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Q60847

- COCA1_MOUSE

UniProt

Q60847 - COCA1_MOUSE

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Protein

Collagen alpha-1(XII) chain

Gene

Col12a1

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

Functioni

Type XII collagen interacts with type I collagen-containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix.By similarity

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_198984. Collagen biosynthesis and modifying enzymes.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(XII) chain
Gene namesi
Name:Col12a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:88448. Col12a1.

Subcellular locationi

GO - Cellular componenti

  1. collagen trimer Source: UniProtKB-KW
  2. extracellular matrix Source: UniProtKB
  3. extracellular space Source: Ensembl
  4. extracellular vesicular exosome Source: Ensembl
  5. 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 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 31203097Collagen alpha-1(XII) chainPRO_0000005784Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi700 – 7001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi798 – 7981O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
Glycosylationi889 – 8891O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
Glycosylationi981 – 9811O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
Glycosylationi1765 – 17651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2208 – 22081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2530 – 25301N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2681 – 26811N-linked (GlcNAc...)Sequence Analysis
Modified residuei2946 – 294614-hydroxyprolineBy similarity
Modified residuei2949 – 294914-hydroxyprolineBy similarity
Modified residuei2952 – 295214-hydroxyprolineBy similarity
Modified residuei2961 – 296114-hydroxyprolineBy similarity
Modified residuei2967 – 296714-hydroxyprolineBy similarity
Modified residuei2970 – 297014-hydroxyprolineBy similarity
Modified residuei2973 – 297314-hydroxyprolineBy similarity
Modified residuei2985 – 298514-hydroxyprolineBy similarity
Modified residuei3002 – 300214-hydroxyprolineBy similarity
Modified residuei3005 – 300514-hydroxyprolineBy similarity
Modified residuei3016 – 301614-hydroxyprolineBy similarity
Modified residuei3025 – 302514-hydroxyprolineBy similarity
Modified residuei3028 – 302814-hydroxyprolineBy similarity
Modified residuei3031 – 303114-hydroxyprolineBy similarity

Post-translational modificationi

The triple-helical tail is stabilized by disulfide bonds at each end.By similarity
Hydroxylation on proline residues within the sequence motif, GXPG, is most likely to be 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates.By similarity
O-glycosylation of isoform 2; glycosaminoglycan of chondroitin-sulfate type.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

MaxQBiQ60847.
PaxDbiQ60847.
PRIDEiQ60847.

PTM databases

PhosphoSiteiQ60847.

Expressioni

Tissue specificityi

Highest expression in tendons, perichondrium, skin, cornea, sclera, blood vessels, and periosteum.

Developmental stagei

The long NC3 XIIA isoforms are predominant at early stages (ED7 and 11); at later stages of development (ED15 and 17) the short NC3 XIIB forms become the major forms. As the short NC3 forms become the major product, the long splice variant continues to be expressed in several tissues, even after birth. The long NC1 isoforms, XIIA-1 and XIIB-1, peak in 15-day old embryos and decrease in 17-day old ones. The expression of the short NC1 form XIIB-2 remains constant throughout late stages of embryonic development (ED15 and ED17).

Gene expression databases

BgeeiQ60847.
CleanExiMM_COL12A1.
ExpressionAtlasiQ60847. baseline and differential.
GenevestigatoriQ60847.

Interactioni

Subunit structurei

Trimer of identical chains each containing 190 kDa of non-triple-helical sequences.By similarity

Protein-protein interaction databases

IntActiQ60847. 1 interaction.
MINTiMINT-4091424.

Structurei

3D structure databases

ProteinModelPortaliQ60847.
SMRiQ60847. Positions 25-317, 333-415, 440-616, 631-1179, 1196-1367, 1378-2312, 2325-2487, 2510-2726.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 11791Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini140 – 316177VWFA 1PROSITE-ProRule annotationAdd
BLAST
Domaini336 – 42691Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini440 – 616177VWFA 2PROSITE-ProRule annotationAdd
BLAST
Domaini634 – 72390Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini725 – 81692Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini817 – 90589Fibronectin type-III 5PROSITE-ProRule annotationAdd
BLAST
Domaini907 – 99892Fibronectin type-III 6PROSITE-ProRule annotationAdd
BLAST
Domaini1000 – 108788Fibronectin type-III 7PROSITE-ProRule annotationAdd
BLAST
Domaini1089 – 117991Fibronectin type-III 8PROSITE-ProRule annotationAdd
BLAST
Domaini1199 – 1371173VWFA 3PROSITE-ProRule annotationAdd
BLAST
Domaini1387 – 147589Fibronectin type-III 9PROSITE-ProRule annotationAdd
BLAST
Domaini1476 – 156792Fibronectin type-III 10PROSITE-ProRule annotationAdd
BLAST
Domaini1568 – 165891Fibronectin type-III 11PROSITE-ProRule annotationAdd
BLAST
Domaini1659 – 175496Fibronectin type-III 12PROSITE-ProRule annotationAdd
BLAST
Domaini1757 – 185195Fibronectin type-III 13PROSITE-ProRule annotationAdd
BLAST
Domaini1852 – 193786Fibronectin type-III 14PROSITE-ProRule annotationAdd
BLAST
Domaini1938 – 202891Fibronectin type-III 15PROSITE-ProRule annotationAdd
BLAST
Domaini2029 – 211991Fibronectin type-III 16PROSITE-ProRule annotationAdd
BLAST
Domaini2120 – 220889Fibronectin type-III 17PROSITE-ProRule annotationAdd
BLAST
Domaini2209 – 229688Fibronectin type-III 18PROSITE-ProRule annotationAdd
BLAST
Domaini2325 – 2498174VWFA 4PROSITE-ProRule annotationAdd
BLAST
Domaini2522 – 2714193Laminin G-likeAdd
BLAST
Domaini2749 – 280052Collagen-like 1Add
BLAST
Domaini2804 – 285451Collagen-like 2Add
BLAST
Domaini2855 – 289945Collagen-like 3Add
BLAST
Domaini2943 – 299250Collagen-like 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2453 – 2748296Nonhelical region (NC3)Add
BLAST
Regioni2749 – 2900152Triple-helical region (COL2) with 1 imperfectionAdd
BLAST
Regioni2901 – 294343Nonhelical region (NC2)Add
BLAST
Regioni2944 – 3046103Triple-helical region (COL1) with 2 imperfectionsAdd
BLAST
Regioni3047 – 312074Nonhelical region (NC1)Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi862 – 8643Cell attachment siteSequence Analysis
Motifi2781 – 27833Cell attachment siteSequence Analysis
Motifi2897 – 28993Cell attachment siteSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi865 – 8684Poly-Thr

Sequence similaritiesi

Contains 4 collagen-like domains.Curated
Contains 18 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 laminin G-like domain.Curated
Contains 4 VWFA domains.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00760000119000.
HOGENOMiHOG000111877.
HOVERGENiHBG051060.
InParanoidiQ60847.
KOiK08132.
OrthoDBiEOG71P290.
PhylomeDBiQ60847.
TreeFamiTF329914.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
2.60.40.10. 18 hits.
3.40.50.410. 4 hits.
InterProiIPR008160. Collagen.
IPR013320. ConA-like_dom.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR001791. Laminin_G.
IPR002035. VWF_A.
[Graphical view]
PfamiPF01391. Collagen. 4 hits.
PF00041. fn3. 18 hits.
PF00092. VWA. 4 hits.
[Graphical view]
SMARTiSM00060. FN3. 18 hits.
SM00210. TSPN. 1 hit.
SM00327. VWA. 4 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 11 hits.
SSF49899. SSF49899. 1 hit.
SSF53300. SSF53300. 4 hits.
PROSITEiPS50853. FN3. 18 hits.
PS50234. VWFA. 4 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. Align

Note: The final tissue form of collagen XII may contain homotrimers or any combination of the various isoforms.

Isoform 1 (identifier: Q60847-1) [UniParc]FASTAAdd to Basket

Also known as: XIIA-1

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
MQTRLPRALA ALGVALLLSS IEAEVDPPSD LNFKIIDENT VHMSWERPVD
60 70 80 90 100
PIVGYRITVD PTTDGPTKEF TLAASTTETL LSDLIPETQY VVTITSYNEV
110 120 130 140 150
EESVPVIGQL TIQTGGPTKP GEKKPGKTEI QKCSVSAWTD LVFLVDGSWS
160 170 180 190 200
VGRNNFKYIL DFIVALVSAF DIGEEKTRVG VVQYSSDTRT EFNLNQYYRR
210 220 230 240 250
EDLLAAVKKI PYKGGNTMTG DAIDYLVKNT FTESAGSRAG FPKVAIIITD
260 270 280 290 300
GKSQDEVEIP ARELRNIGVE VFSLGIKAAD AKELKQIAST PSLNHVFNVA
310 320 330 340 350
NFDAIVDIQN EIISQVCSGV DEQLGELVSG EEVIEPPSNL VVTELSSKYI
360 370 380 390 400
RLSWDPSPSA VTGYKILLTP MAAGSRHHAL SVGPQTTTLN VRDLTADTEY
410 420 430 440 450
QISVFAMKGL TSSEPTSVME KTQPMKVQVE CSRGVDIKAD IVFLVDGSYS
460 470 480 490 500
IGIANFVKVR AFLEVLAKSF EISPNRVQIS LVQYSRDPHT EFTLKEFNRV
510 520 530 540 550
EDIIKAINTF PYRGGSTNTG KAMTYVREKI FVPNKGSRSN VPKVMILITD
560 570 580 590 600
GKSSDAFRDP AIKLRNSDVE IFAVGVKDAV RSELEAIASP PAETHVFTVE
610 620 630 640 650
DFDAFQRISF ELTQSICLRI EQELAAIKKK AYVPPKDLRF TQVTANSFKA
660 670 680 690 700
EWSPPGDNVF SYHVTYKDAN GDDEVTVVEP ASSTSVVLNN LRPETLYLVN
710 720 730 740 750
VTAEYEDGFS VPITGEETTA EVKGVPRNLK VTDETTDSFK LTWSQAPGRV
760 770 780 790 800
LRYRIRYRPV SGGESKEVST PANQRRKTLE NLTPDTKYEI SVIAEYSSGP
810 820 830 840 850
GSPLTGNAAT EEVRGNPRDL RVSDATTSTL KLSWSRAPGK VKQYLVTYTP
860 870 880 890 900
AAGGETQEVT VRGDTTTTML RKLKEGTQYD LSVTALYASG AGEALSGKGS
910 920 930 940 950
TLEERGSPQN LVTKDITDTS IGAYWTSAPG MVRGYRVSWK SLYDDIEAGE
960 970 980 990 1000
TTLPGDAIHT MIENLQPETK YKISVFATYS SGEGEPVTGD ATTELSQDSK
1010 1020 1030 1040 1050
ILRVDEETEH TMRVTWKAAP GKVVNYRVVY RPQGGGRQMV AKVPPTVTST
1060 1070 1080 1090 1100
VLKRLQPQTT YDITVLPMYK TGEGKLRQGS GTTASRFKSP RNLKTSDPTM
1110 1120 1130 1140 1150
SSFRVTWEPA PGEVKGYKVT FHPTGDDRRL GELVLGPYDN TVVLEELRAG
1160 1170 1180 1190 1200
TTYRVNVFGM FDGGESLPLV GQEMTTLSDT TVTPFLSSGM DCLTRAEADI
1210 1220 1230 1240 1250
VLLVDGSWSI GRANFRTVRS FISRIVEVFE IGPKRVQIAL AQYSGDPRTE
1260 1270 1280 1290 1300
WQLNAHRDKK SLLQAVANLP YKGGNTLTGM ALNFIRQQSF KTQAGMRPRA
1310 1320 1330 1340 1350
RKIGVLITDG KSQDDVEAPS KKLKDEGVEL FAIGIKNADE VELKMIATDP
1360 1370 1380 1390 1400
DDTHAYNVAD FESLSKIVDD LTINLCNSVK GPGDLEAPTN LVISERTHRS
1410 1420 1430 1440 1450
FRVSWTPPSD SVDRYKVEYY PVSGGKRQEF YVSRLDTSTV LKDLKPETDY
1460 1470 1480 1490 1500
VVNVYSVVED EYSEPLKGTE KTLPVPVVSL NIYDVGPTTM HVQWQPVGGA
1510 1520 1530 1540 1550
TGYTVSYQPT RSPEGTKPKE MRVGPTVNDV QLTGLLPNTE YEVTVQAVLY
1560 1570 1580 1590 1600
DLTSEPAKAR EVTLPLPRPQ DVKLRDVTHS TMNVVWEPVL GKVRKYIVRY
1610 1620 1630 1640 1650
KTPDEEFKEV EVDRSRASTI LKDLSSQTQY TVSVSAVYDE GTSPPATAYD
1660 1670 1680 1690 1700
TTRRVPAPTN LQFTEVTPES FRGTWDHGAS DVSLYRITWA PVGNPDKMET
1710 1720 1730 1740 1750
ILNGDENTLV FENLNPNTPY EVSITAIYPD ESESEDLSGT ERTLRLIPLT
1760 1770 1780 1790 1800
TQAPKSGPRN LQVYNATSNS LTVKWDPASG RVQKYRITYQ PSTGEGNEQT
1810 1820 1830 1840 1850
ITVGGRQNSV LLQKLKPDTP YTITVYSQYP DGEGGRMTGR GKTKPLNTVR
1860 1870 1880 1890 1900
NLRVYDPSTS SLSVRWDHAE GNPRQYKLFY APTSGGPEEL VPIPGNTNYA
1910 1920 1930 1940 1950
ILRNLQPDTP YTITVVPVYT EGDGGRTSDT GRTLVRGLAR NIQVYNPTPN
1960 1970 1980 1990 2000
SLDVRWDPAP GPVQQYRIVY SPVAGTRPSE SIVVPGNTRT VHLERLIPDT
2010 2020 2030 2040 2050
PYSVNIVALY SDGEGNPSPS QGRTLPRSGP RNIRVFGETT NSLSVAWDHA
2060 2070 2080 2090 2100
DGPVQQYRII YSPTVGDPID EYTTVPGRRN NVILQPLQPD TPYKITVIAI
2110 2120 2130 2140 2150
YEDGDGGHLT GNGRTVGLLP PQNIHIFDEW YTRFRVSWDP SPSPVLGYKI
2160 2170 2180 2190 2200
VYKPVGSNEP MEAFVGEVTS YTLHNLNPST TYDVSVYAQY DSGLSVPLTD
2210 2220 2230 2240 2250
QGTTLYLNVT DLKTYQVGWD TFCVKWSPHR AATSYRLKLS PADGTRGQEI
2260 2270 2280 2290 2300
TVRGSETSHC FTGLSPEAEY GVTVFVQTPN LEGPGVPIKE QTTVKPTEAP
2310 2320 2330 2340 2350
TEPPTPSPPP TIPPARDVCK GAKADIVFLT DASWSIGDDN FNKVVKFIFN
2360 2370 2380 2390 2400
TVGAFDEVNP AGIQVSFVQY SDEVKSEFKL NTYNDKALAL GALQNIRYRG
2410 2420 2430 2440 2450
GNTRTGKALT FIKEKVLTWE SGMRKNVPKV LVVVTDGRSQ DEVKKAAFVI
2460 2470 2480 2490 2500
QQSGFSVFVV GVADVDYNEL ANIASKPSER HVFIVDDFES FEKIEDNLIT
2510 2520 2530 2540 2550
FVCETATSSC PLIYLDGYTS PGFKMLEAYN LTEKNFASVQ GVSLESGSFP
2560 2570 2580 2590 2600
SYSAYRLQKN AFINQPTAEL HPNGLPPSYT IILLFRLLPE TPSDPFAIWQ
2610 2620 2630 2640 2650
ITDRDYRPQV GVIADPSSKT LSFFNKDTRG EVQTVTFDTD EVKTLFYGSF
2660 2670 2680 2690 2700
HKVHIVVTSK SVKIYIDCYE IIEKDIKEAG NITTDGYEIL GKLLKGERKS
2710 2720 2730 2740 2750
ATFQIQSFDI VCSPVWTSRD RCCDIPSRRD EAKCPALPNA CTCTQDSVGP
2760 2770 2780 2790 2800
PGPPGPAGGP GAKGPRGERG INGAVGPPGP RGDTGPPGPQ GPPGPQGPNG
2810 2820 2830 2840 2850
LSIPGEQGRQ GMKGDAGEPG LPGRTGTPGL PGPPGPMGPP GDRGFTGKDG
2860 2870 2880 2890 2900
AMGPRGPPGP PGSPGSPGVT GPSGKPGKPG DHGRPGQSGL KGEKGDRGDI
2910 2920 2930 2940 2950
ASQNMMRAVA RQVCEQLISG QMSRFNQMLN QIPNDYHSSR NQPGPPGPPG
2960 2970 2980 2990 3000
PPGSAGARGE PGPGGRPGFP GTPGMQGPPG ERGLPGEKGE RGTGSQGPRG
3010 3020 3030 3040 3050
PPGPPGPQGE SRTGPPGSTG SRGPPGPPGR PGNSGIRGPP GPPGYCDSSQ
3060 3070 3080 3090 3100
CASIPYNGQG YPEPYVPEGG AYLPEREPFI VPVEPERTAE YEDDYGADEP
3110 3120
DQQHPDHMRW RRALRPGPAE
Length:3,120
Mass (Da):340,214
Last modified:March 6, 2007 - v3
Checksum:iC4D9264E3C5C8CB5
GO
Isoform 2 (identifier: Q60847-2) [UniParc]FASTAAdd to Basket

Also known as: ER#K, XIIA-2

The sequence of this isoform differs from the canonical sequence as follows:
     3063-3065: EPY → GSG
     3066-3120: Missing.

Show »
Length:3,065
Mass (Da):333,671
Checksum:i0FE5F351A4051FD7
GO
Isoform 3 (identifier: Q60847-3) [UniParc]FASTAAdd to Basket

Also known as: XIIB-1

The sequence of this isoform differs from the canonical sequence as follows:
     25-1186: Missing.

Show »
Length:1,958
Mass (Da):212,624
Checksum:i9F869932749E4D20
GO
Isoform 4 (identifier: Q60847-4) [UniParc]FASTAAdd to Basket

Also known as: XIIB-2

The sequence of this isoform differs from the canonical sequence as follows:
     25-1186: Missing.
     3063-3065: EPY → GSG
     3066-3120: Missing.

Show »
Length:1,903
Mass (Da):206,081
Checksum:iB5A0AF0676EFC951
GO
Isoform 5 (identifier: Q60847-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     3063-3068: EPYVPE → GMLLPS
     3069-3120: Missing.

Show »
Length:3,068
Mass (Da):334,069
Checksum:i72C55C50A6D351A4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti245 – 2451A → G in AAA99719. (PubMed:8601036)Curated
Sequence conflicti421 – 4211K → KTQPK in AAA99719. (PubMed:8601036)Curated
Sequence conflicti453 – 4531I → T in AAA99719. (PubMed:8601036)Curated
Sequence conflicti552 – 5521K → E in AAA99719. (PubMed:8601036)Curated
Sequence conflicti611 – 6111E → V in AAB07047. (PubMed:8601036)Curated
Sequence conflicti611 – 6111E → V in AAA99719. (PubMed:8601036)Curated
Sequence conflicti690 – 6901N → S in AAA99719. (PubMed:8601036)Curated
Sequence conflicti797 – 7971S → P in AAA99719. (PubMed:8601036)Curated
Sequence conflicti954 – 9541P → N in AAA99719. (PubMed:8601036)Curated
Sequence conflicti1079 – 10791G → R in AAA99719. (PubMed:8601036)Curated
Sequence conflicti1271 – 12711Y → N in AAA99719. (PubMed:8601036)Curated
Sequence conflicti1472 – 14721T → A in AAA99719. (PubMed:8601036)Curated
Sequence conflicti1524 – 15241G → E in AAA99719. (PubMed:8601036)Curated
Sequence conflicti1773 – 17731V → I in AAA99719. (PubMed:8601036)Curated
Sequence conflicti1831 – 18311D → G in AAA99719. (PubMed:8601036)Curated
Sequence conflicti1939 – 19391A → S in AAA99719. (PubMed:8601036)Curated
Sequence conflicti2005 – 20051N → Y in AAA99719. (PubMed:8601036)Curated
Sequence conflicti2428 – 24292PK → R in AAA99719. (PubMed:8601036)Curated
Sequence conflicti2432 – 24321V → G in AAA99719. (PubMed:8601036)Curated
Sequence conflicti2515 – 25151L → Q in AAA99719. (PubMed:8601036)Curated
Sequence conflicti2551 – 25522SY → DS in AAA99719. (PubMed:8601036)Curated
Sequence conflicti2861 – 28644Missing in AAA99719. (PubMed:8601036)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei25 – 11861162Missing in isoform 3 and isoform 4. CuratedVSP_001150Add
BLAST
Alternative sequencei3063 – 30686EPYVPE → GMLLPS in isoform 5. 1 PublicationVSP_023404
Alternative sequencei3063 – 30653EPY → GSG in isoform 2 and isoform 4. CuratedVSP_001151
Alternative sequencei3066 – 312055Missing in isoform 2 and isoform 4. CuratedVSP_001152Add
BLAST
Alternative sequencei3069 – 312052Missing in isoform 5. 1 PublicationVSP_023405Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U25652 mRNA. Translation: AAA99719.1.
AC157477 Genomic DNA. No translation available.
AC166055 Genomic DNA. No translation available.
U57095 mRNA. Translation: AAB07047.1.
CCDSiCCDS72284.1. [Q60847-2]
PIRiC44479.
D44479.
RefSeqiNP_001277237.1. NM_001290308.1. [Q60847-2]
XP_006510861.1. XM_006510798.1. [Q60847-5]
UniGeneiMm.3819.

Genome annotation databases

EnsembliENSMUST00000071750; ENSMUSP00000071662; ENSMUSG00000032332. [Q60847-2]
GeneIDi12816.
KEGGimmu:12816.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U25652 mRNA. Translation: AAA99719.1 .
AC157477 Genomic DNA. No translation available.
AC166055 Genomic DNA. No translation available.
U57095 mRNA. Translation: AAB07047.1 .
CCDSi CCDS72284.1. [Q60847-2 ]
PIRi C44479.
D44479.
RefSeqi NP_001277237.1. NM_001290308.1. [Q60847-2 ]
XP_006510861.1. XM_006510798.1. [Q60847-5 ]
UniGenei Mm.3819.

3D structure databases

ProteinModelPortali Q60847.
SMRi Q60847. Positions 25-317, 333-415, 440-616, 631-1179, 1196-1367, 1378-2312, 2325-2487, 2510-2726.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q60847. 1 interaction.
MINTi MINT-4091424.

PTM databases

PhosphoSitei Q60847.

Proteomic databases

MaxQBi Q60847.
PaxDbi Q60847.
PRIDEi Q60847.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000071750 ; ENSMUSP00000071662 ; ENSMUSG00000032332 . [Q60847-2 ]
GeneIDi 12816.
KEGGi mmu:12816.

Organism-specific databases

CTDi 1303.
MGIi MGI:88448. Col12a1.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00760000119000.
HOGENOMi HOG000111877.
HOVERGENi HBG051060.
InParanoidi Q60847.
KOi K08132.
OrthoDBi EOG71P290.
PhylomeDBi Q60847.
TreeFami TF329914.

Enzyme and pathway databases

Reactomei REACT_198984. Collagen biosynthesis and modifying enzymes.

Miscellaneous databases

PROi Q60847.
SOURCEi Search...

Gene expression databases

Bgeei Q60847.
CleanExi MM_COL12A1.
ExpressionAtlasi Q60847. baseline and differential.
Genevestigatori Q60847.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
2.60.40.10. 18 hits.
3.40.50.410. 4 hits.
InterProi IPR008160. Collagen.
IPR013320. ConA-like_dom.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR001791. Laminin_G.
IPR002035. VWF_A.
[Graphical view ]
Pfami PF01391. Collagen. 4 hits.
PF00041. fn3. 18 hits.
PF00092. VWA. 4 hits.
[Graphical view ]
SMARTi SM00060. FN3. 18 hits.
SM00210. TSPN. 1 hit.
SM00327. VWA. 4 hits.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 11 hits.
SSF49899. SSF49899. 1 hit.
SSF53300. SSF53300. 4 hits.
PROSITEi PS50853. FN3. 18 hits.
PS50234. VWFA. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of the long and short splice variants of mouse collagen XII and their tissue-specific expression during embryonic development."
    Boehme K., Li Y., Oh P.S., Olsen B.R.
    Dev. Dyn. 204:432-445(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), ALTERNATIVE SPLICING (ISOFORMS 1 AND 3).
    Strain: C57BL/6J and Swiss Webster.
    Tissue: Skin.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Structural variation of type XII collagen at its carboxyl-terminal NC1 domain generated by tissue-specific alternative splicing."
    Kania A.M., Reichenberger E., Baur S.T., Karimbux N.Y., Taylor R.W., Olsen B.R., Nishimura I.
    J. Biol. Chem. 274:22053-22059(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3047-3120, ALTERNATIVE SPLICING (ISOFORMS 2 AND 4).
    Strain: C57BL/6J.
    Tissue: Skin fibroblast.

Entry informationi

Entry nameiCOCA1_MOUSE
AccessioniPrimary (citable) accession number: Q60847
Secondary accession number(s): P70322
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: March 6, 2007
Last modified: October 29, 2014
This is version 137 of the entry and version 3 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