCSSGVGA QHLGPSPGHG LPGLPGTSGI
PGPRGLKGEK GSFGDTGPAG VPGSPGPVGP AGIKGAKGEP CEPCTALSEL QDGDMRVVHL
PGPAGEKGEP GSPGFGLPGK QGKAGERGLK GQKGDAGNPG DPGTPGITGQ PGISGEPGIR
GPAGPKGEKG DGCTACPSLQ GALTDVSGLP GKPGPKGEPG PEGVGHPGKP GQPGLPGVQG
PPGPKGTQGE PGPPGTGAEG PQGEPGTQGL PGTQGLPGPR GPPGSAGEKG AQGSPGPKGA
IGPMGPPGAG VSGPPGQKGS RGEKGEPGEC SCPSRGEPIF SGMPGAPGLW MGSSSQPGPQ
GPPGVPGPPG PPGMPGLQGV PGHNGLPGQP GLTAELGSLP IEKHLLKSIC GDCAQGQTAH
PAFLLEKGEK GDQGIPGVPG FDNCARCFIE RERPRAEEAR GDNSEGEPGC SGSPGLPGPP
GMPGQRGEEG PPGMRGSPGP PGPIGLQGER GLTGLTGDKG EPGPPGQPGY PGAMGPPGLP
GIKGERGYTG PSGEKGESGP PGSEGLPGPQ GPAGPRGERG PQGSSGEKGD QGFQGQPGFP
GPPGPPGFPG KAGAPGPPGP QAEKGSEGIR GPSGLPGSPG PPGPPGIQGP AGLDGLDGKD
GKPGLRGDPG PAGPPGLMGP PGFKGKTGHP GLPGPKGDCG KPGPPGSSGR PGAEGEPGAM
GPQGRPGPPG HLGPPGQPGP PGLSTVGLKG DRGVPGERGL AGLPGQPGTP GHPGPPGEPG
SDGAAGKEGP PGKQGLYGPP GPKGDPGPAG QKGQAGEKGR SGMPGGPGKS GSMGPIGPPG
PAGERGHPGS PGPAGNPGLP GLPGSMGDMV NYDDIKRFIR QEIIKLFDER MAYYTSRMQF
PMEVAAAPGR PGPPGKDGAP GRPGAPGSPG LPGQIGREGR QGLPGMRGLP GTKGEKGDIG
VGIAGENGLP GPPGPQGPPG YGKMGATGPM GQQGIPGIPG PPGPMGQPGK AGHCNPSDCF
GAMPMEQQYP PMKSMKGPFG
