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Q8BLX7

- COGA1_MOUSE

UniProt

Q8BLX7 - COGA1_MOUSE

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Protein

Collagen alpha-1(XVI) chain

Gene

Col16a1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

Involved in mediating cell attachment and inducing integrin-mediated cellular reactions, such as cell spreading and alterations in cell morphology.By similarity

GO - Molecular functioni

  1. integrin binding Source: UniProtKB

GO - Biological processi

  1. cell adhesion Source: UniProtKB
  2. cellular response to amino acid stimulus Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199055. Collagen degradation.
REACT_216309. Integrin cell surface interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(XVI) chain
Gene namesi
Name:Col16a1Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1095396. Col16a1.

Subcellular locationi

GO - Cellular componenti

  1. collagen trimer Source: UniProtKB-KW
  2. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 15801559Collagen alpha-1(XVI) chainSequence AnalysisPRO_0000282960Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi47 – 471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi327 – 3271N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.Curated
Glycosylated.By similarity

Keywords - PTMi

Glycoprotein, Hydroxylation

Proteomic databases

MaxQBiQ8BLX7.
PaxDbiQ8BLX7.
PRIDEiQ8BLX7.

PTM databases

PhosphoSiteiQ8BLX7.

Expressioni

Tissue specificityi

Expressed in most tissues examined with highest levels of expression observed in heart. Strongly expressed in cortical and medullar regions of kidney and more weakly expressed in lung. Also detected in the ciliary muscle of the eye, on the serosa layer lining the muscularis externa of intestinal tissue, and in the perimysium membrane lining both the cardiac muscle bundle and the smooth muscle tissue of the small intestine. Strongly stained in particulate or granular structures. Not detected in brain or skeletal muscle.1 Publication

Developmental stagei

At embryonic day 8 (E8) of gestation no significant expression of mRNA or protein is observed, but strong signals are observed in placental trophoblasts. By E11 weak positive signals are observed in heart. During later stages of development, stronger expression is observed in a variety of tissues, particularly in the atrial and ventricular walls of the developing heart, spinal root neural fibers and skin.1 Publication

Gene expression databases

BgeeiQ8BLX7.
CleanExiMM_COL16A1.
ExpressionAtlasiQ8BLX7. baseline and differential.
GenevestigatoriQ8BLX7.

Interactioni

Subunit structurei

Homotrimer. Interacts with FBN1, fibronectin and integrins ITGA1/ITGB1 and ITGA2/ITGB1. Integrin ITGA1/ITGB1 binds to a unique site within COL16A1 located close to its C-terminal end between collagenous domains COL1-COL3 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ8BLX7.
SMRiQ8BLX7. Positions 44-242.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 231182Laminin G-likeAdd
BLAST
Domaini375 – 42450Collagen-like 1Add
BLAST
Domaini590 – 64354Collagen-like 2Add
BLAST
Domaini676 – 72550Collagen-like 3Add
BLAST
Domaini797 – 84852Collagen-like 4Add
BLAST
Domaini1006 – 106358Collagen-like 5Add
BLAST
Domaini1210 – 126354Collagen-like 6Add
BLAST
Domaini1350 – 140758Collagen-like 7Add
BLAST
Domaini1448 – 150053Collagen-like 8Add
BLAST
Domaini1504 – 155249Collagen-like 9Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni232 – 374143Nonhelical region 10 (NC10)Sequence AnalysisAdd
BLAST
Regioni375 – 509135Triple-helical region 9 (COL9) with 3 imperfectionsSequence AnalysisAdd
BLAST
Regioni510 – 52415Nonhelical region 9 (NC9)Sequence AnalysisAdd
BLAST
Regioni525 – 57046Triple-helical region 8 (COL8) with 1 imperfectionSequence AnalysisAdd
BLAST
Regioni571 – 58616Nonhelical region 8 (NC8)Sequence AnalysisAdd
BLAST
Regioni587 – 64054Triple-helical region 7 (COL7) with 1 imperfectionSequence AnalysisAdd
BLAST
Regioni641 – 66121Nonhelical region 7 (NC7)Sequence AnalysisAdd
BLAST
Regioni662 – 73271Triple-helical region 6 (COL6) with 1 imperfectionSequence AnalysisAdd
BLAST
Regioni733 – 74715Nonhelical region 6 (NC6)Sequence AnalysisAdd
BLAST
Regioni748 – 870123Triple-helical region 5 (COL5) with 3 imperfectionsSequence AnalysisAdd
BLAST
Regioni871 – 88111Nonhelical region 5 (NC5)Sequence AnalysisAdd
BLAST
Regioni882 – 93352Triple-helical region 4 (COL4) with 2 imperfectionsSequence AnalysisAdd
BLAST
Regioni934 – 96734Nonhelical region 4 (NC4)Sequence AnalysisAdd
BLAST
Regioni968 – 98215Triple-helical region 3 (COL3)Sequence AnalysisAdd
BLAST
Regioni983 – 100523Nonhelical region 3 (NC3)Sequence AnalysisAdd
BLAST
Regioni1006 – 1409404Triple-helical region 2 (COL2) with 2 imperfectionsSequence AnalysisAdd
BLAST
Regioni1410 – 144839Nonhelical region 2 (NC2)Sequence AnalysisAdd
BLAST
Regioni1449 – 1554106Triple-helical region 1 (COL1) with 2 imperfectionsSequence AnalysisAdd
BLAST
Regioni1555 – 158026Nonhelical region 1 (NC1)Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi555 – 5573Cell attachment siteSequence Analysis
Motifi1000 – 10023Cell attachment siteSequence Analysis
Motifi1206 – 12083Cell attachment siteSequence Analysis

Domaini

This sequence defines eighteen different domains, nine triple-helical domains (COL9 to COL1) and ten non-triple-helical domains (NC10 to NC1). The numerous interruptions in the triple helix may make this molecule either elastic or flexible.Sequence Analysis

Sequence similaritiesi

Contains 9 collagen-like domains.Curated
Contains 1 laminin G-like domain.Curated

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00760000118927.
HOGENOMiHOG000085653.
HOVERGENiHBG071631.
InParanoidiQ8BLX7.
OMAiSTWYLFQ.
OrthoDBiEOG779NXQ.
PhylomeDBiQ8BLX7.
TreeFamiTF332900.

Family and domain databases

InterProiIPR008160. Collagen.
IPR013320. ConA-like_dom.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF01391. Collagen. 9 hits.
[Graphical view]
SMARTiSM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 11 Publication (identifier: Q8BLX7) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLTSWAPGLW VLGLWATFSH GTNIGERCPT SQQEGLKLEH SSDPSTNVTG
60 70 80 90 100
FNLIRRLNLM KTSAIKKIRN PKGPLILRLG AAPVTQPTRR VFPRGLPEEF
110 120 130 140 150
ALVLTVLLKK HTFRNTWYLF QVTDANGYPQ ISLEVNSQER SLELRAQGQD
160 170 180 190 200
GDFVSCIFPV PQLFDLRWHK LMLSVAGRVA SVHVDCVSAS SQPLGPRQSI
210 220 230 240 250
RPGGHVFLGL DAEQGKPVSF DLQQAHIYCD PELVLEEGCC EILPGGCPPE
260 270 280 290 300
TSKSRRDTQS NELIEINPQT EGKVYTRCFC LEEPQNSKVD AQLMGRNIQK
310 320 330 340 350
AERGTKVHQG TGVNECPPCA HSARESNVTL GPSGLKGGKG ERGLTGPSGP
360 370 380 390 400
KGEKGARGND CVRVSPDAPL QCVEGPKGEK GESGDLGPPG LPGPTGQKGQ
410 420 430 440 450
KGEKGDGGLK GLPGKPGRDG RPGEICVIGP KGQKGDPGFV GPEGLAGEPG
460 470 480 490 500
PPGLPGPPGI GLPGTPGDPG GPPGPKGEKG SSGIPGKEGP GGKPGKPGVP
510 520 530 540 550
GTKGEKGDPC EVCPTLPEGS QNFVGLPGKP GPKGEPGDPA PAWEGLGTVG
560 570 580 590 600
LKGDRGDPGI QGMKGEKGEP CSSCSSGVGA QHLGPSPGHG LPGLPGTSGI
610 620 630 640 650
PGPRGLKGEK GSFGDTGPAG VPGSPGPVGP AGIKGAKGEP CEPCTALSEL
660 670 680 690 700
QDGDMRVVHL PGPAGEKGEP GSPGFGLPGK QGKAGERGLK GQKGDAGNPG
710 720 730 740 750
DPGTPGITGQ PGISGEPGIR GPAGPKGEKG DGCTACPSLQ GALTDVSGLP
760 770 780 790 800
GKPGPKGEPG PEGVGHPGKP GQPGLPGVQG PPGPKGTQGE PGPPGTGAEG
810 820 830 840 850
PQGEPGTQGL PGTQGLPGPR GPPGSAGEKG AQGSPGPKGA IGPMGPPGAG
860 870 880 890 900
VSGPPGQKGS RGEKGEPGEC SCPSRGEPIF SGMPGAPGLW MGSSSQPGPQ
910 920 930 940 950
GPPGVPGPPG PPGMPGLQGV PGHNGLPGQP GLTAELGSLP IEKHLLKSIC
960 970 980 990 1000
GDCAQGQTAH PAFLLEKGEK GDQGIPGVPG FDNCARCFIE RERPRAEEAR
1010 1020 1030 1040 1050
GDNSEGEPGC SGSPGLPGPP GMPGQRGEEG PPGMRGSPGP PGPIGLQGER
1060 1070 1080 1090 1100
GLTGLTGDKG EPGPPGQPGY PGAMGPPGLP GIKGERGYTG PSGEKGESGP
1110 1120 1130 1140 1150
PGSEGLPGPQ GPAGPRGERG PQGSSGEKGD QGFQGQPGFP GPPGPPGFPG
1160 1170 1180 1190 1200
KAGAPGPPGP QAEKGSEGIR GPSGLPGSPG PPGPPGIQGP AGLDGLDGKD
1210 1220 1230 1240 1250
GKPGLRGDPG PAGPPGLMGP PGFKGKTGHP GLPGPKGDCG KPGPPGSSGR
1260 1270 1280 1290 1300
PGAEGEPGAM GPQGRPGPPG HLGPPGQPGP PGLSTVGLKG DRGVPGERGL
1310 1320 1330 1340 1350
AGLPGQPGTP GHPGPPGEPG SDGAAGKEGP PGKQGLYGPP GPKGDPGPAG
1360 1370 1380 1390 1400
QKGQAGEKGR SGMPGGPGKS GSMGPIGPPG PAGERGHPGS PGPAGNPGLP
1410 1420 1430 1440 1450
GLPGSMGDMV NYDDIKRFIR QEIIKLFDER MAYYTSRMQF PMEVAAAPGR
1460 1470 1480 1490 1500
PGPPGKDGAP GRPGAPGSPG LPGQIGREGR QGLPGMRGLP GTKGEKGDIG
1510 1520 1530 1540 1550
VGIAGENGLP GPPGPQGPPG YGKMGATGPM GQQGIPGIPG PPGPMGQPGK
1560 1570 1580
AGHCNPSDCF GAMPMEQQYP PMKSMKGPFG

Note: No experimental confirmation available.Curated

Length:1,580
Mass (Da):155,805
Last modified:April 3, 2007 - v2
Checksum:iFC01635F6E410E3A
GO
Isoform 21 Publication (identifier: Q8BLX7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1430: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:150
Mass (Da):14,823
Checksum:iD956EF9160987FC8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti726 – 7261K → R in BAC30765. (PubMed:16141072)Curated
Sequence conflicti1119 – 11191R → Q in BAC30765. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 14301430Missing in isoform 2. 1 PublicationVSP_052375Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK012212 mRNA. Translation: BAB28100.1.
AK040971 mRNA. Translation: BAC30765.1.
AL606925 Genomic DNA. Translation: CAM45907.1.
CCDSiCCDS38889.1. [Q8BLX7-1]
RefSeqiNP_082542.3. NM_028266.5. [Q8BLX7-1]
UniGeneiMm.41860.

Genome annotation databases

EnsembliENSMUST00000044565; ENSMUSP00000035802; ENSMUSG00000040690. [Q8BLX7-1]
GeneIDi107581.
KEGGimmu:107581.
UCSCiuc008uys.2. mouse. [Q8BLX7-1]
uc008uyv.2. mouse. [Q8BLX7-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK012212 mRNA. Translation: BAB28100.1 .
AK040971 mRNA. Translation: BAC30765.1 .
AL606925 Genomic DNA. Translation: CAM45907.1 .
CCDSi CCDS38889.1. [Q8BLX7-1 ]
RefSeqi NP_082542.3. NM_028266.5. [Q8BLX7-1 ]
UniGenei Mm.41860.

3D structure databases

ProteinModelPortali Q8BLX7.
SMRi Q8BLX7. Positions 44-242.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q8BLX7.

Proteomic databases

MaxQBi Q8BLX7.
PaxDbi Q8BLX7.
PRIDEi Q8BLX7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000044565 ; ENSMUSP00000035802 ; ENSMUSG00000040690 . [Q8BLX7-1 ]
GeneIDi 107581.
KEGGi mmu:107581.
UCSCi uc008uys.2. mouse. [Q8BLX7-1 ]
uc008uyv.2. mouse. [Q8BLX7-2 ]

Organism-specific databases

CTDi 1307.
MGIi MGI:1095396. Col16a1.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00760000118927.
HOGENOMi HOG000085653.
HOVERGENi HBG071631.
InParanoidi Q8BLX7.
OMAi STWYLFQ.
OrthoDBi EOG779NXQ.
PhylomeDBi Q8BLX7.
TreeFami TF332900.

Enzyme and pathway databases

Reactomei REACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199055. Collagen degradation.
REACT_216309. Integrin cell surface interactions.

Miscellaneous databases

NextBioi 359082.
PROi Q8BLX7.
SOURCEi Search...

Gene expression databases

Bgeei Q8BLX7.
CleanExi MM_COL16A1.
ExpressionAtlasi Q8BLX7. baseline and differential.
Genevestigatori Q8BLX7.

Family and domain databases

InterProi IPR008160. Collagen.
IPR013320. ConA-like_dom.
IPR001791. Laminin_G.
[Graphical view ]
Pfami PF01391. Collagen. 9 hits.
[Graphical view ]
SMARTi SM00210. TSPN. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6JImported.
    Tissue: EmbryoImported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Tissue distribution and developmental expression of type XVI collagen in the mouse."
    Lai C.-H., Chu M.-L.
    Tissue Cell 28:155-164(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiCOGA1_MOUSE
AccessioniPrimary (citable) accession number: Q8BLX7
Secondary accession number(s): A3KFV5, Q9CZS2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: October 29, 2014
This is version 101 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3