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Q60847 (COCA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(XII) chain
Gene names
Name:Col12a1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length3120 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Tissue specificity

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

Developmental stage

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).

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.

O-glycosylation of isoform 2;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.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: The final tissue form of collagen XII may contain homotrimers or any combination of the various isoforms.
Isoform 1 (identifier: Q60847-1)

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.
Isoform 2 (identifier: Q60847-2)

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.
Isoform 3 (identifier: Q60847-3)

Also known as: XIIB-1;

The sequence of this isoform differs from the canonical sequence as follows:
     25-1186: Missing.
Isoform 4 (identifier: Q60847-4)

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.
Isoform 5 (identifier: Q60847-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 31203097Collagen alpha-1(XII) chain
PRO_0000005784

Regions

Domain27 – 11791Fibronectin type-III 1
Domain140 – 316177VWFA 1
Domain336 – 42691Fibronectin type-III 2
Domain440 – 616177VWFA 2
Domain634 – 72390Fibronectin type-III 3
Domain725 – 81692Fibronectin type-III 4
Domain817 – 90589Fibronectin type-III 5
Domain907 – 99892Fibronectin type-III 6
Domain1000 – 108788Fibronectin type-III 7
Domain1089 – 117991Fibronectin type-III 8
Domain1199 – 1371173VWFA 3
Domain1387 – 147589Fibronectin type-III 9
Domain1476 – 156792Fibronectin type-III 10
Domain1568 – 165891Fibronectin type-III 11
Domain1659 – 175496Fibronectin type-III 12
Domain1757 – 185195Fibronectin type-III 13
Domain1852 – 193786Fibronectin type-III 14
Domain1938 – 202891Fibronectin type-III 15
Domain2029 – 211991Fibronectin type-III 16
Domain2120 – 220889Fibronectin type-III 17
Domain2209 – 229688Fibronectin type-III 18
Domain2325 – 2498174VWFA 4
Domain2522 – 2714193Laminin G-like
Domain2749 – 280052Collagen-like 1
Domain2804 – 285451Collagen-like 2
Domain2855 – 289945Collagen-like 3
Domain2943 – 299250Collagen-like 4
Region2453 – 2748296Nonhelical region (NC3)
Region2749 – 2900152Triple-helical region (COL2) with 1 imperfection
Region2901 – 294343Nonhelical region (NC2)
Region2944 – 3046103Triple-helical region (COL1) with 2 imperfections
Region3047 – 312074Nonhelical region (NC1)
Motif862 – 8643Cell attachment site Potential
Motif2781 – 27833Cell attachment site Potential
Motif2897 – 28993Cell attachment site Potential
Compositional bias865 – 8684Poly-Thr

Amino acid modifications

Modified residue294614-hydroxyproline By similarity
Modified residue294914-hydroxyproline By similarity
Modified residue295214-hydroxyproline By similarity
Modified residue296114-hydroxyproline By similarity
Modified residue296714-hydroxyproline By similarity
Modified residue297014-hydroxyproline By similarity
Modified residue297314-hydroxyproline By similarity
Modified residue298514-hydroxyproline By similarity
Modified residue300214-hydroxyproline By similarity
Modified residue300514-hydroxyproline By similarity
Modified residue301614-hydroxyproline By similarity
Modified residue302514-hydroxyproline By similarity
Modified residue302814-hydroxyproline By similarity
Modified residue303114-hydroxyproline By similarity
Glycosylation7001N-linked (GlcNAc...) Potential
Glycosylation7981O-linked (Xyl...) (chondroitin sulfate) Potential
Glycosylation8891O-linked (Xyl...) (chondroitin sulfate) Potential
Glycosylation9811O-linked (Xyl...) (chondroitin sulfate) Potential
Glycosylation17651N-linked (GlcNAc...) Potential
Glycosylation22081N-linked (GlcNAc...) Potential
Glycosylation25301N-linked (GlcNAc...) Potential
Glycosylation26811N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence25 – 11861162Missing in isoform 3 and isoform 4.
VSP_001150
Alternative sequence3063 – 30686EPYVPE → GMLLPS in isoform 5.
VSP_023404
Alternative sequence3063 – 30653EPY → GSG in isoform 2 and isoform 4.
VSP_001151
Alternative sequence3066 – 312055Missing in isoform 2 and isoform 4.
VSP_001152
Alternative sequence3069 – 312052Missing in isoform 5.
VSP_023405

Experimental info

Sequence conflict2451A → G in AAA99719. Ref.1
Sequence conflict4211K → KTQPK in AAA99719. Ref.1
Sequence conflict4531I → T in AAA99719. Ref.1
Sequence conflict5521K → E in AAA99719. Ref.1
Sequence conflict6111E → V in AAB07047. Ref.1
Sequence conflict6111E → V in AAA99719. Ref.1
Sequence conflict6901N → S in AAA99719. Ref.1
Sequence conflict7971S → P in AAA99719. Ref.1
Sequence conflict9541P → N in AAA99719. Ref.1
Sequence conflict10791G → R in AAA99719. Ref.1
Sequence conflict12711Y → N in AAA99719. Ref.1
Sequence conflict14721T → A in AAA99719. Ref.1
Sequence conflict15241G → E in AAA99719. Ref.1
Sequence conflict17731V → I in AAA99719. Ref.1
Sequence conflict18311D → G in AAA99719. Ref.1
Sequence conflict19391A → S in AAA99719. Ref.1
Sequence conflict20051N → Y in AAA99719. Ref.1
Sequence conflict2428 – 24292PK → R in AAA99719. Ref.1
Sequence conflict24321V → G in AAA99719. Ref.1
Sequence conflict25151L → Q in AAA99719. Ref.1
Sequence conflict2551 – 25522SY → DS in AAA99719. Ref.1
Sequence conflict2861 – 28644Missing in AAA99719. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (XIIA-1) [UniParc].

Last modified March 6, 2007. Version 3.
Checksum: C4D9264E3C5C8CB5

FASTA3,120340,214
        10         20         30         40         50         60 
MQTRLPRALA ALGVALLLSS IEAEVDPPSD LNFKIIDENT VHMSWERPVD PIVGYRITVD 

        70         80         90        100        110        120 
PTTDGPTKEF TLAASTTETL LSDLIPETQY VVTITSYNEV EESVPVIGQL TIQTGGPTKP 

       130        140        150        160        170        180 
GEKKPGKTEI QKCSVSAWTD LVFLVDGSWS VGRNNFKYIL DFIVALVSAF DIGEEKTRVG 

       190        200        210        220        230        240 
VVQYSSDTRT EFNLNQYYRR EDLLAAVKKI PYKGGNTMTG DAIDYLVKNT FTESAGSRAG 

       250        260        270        280        290        300 
FPKVAIIITD GKSQDEVEIP ARELRNIGVE VFSLGIKAAD AKELKQIAST PSLNHVFNVA 

       310        320        330        340        350        360 
NFDAIVDIQN EIISQVCSGV DEQLGELVSG EEVIEPPSNL VVTELSSKYI RLSWDPSPSA 

       370        380        390        400        410        420 
VTGYKILLTP MAAGSRHHAL SVGPQTTTLN VRDLTADTEY QISVFAMKGL TSSEPTSVME 

       430        440        450        460        470        480 
KTQPMKVQVE CSRGVDIKAD IVFLVDGSYS IGIANFVKVR AFLEVLAKSF EISPNRVQIS 

       490        500        510        520        530        540 
LVQYSRDPHT EFTLKEFNRV EDIIKAINTF PYRGGSTNTG KAMTYVREKI FVPNKGSRSN 

       550        560        570        580        590        600 
VPKVMILITD GKSSDAFRDP AIKLRNSDVE IFAVGVKDAV RSELEAIASP PAETHVFTVE 

       610        620        630        640        650        660 
DFDAFQRISF ELTQSICLRI EQELAAIKKK AYVPPKDLRF TQVTANSFKA EWSPPGDNVF 

       670        680        690        700        710        720 
SYHVTYKDAN GDDEVTVVEP ASSTSVVLNN LRPETLYLVN VTAEYEDGFS VPITGEETTA 

       730        740        750        760        770        780 
EVKGVPRNLK VTDETTDSFK LTWSQAPGRV LRYRIRYRPV SGGESKEVST PANQRRKTLE 

       790        800        810        820        830        840 
NLTPDTKYEI SVIAEYSSGP GSPLTGNAAT EEVRGNPRDL RVSDATTSTL KLSWSRAPGK 

       850        860        870        880        890        900 
VKQYLVTYTP AAGGETQEVT VRGDTTTTML RKLKEGTQYD LSVTALYASG AGEALSGKGS 

       910        920        930        940        950        960 
TLEERGSPQN LVTKDITDTS IGAYWTSAPG MVRGYRVSWK SLYDDIEAGE TTLPGDAIHT 

       970        980        990       1000       1010       1020 
MIENLQPETK YKISVFATYS SGEGEPVTGD ATTELSQDSK ILRVDEETEH TMRVTWKAAP 

      1030       1040       1050       1060       1070       1080 
GKVVNYRVVY RPQGGGRQMV AKVPPTVTST VLKRLQPQTT YDITVLPMYK TGEGKLRQGS 

      1090       1100       1110       1120       1130       1140 
GTTASRFKSP RNLKTSDPTM SSFRVTWEPA PGEVKGYKVT FHPTGDDRRL GELVLGPYDN 

      1150       1160       1170       1180       1190       1200 
TVVLEELRAG TTYRVNVFGM FDGGESLPLV GQEMTTLSDT TVTPFLSSGM DCLTRAEADI 

      1210       1220       1230       1240       1250       1260 
VLLVDGSWSI GRANFRTVRS FISRIVEVFE IGPKRVQIAL AQYSGDPRTE WQLNAHRDKK 

      1270       1280       1290       1300       1310       1320 
SLLQAVANLP YKGGNTLTGM ALNFIRQQSF KTQAGMRPRA RKIGVLITDG KSQDDVEAPS 

      1330       1340       1350       1360       1370       1380 
KKLKDEGVEL FAIGIKNADE VELKMIATDP DDTHAYNVAD FESLSKIVDD LTINLCNSVK 

      1390       1400       1410       1420       1430       1440 
GPGDLEAPTN LVISERTHRS FRVSWTPPSD SVDRYKVEYY PVSGGKRQEF YVSRLDTSTV 

      1450       1460       1470       1480       1490       1500 
LKDLKPETDY VVNVYSVVED EYSEPLKGTE KTLPVPVVSL NIYDVGPTTM HVQWQPVGGA 

      1510       1520       1530       1540       1550       1560 
TGYTVSYQPT RSPEGTKPKE MRVGPTVNDV QLTGLLPNTE YEVTVQAVLY DLTSEPAKAR 

      1570       1580       1590       1600       1610       1620 
EVTLPLPRPQ DVKLRDVTHS TMNVVWEPVL GKVRKYIVRY KTPDEEFKEV EVDRSRASTI 

      1630       1640       1650       1660       1670       1680 
LKDLSSQTQY TVSVSAVYDE GTSPPATAYD TTRRVPAPTN LQFTEVTPES FRGTWDHGAS 

      1690       1700       1710       1720       1730       1740 
DVSLYRITWA PVGNPDKMET ILNGDENTLV FENLNPNTPY EVSITAIYPD ESESEDLSGT 

      1750       1760       1770       1780       1790       1800 
ERTLRLIPLT TQAPKSGPRN LQVYNATSNS LTVKWDPASG RVQKYRITYQ PSTGEGNEQT 

      1810       1820       1830       1840       1850       1860 
ITVGGRQNSV LLQKLKPDTP YTITVYSQYP DGEGGRMTGR GKTKPLNTVR NLRVYDPSTS 

      1870       1880       1890       1900       1910       1920 
SLSVRWDHAE GNPRQYKLFY APTSGGPEEL VPIPGNTNYA ILRNLQPDTP YTITVVPVYT 

      1930       1940       1950       1960       1970       1980 
EGDGGRTSDT GRTLVRGLAR NIQVYNPTPN SLDVRWDPAP GPVQQYRIVY SPVAGTRPSE 

      1990       2000       2010       2020       2030       2040 
SIVVPGNTRT VHLERLIPDT PYSVNIVALY SDGEGNPSPS QGRTLPRSGP RNIRVFGETT 

      2050       2060       2070       2080       2090       2100 
NSLSVAWDHA DGPVQQYRII YSPTVGDPID EYTTVPGRRN NVILQPLQPD TPYKITVIAI 

      2110       2120       2130       2140       2150       2160 
YEDGDGGHLT GNGRTVGLLP PQNIHIFDEW YTRFRVSWDP SPSPVLGYKI VYKPVGSNEP 

      2170       2180       2190       2200       2210       2220 
MEAFVGEVTS YTLHNLNPST TYDVSVYAQY DSGLSVPLTD QGTTLYLNVT DLKTYQVGWD 

      2230       2240       2250       2260       2270       2280 
TFCVKWSPHR AATSYRLKLS PADGTRGQEI TVRGSETSHC FTGLSPEAEY GVTVFVQTPN 

      2290       2300       2310       2320       2330       2340 
LEGPGVPIKE QTTVKPTEAP TEPPTPSPPP TIPPARDVCK GAKADIVFLT DASWSIGDDN 

      2350       2360       2370       2380       2390       2400 
FNKVVKFIFN TVGAFDEVNP AGIQVSFVQY SDEVKSEFKL NTYNDKALAL GALQNIRYRG 

      2410       2420       2430       2440       2450       2460 
GNTRTGKALT FIKEKVLTWE SGMRKNVPKV LVVVTDGRSQ DEVKKAAFVI QQSGFSVFVV 

      2470       2480       2490       2500       2510       2520 
GVADVDYNEL ANIASKPSER HVFIVDDFES FEKIEDNLIT FVCETATSSC PLIYLDGYTS 

      2530       2540       2550       2560       2570       2580 
PGFKMLEAYN LTEKNFASVQ GVSLESGSFP SYSAYRLQKN AFINQPTAEL HPNGLPPSYT 

      2590       2600       2610       2620       2630       2640 
IILLFRLLPE TPSDPFAIWQ ITDRDYRPQV GVIADPSSKT LSFFNKDTRG EVQTVTFDTD 

      2650       2660       2670       2680       2690       2700 
EVKTLFYGSF HKVHIVVTSK SVKIYIDCYE IIEKDIKEAG NITTDGYEIL GKLLKGERKS 

      2710       2720       2730       2740       2750       2760 
ATFQIQSFDI VCSPVWTSRD RCCDIPSRRD EAKCPALPNA CTCTQDSVGP PGPPGPAGGP 

      2770       2780       2790       2800       2810       2820 
GAKGPRGERG INGAVGPPGP RGDTGPPGPQ GPPGPQGPNG LSIPGEQGRQ GMKGDAGEPG 

      2830       2840       2850       2860       2870       2880 
LPGRTGTPGL PGPPGPMGPP GDRGFTGKDG AMGPRGPPGP PGSPGSPGVT GPSGKPGKPG 

      2890       2900       2910       2920       2930       2940 
DHGRPGQSGL KGEKGDRGDI ASQNMMRAVA RQVCEQLISG QMSRFNQMLN QIPNDYHSSR 

      2950       2960       2970       2980       2990       3000 
NQPGPPGPPG PPGSAGARGE PGPGGRPGFP GTPGMQGPPG ERGLPGEKGE RGTGSQGPRG 

      3010       3020       3030       3040       3050       3060 
PPGPPGPQGE SRTGPPGSTG SRGPPGPPGR PGNSGIRGPP GPPGYCDSSQ CASIPYNGQG 

      3070       3080       3090       3100       3110       3120 
YPEPYVPEGG AYLPEREPFI VPVEPERTAE YEDDYGADEP DQQHPDHMRW RRALRPGPAE 

« Hide

Isoform 2 (ER#K) (XIIA-2) [UniParc].

Checksum: 0FE5F351A4051FD7
Show »

FASTA3,065333,671
Isoform 3 (XIIB-1) [UniParc].

Checksum: 9F869932749E4D20
Show »

FASTA1,958212,624
Isoform 4 (XIIB-2) [UniParc].

Checksum: B5A0AF0676EFC951
Show »

FASTA1,903206,081
Isoform 5 [UniParc].

Checksum: 72C55C50A6D351A4
Show »

FASTA3,068334,069

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U25652 mRNA. Translation: AAA99719.1.
AC157477 Genomic DNA. No translation available.
AC166055 Genomic DNA. No translation available.
U57095 mRNA. Translation: AAB07047.1.
PIRC44479.
D44479.
RefSeqNP_001277237.1. NM_001290308.1. [Q60847-2]
XP_006510861.1. XM_006510798.1. [Q60847-5]
UniGeneMm.3819.

3D structure databases

ProteinModelPortalQ60847.
SMRQ60847. Positions 25-1179, 1196-1367, 1378-2312, 2319-2726.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ60847. 1 interaction.
MINTMINT-4091424.

PTM databases

PhosphoSiteQ60847.

Proteomic databases

MaxQBQ60847.
PaxDbQ60847.
PRIDEQ60847.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000071750; ENSMUSP00000071662; ENSMUSG00000032332. [Q60847-2]
GeneID12816.
KEGGmmu:12816.

Organism-specific databases

CTD1303.
MGIMGI:88448. Col12a1.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00740000115118.
HOGENOMHOG000111877.
HOVERGENHBG051060.
InParanoidQ60847.
KOK08132.
OrthoDBEOG71P290.
PhylomeDBQ60847.
TreeFamTF329914.

Gene expression databases

ArrayExpressQ60847.
BgeeQ60847.
CleanExMM_COL12A1.
GenevestigatorQ60847.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
2.60.40.10. 18 hits.
3.40.50.410. 4 hits.
InterProIPR008160. 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]
PfamPF01391. Collagen. 4 hits.
PF00041. fn3. 18 hits.
PF00092. VWA. 4 hits.
[Graphical view]
SMARTSM00060. FN3. 18 hits.
SM00210. TSPN. 1 hit.
SM00327. VWA. 4 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 11 hits.
SSF49899. SSF49899. 1 hit.
SSF53300. SSF53300. 4 hits.
PROSITEPS50853. FN3. 18 hits.
PS50234. VWFA. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

PROQ60847.
SOURCESearch...

Entry information

Entry nameCOCA1_MOUSE
AccessionPrimary (citable) accession number: Q60847
Secondary accession number(s): P70322
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: March 6, 2007
Last modified: July 9, 2014
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot