Q99715 (COCA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Collagen alpha-1(XII) chain

Gene names

Name:	COL12A1
Synonyms:	COL12A1L

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	3063 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Trimer of identical chains each containing 190 kDa of non-triple-helical sequences.
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
Tissue specificity	Found in collagen I-containing tissues: both isoform 1 and isoform 2 appear in amnion, chorion, skeletal muscle, small intestine, and in cell culture of dermal fibroblasts, keratinocytes and endothelial cells. Only isoform 2 is found in lung, placenta, kidney and a squamous cell carcinoma cell line. Isoform 1 is also present in the corneal epithelial Bowman's membrane (BM) and the interfibrillar matrix of the corneal stroma, but it is not detected in the limbal BM. Ref.4
Post-translational modification	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. Isoform 1 O-glycosylation; glycosaminoglycan of chondroitin-sulfate type By similarity.
Sequence similarities	Belongs to the fibril-associated collagens with interrupted helices (FACIT) family. Contains 4 collagen-like domains. Contains 18 fibronectin type-III domains. Contains 1 laminin G-like domain. Contains 4 VWFA domains.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Collagen Repeat Signal
PTM	Disulfide bond Glycoprotein Hydroxylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW collagen fibril organization Non-traceable author statement Ref.5. Source: UniProtKB skeletal system development Traceable author statement PubMed 3476925. Source: ProtInc
Cellular_component	collagen type XII Non-traceable author statement Ref.5. Source: UniProtKB endoplasmic reticulum lumen Traceable author statement. Source: Reactome extracellular space Inferred from direct assay PubMed 20551380. Source: BHF-UCL extracellular vesicular exosome Inferred from direct assay PubMed 21362503. Source: UniProtKB
Molecular_function	extracellular matrix structural constituent conferring tensile strength Non-traceable author statement Ref.5. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: The final tissue form of collagen XII may contain homotrimers of either isoform 1 or isoform 2 or any combination of isoform 1 and isoform 2.

Isoform 1 (identifier: Q99715-1)

Also known as: Long;

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.

Isoform 2 (identifier: Q99715-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     25-1188: Missing.

Isoform 4 (identifier: Q99715-4)

The sequence of this isoform differs from the canonical sequence as follows:
     2651-2726: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 3063	3040	Collagen alpha-1(XII) chain		PRO_0000005783
Regions
	Domain	24 – 112	89	Fibronectin type-III 1
	Domain	140 – 316	177	VWFA 1
	Domain	333 – 422	90	Fibronectin type-III 2
	Domain	440 – 616	177	VWFA 2
	Domain	631 – 719	89	Fibronectin type-III 3
	Domain	722 – 810	89	Fibronectin type-III 4
	Domain	813 – 901	89	Fibronectin type-III 5
	Domain	904 – 993	90	Fibronectin type-III 6
	Domain	995 – 1083	89	Fibronectin type-III 7
	Domain	1086 – 1175	90	Fibronectin type-III 8
	Domain	1199 – 1371	173	VWFA 3
	Domain	1384 – 1472	89	Fibronectin type-III 9
	Domain	1474 – 1563	90	Fibronectin type-III 10
	Domain	1565 – 1652	88	Fibronectin type-III 11
	Domain	1654 – 1743	90	Fibronectin type-III 12
	Domain	1752 – 1841	90	Fibronectin type-III 13
	Domain	1843 – 1931	89	Fibronectin type-III 14
	Domain	1933 – 2022	90	Fibronectin type-III 15
	Domain	2024 – 2113	90	Fibronectin type-III 16
	Domain	2115 – 2202	88	Fibronectin type-III 17
	Domain	2206 – 2290	85	Fibronectin type-III 18
	Domain	2323 – 2496	174	VWFA 4
	Domain	2520 – 2712	193	Laminin G-like
	Domain	2747 – 2798	52	Collagen-like 1
	Domain	2802 – 2852	51	Collagen-like 2
	Domain	2853 – 2898	46	Collagen-like 3
	Domain	2941 – 2990	50	Collagen-like 4
	Region	2451 – 2746	296	Nonhelical region (NC3)
	Region	2747 – 2898	152	Triple-helical region (COL2) with 1 imperfection
	Region	2899 – 2941	43	Nonhelical region (NC2)
	Region	2942 – 3044	103	Triple-helical region (COL1) with 2 imperfections
	Region	3045 – 3063	19	Nonhelical region (NC1)
	Motif	862 – 864	3	Cell attachment site Potential
	Motif	2779 – 2781	3	Cell attachment site Potential
	Motif	2895 – 2897	3	Cell attachment site Potential
Amino acid modifications
	Modified residue	2944	1	4-hydroxyproline By similarity
	Modified residue	2947	1	4-hydroxyproline By similarity
	Modified residue	2950	1	4-hydroxyproline By similarity
	Modified residue	2959	1	4-hydroxyproline By similarity
	Modified residue	2965	1	4-hydroxyproline By similarity
	Modified residue	2968	1	4-hydroxyproline By similarity
	Modified residue	2971	1	4-hydroxyproline By similarity
	Modified residue	2983	1	4-hydroxyproline By similarity
	Modified residue	3000	1	4-hydroxyproline By similarity
	Modified residue	3003	1	4-hydroxyproline By similarity
	Modified residue	3014	1	4-hydroxyproline By similarity
	Modified residue	3023	1	4-hydroxyproline By similarity
	Modified residue	3026	1	4-hydroxyproline By similarity
	Modified residue	3029	1	4-hydroxyproline By similarity
	Glycosylation	700	1	N-linked (GlcNAc...) Potential
	Glycosylation	798	1	O-linked (Xyl...) (chondroitin sulfate) Potential
	Glycosylation	889	1	O-linked (Xyl...) (chondroitin sulfate) Potential
	Glycosylation	981	1	O-linked (Xyl...) (chondroitin sulfate) Potential
	Glycosylation	1763	1	N-linked (GlcNAc...) Potential
	Glycosylation	2206	1	N-linked (GlcNAc...) Potential
	Glycosylation	2528	1	N-linked (GlcNAc...) Ref.6
	Glycosylation	2679	1	N-linked (GlcNAc...) Ref.6
Natural variations
	Alternative sequence	25 – 1188	1164	Missing in isoform 2.		VSP_001149
	Alternative sequence	2651 – 2726	76	Missing in isoform 4.		VSP_024942
	Natural variant	461	1	A → P. Corresponds to variant rs34730529 [ dbSNP | Ensembl ].		VAR_048768
	Natural variant	1738	1	I → T. Corresponds to variant rs240736 [ dbSNP | Ensembl ].		VAR_048769
	Natural variant	2021	1	R → Q. Corresponds to variant rs34438461 [ dbSNP | Ensembl ].		VAR_061111
	Natural variant	2160	1	E → V. Corresponds to variant rs35523808 [ dbSNP | Ensembl ].		VAR_048770
	Natural variant	2596	1	I → V. Corresponds to variant rs35710072 [ dbSNP | Ensembl ].		VAR_048771
	Natural variant	3048	1	Q → H. Corresponds to variant rs57396313 [ dbSNP | Ensembl ].		VAR_061112
	Natural variant	3058	1	G → S. Ref.1 Corresponds to variant rs970547 [ dbSNP | Ensembl ].		VAR_032059
Experimental info
	Sequence conflict	47	1	K → E in AAC51244. Ref.1
	Sequence conflict	441 – 442	2	IV → M in AAC01506. Ref.4
	Sequence conflict	581	1	R → D in AAC01506. Ref.4
	Sequence conflict	689	1	S → N in AAC01506. Ref.4
	Sequence conflict	743	1	W → S in AAC01506. Ref.4
	Sequence conflict	749	1	R → K in AAC01506. Ref.4
	Sequence conflict	753	1	Y → C in AAC51244. Ref.1
	Sequence conflict	813	1	V → G in AAC01506. Ref.4
	Sequence conflict	1355	1	A → D in AAC51244. Ref.1
	Sequence conflict	1690	1	A → G in AAC51244. Ref.1
	Sequence conflict	1729	1	P → A in AAC51244. Ref.1
	Sequence conflict	1949 – 1951	3	SLD → RLG in AAC51244. Ref.1
	Sequence conflict	2614	1	P → S in AAB23937. Ref.5
	Sequence conflict	2647 – 2648	2	SF → RK in AAB23937. Ref.5
	Sequence conflict	2848	1	G → S in AAC51244. Ref.1
	Sequence conflict	2858	1	P → R in AAC51244. Ref.1
	Sequence conflict	3035	1	R → Q in AAC51244. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified May 1, 2007. Version 2. Checksum: EA38CAFECE8393D2	FASTA	3,063	333,147
	10 20 30 40 50 60 MRSRLPPALA ALGAALLLSS IEAEVDPPSD LNFKIIDENT VHMSWAKPVD PIVGYRITVD 70 80 90 100 110 120 PTTDGPTKEF TLSASTTETL LSELVPETEY VVTITSYDEV EESVPVIGQL TIQTGSSTKP 130 140 150 160 170 180 VEKKPGKTEI QKCSVSAWTD LVFLVDGSWS VGRNNFKYIL DFIAALVSAF DIGEEKTRVG 190 200 210 220 230 240 VVQYSSDTRT EFNLNQYYQR DELLAAIKKI PYKGGNTMTG DAIDYLVKNT FTESAGARVG 250 260 270 280 290 300 FPKVAIIITD GKSQDEVEIP ARELRNVGVE VFSLGIKAAD AKELKQIAST PSLNHVFNVA 310 320 330 340 350 360 NFDAIVDIQN EIISQVCSGV DEQLGELVSG EEVVEPPSNL IAMEVSSKYV KLNWNPSPSP 370 380 390 400 410 420 VTGYKVILTP MTAGSRQHAL SVGPQTTTLS VRDLSADTEY QISVSAMKGM TSSEPISIME 430 440 450 460 470 480 KTQPMKVQVE CSRGVDIKAD IVFLVDGSYS IGIANFVKVR AFLEVLVKSF EISPNRVQIS 490 500 510 520 530 540 LVQYSRDPHT EFTLKKFTKV EDIIEAINTF PYRGGSTNTG KAMTYVREKI FVPSKGSRSN 550 560 570 580 590 600 VPKVMILITD GKSSDAFRDP AIKLRNSDVE IFAVGVKDAV RSELEAIASP PAETHVFTVE 610 620 630 640 650 660 DFDAFQRISF ELTQSICLRI EQELAAIKKK AYVPPKDLSF SEVTSYGFKT NWSPAGENVF 670 680 690 700 710 720 SYHITYKEAA GDDEVTVVEP ASSTSVVLSS LKPETLYLVN VTAEYEDGFS IPLAGEETTE 730 740 750 760 770 780 EVKGAPRNLK VTDETTDSFK ITWTQAPGRV LRYRIIYRPV AGGESREVTT PPNQRRRTLE 790 800 810 820 830 840 NLIPDTKYEV SVIPEYFSGP GTPLTGNAAT EEVRGNPRDL RVSDPTTSTM KLSWSGAPGK 850 860 870 880 890 900 VKQYLVTYTP VAGGETQEVT VRGDTTNTVL QGLKEGTQYA LSVTALYASG AGDALFGEGT 910 920 930 940 950 960 TLEERGSPQD LVTKDITDTS IGAYWTSAPG MVRGYRVSWK SLYDDVDTGE KNLPEDAIHT 970 980 990 1000 1010 1020 MIENLQPETK YRISVFATYS SGEGEPLTGD ATTELSQDSK TLKVDEETEN TMRVTWKPAP 1030 1040 1050 1060 1070 1080 GKVVNYRVVY RPHGRGKQMV AKVPPTVTST VLKRLQPQTT YDITVLPIYK MGEGKLRQGS 1090 1100 1110 1120 1130 1140 GTTASRFKSP RNLKTSDPTM SSFRVTWEPA PGEVKGYKVT FHPTGDDRRL GELVVGPYDN 1150 1160 1170 1180 1190 1200 TVVLEELRAG TTYKVNVFGM FDGGESSPLV GQEMTTLSDT TVMPILSSGM ECLTRAEADI 1210 1220 1230 1240 1250 1260 VLLVDGSWSI GRANFRTVRS FISRIVEVFD IGPKRVQIAL AQYSGDPRTE WQLNAHRDKK 1270 1280 1290 1300 1310 1320 SLLQAVANLP YKGGNTLTGM ALNFIRQQNF RTQAGMRPRA RKIGVLITDG KSQDDVEAPS 1330 1340 1350 1360 1370 1380 KKLKDEGVEL FAIGIKNADE VELKMIATDP DDTHAYNVAD FESLSRIVDD LTINLCNSVK 1390 1400 1410 1420 1430 1440 GPGDLEAPSN LVISERTHRS FRVSWTPPSD SVDRYKVEYY PVSGGKRQEF YVSRMETSTV 1450 1460 1470 1480 1490 1500 LKDLKPETEY VVNVYSVVED EYSEPLKGTE KTLPVPVVSL NIYDVGPTTM HVQWQPVGGA 1510 1520 1530 1540 1550 1560 TGYILSYKPV KDTEPTRPKE VRLGPTVNDM QLTDLVPNTE YAVTVQAVLH DLTSEPVTVR 1570 1580 1590 1600 1610 1620 EVTLPLPRPQ DLKLRDVTHS TMNVFWEPVP GKVRKYIVRY KTPEEDVKEV EVDRSETSTS 1630 1640 1650 1660 1670 1680 LKDLFSQTLY TVSVSAVHDE GESPPVTAQE TTRPVPAPTN LKITEVTSEG FRGTWDHGAS 1690 1700 1710 1720 1730 1740 DVSLYRITWA PFGSSDKMET ILNGDENTLV FENLNPNTIY EVSITAIYPD ESESDDLIGS 1750 1760 1770 1780 1790 1800 ERTLPILTTQ APKSGPRNLQ VYNATSNSLT VKWDPASGRV QKYRITYQPS TGEGNEQTTT 1810 1820 1830 1840 1850 1860 IGGRQNSVVL QKLKPDTPYT ITVSSLYPDG EGGRMTGRGK TKPLNTVRNL RVYDPSTSTL 1870 1880 1890 1900 1910 1920 NVRWDHAEGN PRQYKLFYAP AAGGPEELVP IPGNTNYAIL RNLQPDTSYT VTVVPVYTEG 1930 1940 1950 1960 1970 1980 DGGRTSDTGR TLMRGLARNV QVYNPTPNSL DVRWDPAPGP VLQYRVVYSP VDGTRPSESI 1990 2000 2010 2020 2030 2040 VVPGNTRMVH LERLIPDTLY SVNLVALYSD GEGNPSPAQG RTLPRSGPRN LRVFGETTNS 2050 2060 2070 2080 2090 2100 LSVAWDHADG PVQQYRIIYS PTVGDPIDEY TTVPGRRNNV ILQPLQPDTP YKITVIAVYE 2110 2120 2130 2140 2150 2160 DGDGGHLTGN GRTVGLLPPQ NIHISDEWYT RFRVSWDPSP SPVLGYKIVY KPVGSNEPME 2170 2180 2190 2200 2210 2220 AFVGEMTSYT LHNLNPSTTY DVNVYAQYDS GLSVPLTDQG TTLYLNVTDL KTYQIGWDTF 2230 2240 2250 2260 2270 2280 CVKWSPHRAA TSYRLKLSPA DGTRGQEITV RGSETSHCFT GLSPDTDYGV TVFVQTPNLE 2290 2300 2310 2320 2330 2340 GPGVSVKEHT TVKPTEAPTE PPTPPPPPTI PPARDVCKGA KADIVFLTDA SWSIGDDNFN 2350 2360 2370 2380 2390 2400 KVVKFIFNTV GGFDEISPAG IQVSFVQYSD EVKSEFKLNT YNDKALALGA LQNIRYRGGN 2410 2420 2430 2440 2450 2460 TRTGKALTFI KEKVLTWESG MRKNVPKVLV VVTDGRSQDE VKKAALVIQQ SGFSVFVVGV 2470 2480 2490 2500 2510 2520 ADVDYNELAN IASKPSERHV FIVDDFESFE KIEDNLITFV CETATSSCPL IYLDGYTSPG 2530 2540 2550 2560 2570 2580 FKMLEAYNLT EKNFASVQGV SLESGSFPSY SAYRIQKNAF VNQPTADLHP NGLPPSYTII 2590 2600 2610 2620 2630 2640 LLFRLLPETP SDPFAIWQIT DRDYKPQVGV IADPSSKTLS FFNKDTRGEV QTVTFDTEEV 2650 2660 2670 2680 2690 2700 KTLFYGSFHK VHIVVTSKSV KIYIDCYEII EKDIKEAGNI TTDGYEILGK LLKGERKSAA 2710 2720 2730 2740 2750 2760 FQIQSFDIVC SPVWTSRDRC CDIPSRRDEG KCPAFPNSCT CTQDSVGPPG PPGPAGGPGA 2770 2780 2790 2800 2810 2820 KGPRGERGIS GAIGPPGPRG DIGPPGPQGP PGPQGPNGLS IPGEQGRQGM KGDAGEPGLP 2830 2840 2850 2860 2870 2880 GRTGTPGLPG PPGPMGPPGD RGFTGKDGAM GPRGPPGPPG SPGSPGVTGP SGKPGKPGDH 2890 2900 2910 2920 2930 2940 GRPGPSGLKG EKGDRGDIAS QNMMRAVARQ VCEQLISGQM NRFNQMLNQI PNDYQSSRNQ 2950 2960 2970 2980 2990 3000 PGPPGPPGPP GSAGARGEPG PGGRPGFPGT PGMQGPPGER GLPGEKGERG TGSSGPRGLP 3010 3020 3030 3040 3050 3060 GPPGPQGESR TGPPGSTGSR GPPGPPGRPG NSGIRGPPGP PGYCDSSQCA SIPYNGQGYP GSG
	Isoform 2 (Short) [UniParc]. Checksum: ECFB9F5436FF7B24	FASTA	1,899	205,491
	10 20 30 40 50 60 MRSRLPPALA ALGAALLLSS IEAEGMECLT RAEADIVLLV DGSWSIGRAN FRTVRSFISR 70 80 90 100 110 120 IVEVFDIGPK RVQIALAQYS GDPRTEWQLN AHRDKKSLLQ AVANLPYKGG NTLTGMALNF 130 140 150 160 170 180 IRQQNFRTQA GMRPRARKIG VLITDGKSQD DVEAPSKKLK DEGVELFAIG IKNADEVELK 190 200 210 220 230 240 MIATDPDDTH AYNVADFESL SRIVDDLTIN LCNSVKGPGD LEAPSNLVIS ERTHRSFRVS 250 260 270 280 290 300 WTPPSDSVDR YKVEYYPVSG GKRQEFYVSR METSTVLKDL KPETEYVVNV YSVVEDEYSE 310 320 330 340 350 360 PLKGTEKTLP VPVVSLNIYD VGPTTMHVQW QPVGGATGYI LSYKPVKDTE PTRPKEVRLG 370 380 390 400 410 420 PTVNDMQLTD LVPNTEYAVT VQAVLHDLTS EPVTVREVTL PLPRPQDLKL RDVTHSTMNV 430 440 450 460 470 480 FWEPVPGKVR KYIVRYKTPE EDVKEVEVDR SETSTSLKDL FSQTLYTVSV SAVHDEGESP 490 500 510 520 530 540 PVTAQETTRP VPAPTNLKIT EVTSEGFRGT WDHGASDVSL YRITWAPFGS SDKMETILNG 550 560 570 580 590 600 DENTLVFENL NPNTIYEVSI TAIYPDESES DDLIGSERTL PILTTQAPKS GPRNLQVYNA 610 620 630 640 650 660 TSNSLTVKWD PASGRVQKYR ITYQPSTGEG NEQTTTIGGR QNSVVLQKLK PDTPYTITVS 670 680 690 700 710 720 SLYPDGEGGR MTGRGKTKPL NTVRNLRVYD PSTSTLNVRW DHAEGNPRQY KLFYAPAAGG 730 740 750 760 770 780 PEELVPIPGN TNYAILRNLQ PDTSYTVTVV PVYTEGDGGR TSDTGRTLMR GLARNVQVYN 790 800 810 820 830 840 PTPNSLDVRW DPAPGPVLQY RVVYSPVDGT RPSESIVVPG NTRMVHLERL IPDTLYSVNL 850 860 870 880 890 900 VALYSDGEGN PSPAQGRTLP RSGPRNLRVF GETTNSLSVA WDHADGPVQQ YRIIYSPTVG 910 920 930 940 950 960 DPIDEYTTVP GRRNNVILQP LQPDTPYKIT VIAVYEDGDG GHLTGNGRTV GLLPPQNIHI 970 980 990 1000 1010 1020 SDEWYTRFRV SWDPSPSPVL GYKIVYKPVG SNEPMEAFVG EMTSYTLHNL NPSTTYDVNV 1030 1040 1050 1060 1070 1080 YAQYDSGLSV PLTDQGTTLY LNVTDLKTYQ IGWDTFCVKW SPHRAATSYR LKLSPADGTR 1090 1100 1110 1120 1130 1140 GQEITVRGSE TSHCFTGLSP DTDYGVTVFV QTPNLEGPGV SVKEHTTVKP TEAPTEPPTP 1150 1160 1170 1180 1190 1200 PPPPTIPPAR DVCKGAKADI VFLTDASWSI GDDNFNKVVK FIFNTVGGFD EISPAGIQVS 1210 1220 1230 1240 1250 1260 FVQYSDEVKS EFKLNTYNDK ALALGALQNI RYRGGNTRTG KALTFIKEKV LTWESGMRKN 1270 1280 1290 1300 1310 1320 VPKVLVVVTD GRSQDEVKKA ALVIQQSGFS VFVVGVADVD YNELANIASK PSERHVFIVD 1330 1340 1350 1360 1370 1380 DFESFEKIED NLITFVCETA TSSCPLIYLD GYTSPGFKML EAYNLTEKNF ASVQGVSLES 1390 1400 1410 1420 1430 1440 GSFPSYSAYR IQKNAFVNQP TADLHPNGLP PSYTIILLFR LLPETPSDPF AIWQITDRDY 1450 1460 1470 1480 1490 1500 KPQVGVIADP SSKTLSFFNK DTRGEVQTVT FDTEEVKTLF YGSFHKVHIV VTSKSVKIYI 1510 1520 1530 1540 1550 1560 DCYEIIEKDI KEAGNITTDG YEILGKLLKG ERKSAAFQIQ SFDIVCSPVW TSRDRCCDIP 1570 1580 1590 1600 1610 1620 SRRDEGKCPA FPNSCTCTQD SVGPPGPPGP AGGPGAKGPR GERGISGAIG PPGPRGDIGP 1630 1640 1650 1660 1670 1680 PGPQGPPGPQ GPNGLSIPGE QGRQGMKGDA GEPGLPGRTG TPGLPGPPGP MGPPGDRGFT 1690 1700 1710 1720 1730 1740 GKDGAMGPRG PPGPPGSPGS PGVTGPSGKP GKPGDHGRPG PSGLKGEKGD RGDIASQNMM 1750 1760 1770 1780 1790 1800 RAVARQVCEQ LISGQMNRFN QMLNQIPNDY QSSRNQPGPP GPPGPPGSAG ARGEPGPGGR 1810 1820 1830 1840 1850 1860 PGFPGTPGMQ GPPGERGLPG EKGERGTGSS GPRGLPGPPG PQGESRTGPP GSTGSRGPPG 1870 1880 1890 PPGRPGNSGI RGPPGPPGYC DSSQCASIPY NGQGYPGSG
	Isoform 4 [UniParc]. Checksum: E5EEB57CBFB556E2	FASTA	2,987	324,570
	10 20 30 40 50 60 MRSRLPPALA ALGAALLLSS IEAEVDPPSD LNFKIIDENT VHMSWAKPVD PIVGYRITVD 70 80 90 100 110 120 PTTDGPTKEF TLSASTTETL LSELVPETEY VVTITSYDEV EESVPVIGQL TIQTGSSTKP 130 140 150 160 170 180 VEKKPGKTEI QKCSVSAWTD LVFLVDGSWS VGRNNFKYIL DFIAALVSAF DIGEEKTRVG 190 200 210 220 230 240 VVQYSSDTRT EFNLNQYYQR DELLAAIKKI PYKGGNTMTG DAIDYLVKNT FTESAGARVG 250 260 270 280 290 300 FPKVAIIITD GKSQDEVEIP ARELRNVGVE VFSLGIKAAD AKELKQIAST PSLNHVFNVA 310 320 330 340 350 360 NFDAIVDIQN EIISQVCSGV DEQLGELVSG EEVVEPPSNL IAMEVSSKYV KLNWNPSPSP 370 380 390 400 410 420 VTGYKVILTP MTAGSRQHAL SVGPQTTTLS VRDLSADTEY QISVSAMKGM TSSEPISIME 430 440 450 460 470 480 KTQPMKVQVE CSRGVDIKAD IVFLVDGSYS IGIANFVKVR AFLEVLVKSF EISPNRVQIS 490 500 510 520 530 540 LVQYSRDPHT EFTLKKFTKV EDIIEAINTF PYRGGSTNTG KAMTYVREKI FVPSKGSRSN 550 560 570 580 590 600 VPKVMILITD GKSSDAFRDP AIKLRNSDVE IFAVGVKDAV RSELEAIASP PAETHVFTVE 610 620 630 640 650 660 DFDAFQRISF ELTQSICLRI EQELAAIKKK AYVPPKDLSF SEVTSYGFKT NWSPAGENVF 670 680 690 700 710 720 SYHITYKEAA GDDEVTVVEP ASSTSVVLSS LKPETLYLVN VTAEYEDGFS IPLAGEETTE 730 740 750 760 770 780 EVKGAPRNLK VTDETTDSFK ITWTQAPGRV LRYRIIYRPV AGGESREVTT PPNQRRRTLE 790 800 810 820 830 840 NLIPDTKYEV SVIPEYFSGP GTPLTGNAAT EEVRGNPRDL RVSDPTTSTM KLSWSGAPGK 850 860 870 880 890 900 VKQYLVTYTP VAGGETQEVT VRGDTTNTVL QGLKEGTQYA LSVTALYASG AGDALFGEGT 910 920 930 940 950 960 TLEERGSPQD LVTKDITDTS IGAYWTSAPG MVRGYRVSWK SLYDDVDTGE KNLPEDAIHT 970 980 990 1000 1010 1020 MIENLQPETK YRISVFATYS SGEGEPLTGD ATTELSQDSK TLKVDEETEN TMRVTWKPAP 1030 1040 1050 1060 1070 1080 GKVVNYRVVY RPHGRGKQMV AKVPPTVTST VLKRLQPQTT YDITVLPIYK MGEGKLRQGS 1090 1100 1110 1120 1130 1140 GTTASRFKSP RNLKTSDPTM SSFRVTWEPA PGEVKGYKVT FHPTGDDRRL GELVVGPYDN 1150 1160 1170 1180 1190 1200 TVVLEELRAG TTYKVNVFGM FDGGESSPLV GQEMTTLSDT TVMPILSSGM ECLTRAEADI 1210 1220 1230 1240 1250 1260 VLLVDGSWSI GRANFRTVRS FISRIVEVFD IGPKRVQIAL AQYSGDPRTE WQLNAHRDKK 1270 1280 1290 1300 1310 1320 SLLQAVANLP YKGGNTLTGM ALNFIRQQNF RTQAGMRPRA RKIGVLITDG KSQDDVEAPS 1330 1340 1350 1360 1370 1380 KKLKDEGVEL FAIGIKNADE VELKMIATDP DDTHAYNVAD FESLSRIVDD LTINLCNSVK 1390 1400 1410 1420 1430 1440 GPGDLEAPSN LVISERTHRS FRVSWTPPSD SVDRYKVEYY PVSGGKRQEF YVSRMETSTV 1450 1460 1470 1480 1490 1500 LKDLKPETEY VVNVYSVVED EYSEPLKGTE KTLPVPVVSL NIYDVGPTTM HVQWQPVGGA 1510 1520 1530 1540 1550 1560 TGYILSYKPV KDTEPTRPKE VRLGPTVNDM QLTDLVPNTE YAVTVQAVLH DLTSEPVTVR 1570 1580 1590 1600 1610 1620 EVTLPLPRPQ DLKLRDVTHS TMNVFWEPVP GKVRKYIVRY KTPEEDVKEV EVDRSETSTS 1630 1640 1650 1660 1670 1680 LKDLFSQTLY TVSVSAVHDE GESPPVTAQE TTRPVPAPTN LKITEVTSEG FRGTWDHGAS 1690 1700 1710 1720 1730 1740 DVSLYRITWA PFGSSDKMET ILNGDENTLV FENLNPNTIY EVSITAIYPD ESESDDLIGS 1750 1760 1770 1780 1790 1800 ERTLPILTTQ APKSGPRNLQ VYNATSNSLT VKWDPASGRV QKYRITYQPS TGEGNEQTTT 1810 1820 1830 1840 1850 1860 IGGRQNSVVL QKLKPDTPYT ITVSSLYPDG EGGRMTGRGK TKPLNTVRNL RVYDPSTSTL 1870 1880 1890 1900 1910 1920 NVRWDHAEGN PRQYKLFYAP AAGGPEELVP IPGNTNYAIL RNLQPDTSYT VTVVPVYTEG 1930 1940 1950 1960 1970 1980 DGGRTSDTGR TLMRGLARNV QVYNPTPNSL DVRWDPAPGP VLQYRVVYSP VDGTRPSESI 1990 2000 2010 2020 2030 2040 VVPGNTRMVH LERLIPDTLY SVNLVALYSD GEGNPSPAQG RTLPRSGPRN LRVFGETTNS 2050 2060 2070 2080 2090 2100 LSVAWDHADG PVQQYRIIYS PTVGDPIDEY TTVPGRRNNV ILQPLQPDTP YKITVIAVYE 2110 2120 2130 2140 2150 2160 DGDGGHLTGN GRTVGLLPPQ NIHISDEWYT RFRVSWDPSP SPVLGYKIVY KPVGSNEPME 2170 2180 2190 2200 2210 2220 AFVGEMTSYT LHNLNPSTTY DVNVYAQYDS GLSVPLTDQG TTLYLNVTDL KTYQIGWDTF 2230 2240 2250 2260 2270 2280 CVKWSPHRAA TSYRLKLSPA DGTRGQEITV RGSETSHCFT GLSPDTDYGV TVFVQTPNLE 2290 2300 2310 2320 2330 2340 GPGVSVKEHT TVKPTEAPTE PPTPPPPPTI PPARDVCKGA KADIVFLTDA SWSIGDDNFN 2350 2360 2370 2380 2390 2400 KVVKFIFNTV GGFDEISPAG IQVSFVQYSD EVKSEFKLNT YNDKALALGA LQNIRYRGGN 2410 2420 2430 2440 2450 2460 TRTGKALTFI KEKVLTWESG MRKNVPKVLV VVTDGRSQDE VKKAALVIQQ SGFSVFVVGV 2470 2480 2490 2500 2510 2520 ADVDYNELAN IASKPSERHV FIVDDFESFE KIEDNLITFV CETATSSCPL IYLDGYTSPG 2530 2540 2550 2560 2570 2580 FKMLEAYNLT EKNFASVQGV SLESGSFPSY SAYRIQKNAF VNQPTADLHP NGLPPSYTII 2590 2600 2610 2620 2630 2640 LLFRLLPETP SDPFAIWQIT DRDYKPQVGV IADPSSKTLS FFNKDTRGEV QTVTFDTEEV 2650 2660 2670 2680 2690 2700 KTLFYGSFHK RDEGKCPAFP NSCTCTQDSV GPPGPPGPAG GPGAKGPRGE RGISGAIGPP 2710 2720 2730 2740 2750 2760 GPRGDIGPPG PQGPPGPQGP NGLSIPGEQG RQGMKGDAGE PGLPGRTGTP GLPGPPGPMG 2770 2780 2790 2800 2810 2820 PPGDRGFTGK DGAMGPRGPP GPPGSPGSPG VTGPSGKPGK PGDHGRPGPS GLKGEKGDRG 2830 2840 2850 2860 2870 2880 DIASQNMMRA VARQVCEQLI SGQMNRFNQM LNQIPNDYQS SRNQPGPPGP PGPPGSAGAR 2890 2900 2910 2920 2930 2940 GEPGPGGRPG FPGTPGMQGP PGERGLPGEK GERGTGSSGP RGLPGPPGPQ GESRTGPPGS 2950 2960 2970 2980 TGSRGPPGPP GRPGNSGIRG PPGPPGYCDS SQCASIPYNG QGYPGSG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete primary structure of two splice variants of collagen XII, and assignment of alpha 1(XII) collagen (COL12A1), alpha 1(IX) collagen (COL9A1), and alpha 1(XIX) collagen (COL19A1) to human chromosome 6q12-q13." Gerecke D.R., Olson P.F., Koch M., Knoll J.H.M., Taylor R., Hudson D.L., Champliaud M.-F., Olsen B.R., Burgeson R.E. Genomics 41:236-242(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 1280-1295; 1782-1801 AND 2906-2916, VARIANT SER-3058.
[2]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The chick and human collagen alpha1(XII) gene promoter -- activity of highly conserved regions around the first exon and in the first intron." Chiquet M., Mumenthaler U., Wittwer M., Jin W., Koch M. Eur. J. Biochem. 257:362-371(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
[4]	"Type XII collagen contributes to diversities in human corneal and limbal extracellular matrices." Wessel H., Anderson S., Fite D., Halvas E., Hempel J., SundarRaj N. Invest. Ophthalmol. Vis. Sci. 38:2408-2422(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 299-816 (ISOFORMS 1/4), TISSUE SPECIFICITY. Tissue: Cornea.
[5]	"The mouse alpha 1(XII) and human alpha 1(XII)-like collagen genes are localized on mouse chromosome 9 and human chromosome 6." Oh S.P., Taylor R.W., Gerecke D.R., Rochelle J.M., Seldin M.F., Olsen B.R. Genomics 14:225-231(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2567-2755 (ISOFORM 4).
[6]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2528 AND ASN-2679, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U73778 mRNA. Translation: AAC51244.1. U73779 mRNA. Translation: AAD40483.1. AL080250, AL096771, AL354664 Genomic DNA. Translation: CAI19898.1. AL354664, AL080250, AL096771 Genomic DNA. Translation: CAH71310.1. AL096771, AL354664, AL080250 Genomic DNA. Translation: CAI19908.1. AF061871 Genomic DNA. Translation: AAC83578.1. U68139 mRNA. Translation: AAC01506.1. AH004088 Genomic DNA. Translation: AAB23937.2.
IPI	IPI00221384. IPI00302944. IPI00329573.
PIR	A44479.
RefSeq	NP_004361.3. NM_004370.5. NP_542376.2. NM_080645.2.
UniGene	Hs.101302.
3D structure databases
ProteinModelPortal	Q99715.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99715. 5 interactions.
STRING	9606.ENSP00000325146.
PTM databases
PhosphoSite	Q99715.
Polymorphism databases
DMDM	146345397.
Proteomic databases
PaxDb	Q99715.
PRIDE	Q99715.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000322507; ENSP00000325146; ENSG00000111799. ENST00000345356; ENSP00000305147; ENSG00000111799. ENST00000416123; ENSP00000412864; ENSG00000111799.
GeneID	1303.
KEGG	hsa:1303.
UCSC	uc003phs.3. human. uc003pht.3. human.
Organism-specific databases
CTD	1303.
GeneCards	GC06M075850.
H-InvDB	HIX0006013.
HGNC	HGNC:2188. COL12A1.
HPA	HPA009143.
MIM	120320. gene.
neXtProt	NX_Q99715.
PharmGKB	PA26704.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG12793.
HOVERGEN	HBG051060.
InParanoid	Q99715.
KO	K08132.
OMA	NTEYAVT.
OrthoDB	EOG4BCDM1.
Enzyme and pathway databases
Reactome	REACT_118779. Extracellular matrix organization.
Gene expression databases
ArrayExpress	Q99715.
Bgee	Q99715.
CleanEx	HS_COL12A1.
Genevestigator	Q99715.
GermOnline	ENSG00000111799. Homo sapiens.
Family and domain databases
Gene3D	2.60.120.200. 1 hit. 2.60.40.10. 18 hits.
InterPro	IPR008160. Collagen. IPR008985. ConA-like_lec_gl_sf. IPR013320. ConA-like_subgrp. IPR003961. Fibronectin_type3. IPR013783. Ig-like_fold. IPR001791. Laminin_G. IPR002035. VWF_A. [Graphical view]
Pfam	PF01391. Collagen. 4 hits. PF00041. fn3. 18 hits. PF00092. VWA. 4 hits. [Graphical view]
SMART	SM00060. FN3. 18 hits. SM00210. TSPN. 1 hit. SM00327. VWA. 4 hits. [Graphical view]
SUPFAM	SSF49899. ConA_like_lec_gl. 1 hit. SSF49265. FN_III-like. 18 hits.
PROSITE	PS50853. FN3. 18 hits. PS50025. LAM_G_DOMAIN. False negative. PS50234. VWFA. 4 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	COL12A1. human.
GenomeRNAi	1303.
NextBio	5299.
SOURCE	Search...

Entry information

Entry name

COCA1_HUMAN

Accession

Primary (citable) accession number: Q99715
Secondary accession number(s): O43853 , Q15955, Q5VYK1, Q5VYK2, Q71UR3, Q99716

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	May 1, 2007
Last modified:	May 1, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.