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P01027 (CO3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. 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

Protein attributes

Sequence length1663 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates. Ref.13 Ref.14

Derived from proteolytic degradation of complement C3, C3a anaphylatoxin is a mediator of local inflammatory process. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. The short isoform hasB-cell stimulatory activity. Ref.13 Ref.14

Acylation stimulating protein: adipogenic hormone that stimulates triglyceride (TG) synthesis and glucose transport in adipocytes, regulating fat storage and playing a role in postprandial TG clearance. Appears to stimulate TG synthesis via activation of the PLC, MAPK and AKT signaling pathways. Ligand for C5AR2. Promotes the phosphorylation, ARRB2-mediated internalization and recycling of C5AR2. Ref.13 Ref.14

Subunit structure

C3 precursor is first processed by the removal of 4 Arg residues, forming two chains, beta and alpha, linked by a disulfide bond. C3 convertase activates C3 by cleaving the alpha chain, releasing C3a anaphylatoxin and generating C3b (beta chain + alpha' chain). C3dg interacts with CR2 (via the N-terminal Sushi domains 1 and 2). Interacts with VSIG4. Interacts (both C3a and ASP) with C5AR2; the interaction occurs with higher affinity for ASP, enhancing the phosphorylation and activation of C5AR2, recruitment of ARRB2 to the cell surface and endocytosis of GRP77 By similarity.

Subcellular location

Secreted.

Post-translational modification

C3b is rapidly split in two positions by factor I and a cofactor to form iC3b (inactivated C3b) and C3f which is released. Then iC3b is slowly cleaved (possibly by factor I) to form C3c (beta chain + alpha' chain fragment 1 + alpha' chain fragment 2), C3dg and C3f. Other proteases produce other fragments such as C3d or C3g. C3a is further processed by carboxypeptidases to release the C-terminal arginine residue generating the acylation stimulating protein (ASP). Levels of ASP are increased in adipocytes in the postprandial period and by dietary chylomicrons.

Phosphorylation sites are present in the extracellular medium By similarity.

Disruption phenotype

Null mice displayed altered lipid metabolism and morphological changes in adipocyte distribution. There is reduced adipsin/CFD expression, increased number of smaller fat cells, decreased DGAT1 expression and activity, and less triglyceride storage capacity associated with delayed postprandial clearance. Mice on a high-fat diet exihibited no diet-induced up-regulation of adipsin/CFD expression nor adipocyte differentiation. Ref.14

Sequence similarities

Contains 1 anaphylatoxin-like domain.

Contains 1 NTR domain.

Ontologies

Keywords
   Biological processComplement alternate pathway
Complement pathway
Fatty acid metabolism
Immunity
Inflammatory response
Innate immunity
Lipid metabolism
   Cellular componentSecreted
   Coding sequence diversityAlternative initiation
   DomainSignal
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
Thioester bond
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcomplement activation

Inferred from direct assay PubMed 18947875. Source: MGI

complement activation, alternative pathway

Inferred from electronic annotation. Source: UniProtKB-KW

complement activation, classical pathway

Inferred from electronic annotation. Source: UniProtKB-KW

fatty acid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of G-protein coupled receptor protein signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of activation of membrane attack complex

Inferred from mutant phenotype PubMed 15611275. Source: BHF-UCL

positive regulation of angiogenesis

Inferred from mutant phenotype PubMed 15611275PubMed 16452172. Source: BHF-UCL

positive regulation of glucose transport

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of lipid storage

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phagocytosis

Inferred from mutant phenotype PubMed 11901193. Source: MGI

positive regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of type IIa hypersensitivity

Inferred from mutant phenotype PubMed 11901193. Source: MGI

positive regulation vascular endothelial growth factor production

Inferred from electronic annotation. Source: Ensembl

regulation of triglyceride biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: InterPro

extracellular vesicular exosome

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionC5L2 anaphylatoxin chemotactic receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

endopeptidase inhibitor activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 11728339PubMed 16023208. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Long (identifier: P01027-1)

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 Short (identifier: P01027-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1128: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.7 Ref.8
Chain25 – 16631639Complement C3
PRO_0000005917
Chain25 – 666642Complement C3 beta chain
PRO_0000005918
Chain671 – 1663993Complement C3 alpha chain
PRO_0000005919
Chain671 – 74878C3a anaphylatoxin
PRO_0000005920
Chain671 – 74777Acylation stimulating protein
PRO_0000419936
Chain749 – 1663915Complement C3b alpha' chain
PRO_0000005921
Chain749 – 954206Complement C3c alpha' chain fragment 1
PRO_0000005922
Chain955 – 1303349Complement C3dg fragment
PRO_0000005923
Chain955 – 100147Complement C3g fragment
PRO_0000005924
Chain1002 – 1303302Complement C3d fragment
PRO_0000005925
Peptide1304 – 132017Complement C3f fragment
PRO_0000005927
Chain1321 – 1663343Complement C3c alpha' chain fragment 2
PRO_0000273949

Regions

Domain693 – 72836Anaphylatoxin-like
Domain1518 – 1661144NTR
Region1424 – 145633Properdin-binding By similarity

Sites

Site747 – 7482Cleavage; by carboxypeptidases By similarity
Site748 – 7492Cleavage; by C3 convertase
Site954 – 9552Cleavage; by factor I Potential
Site1303 – 13042Cleavage; by factor I
Site1320 – 13212Cleavage; by factor I

Amino acid modifications

Glycosylation9391N-linked (GlcNAc...)
Glycosylation16171N-linked (GlcNAc...)
Disulfide bond559 ↔ 816Interchain (between beta and alpha chains) By similarity
Disulfide bond626 ↔ 661 By similarity
Disulfide bond693 ↔ 720 By similarity
Disulfide bond694 ↔ 727 By similarity
Disulfide bond707 ↔ 728 By similarity
Disulfide bond873 ↔ 1513 By similarity
Disulfide bond1101 ↔ 1158 By similarity
Disulfide bond1358 ↔ 1489 By similarity
Disulfide bond1389 ↔ 1458 By similarity
Disulfide bond1506 ↔ 1511 By similarity
Disulfide bond1518 ↔ 1590 By similarity
Disulfide bond1537 ↔ 1661 By similarity
Disulfide bond1637 ↔ 1646 By similarity
Cross-link1010 ↔ 1013Isoglutamyl cysteine thioester (Cys-Gln) By similarity

Natural variations

Alternative sequence1 – 11281128Missing in isoform Short.
VSP_018708

Experimental info

Sequence conflict1371K → Q in AAA37339. Ref.6
Sequence conflict8581E → Q in AAC42013. Ref.1
Sequence conflict15531E → K in AAC42013. Ref.1
Sequence conflict15531E → K in AAA37336. Ref.10

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 7E5546CC7C314779

FASTA1,663186,484
        10         20         30         40         50         60 
MGPASGSQLL VLLLLLASSP LALGIPMYSI ITPNVLRLES EETIVLEAHD AQGDIPVTVT 

        70         80         90        100        110        120 
VQDFLKRQVL TSEKTVLTGA SGHLRSVSIK IPASKEFNSD KEGHKYVTVV ANFGETVVEK 

       130        140        150        160        170        180 
AVMVSFQSGY LFIQTDKTIY TPGSTVLYRI FTVDNNLLPV GKTVVILIET PDGIPVKRDI 

       190        200        210        220        230        240 
LSSNNQHGIL PLSWNIPELV NMGQWKIRAF YEHAPKQIFS AEFEVKEYVL PSFEVRVEPT 

       250        260        270        280        290        300 
ETFYYIDDPN GLEVSIIAKF LYGKNVDGTA FVIFGVQDGD KKISLAHSLT RVVIEDGVGD 

       310        320        330        340        350        360 
AVLTRKVLME GVRPSNADAL VGKSLYVSVT VILHSGSDMV EAERSGIPIV TSPYQIHFTK 

       370        380        390        400        410        420 
TPKFFKPAMP FDLMVFVTNP DGSPASKVLV VTQGSNAKAL TQDDGVAKLS INTPNSRQPL 

       430        440        450        460        470        480 
TITVRTKKDT LPESRQATKT MEAHPYSTMH NSNNYLHLSV SRMELKPGDN LNVNFHLRTD 

       490        500        510        520        530        540 
PGHEAKIRYY TYLVMNKGKL LKAGRQVREP GQDLVVLSLP ITPEFIPSFR LVAYYTLIGA 

       550        560        570        580        590        600 
SGQREVVADS VWVDVKDSCI GTLVVKGDPR DNHLAPGQQT TLRIEGNQGA RVGLVAVDKG 

       610        620        630        640        650        660 
VFVLNKKNKL TQSKIWDVVE KADIGCTPGS GKNYAGVFMD AGLAFKTSQG LQTEQRADLE 

       670        680        690        700        710        720 
CTKPAARRRR SVQLMERRMD KAGQYTDKGL RKCCEDGMRD IPMRYSCQRR ARLITQGENC 

       730        740        750        760        770        780 
IKAFIDCCNH ITKLREQHRR DHVLGLARSE LEEDIIPEED IISRSHFPQS WLWTIEELKE 

       790        800        810        820        830        840 
PEKNGISTKV MNIFLKDSIT TWEILAVSLS DKKGICVADP YEIRVMQDFF IDLRLPYSVV 

       850        860        870        880        890        900 
RNEQVEIRAV LFNYREQEEL KVRVELLHNP AFCSMATAKN RYFQTIKIPP KSSVAVPYVI 

       910        920        930        940        950        960 
VPLKIGQQEV EVKAAVFNHF ISDGVKKTLK VVPEGMRINK TVAIHTLDPE KLGQGGVQKV 

       970        980        990       1000       1010       1020 
DVPAADLSDQ VPDTDSETRI ILQGSPVVQM AEDAVDGERL KHLIVTPAGC GEQNMIGMTP 

      1030       1040       1050       1060       1070       1080 
TVIAVHYLDQ TEQWEKFGIE KRQEALELIK KGYTQQLAFK QPSSAYAAFN NRPPSTWLTA 

      1090       1100       1110       1120       1130       1140 
YVVKVFSLAA NLIAIDSHVL CGAVKWLILE KQKPDGVFQE DGPVIHQEMI GGFRNAKEAD 

      1150       1160       1170       1180       1190       1200 
VSLTAFVLIA LQEARDICEG QVNSLPGSIN KAGEYIEASY MNLQRPYTVA IAGYALALMN 

      1210       1220       1230       1240       1250       1260 
KLEEPYLGKF LNTAKDRNRW EEPDQQLYNV EATSYALLAL LLLKDFDSVP PVVRWLNEQR 

      1270       1280       1290       1300       1310       1320 
YYGGGYGSTQ ATFMVFQALA QYQTDVPDHK DLNMDVSFHL PSRSSATTFR LLWENGNLLR 

      1330       1340       1350       1360       1370       1380 
SEETKQNEAF SLTAKGKGRG TLSVVAVYHA KLKSKVTCKK FDLRVSIRPA PETAKKPEEA 

      1390       1400       1410       1420       1430       1440 
KNTMFLEICT KYLGDVDATM SILDISMMTG FAPDTKDLEL LASGVDRYIS KYEMNKAFSN 

      1450       1460       1470       1480       1490       1500 
KNTLIIYLEK ISHTEEDCLT FKVHQYFNVG LIQPGSVKVY SYYNLEESCT RFYHPEKDDG 

      1510       1520       1530       1540       1550       1560 
MLSKLCHSEM CRCAEENCFM QQSQEKINLN VRLDKACEPG VDYVYKTELT NIELLDDFDE 

      1570       1580       1590       1600       1610       1620 
YTMTIQQVIK SGSDEVQAGQ QRKFISHIKC RNALKLQKGK KYLMWGLSSD LWGEKPNTSY 

      1630       1640       1650       1660 
IIGKDTWVEH WPEAEECQDQ KYQKQCEELG AFTESMVVYG CPN 

« Hide

Isoform Short [UniParc].

Checksum: 6F6187342DC868CD
Show »

FASTA53560,952

References

« Hide 'large scale' references
[1]"Nucleotide sequence of complementary DNA and derived amino acid sequence of murine complement protein C3."
Fey G.H., Lundwall A., Wetsel R.A., Tack B.F., de Bruijn M.H.L., Domdey H.
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 306:333-344(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
[3]"Structure of murine complement component C3. I. Nucleotide sequence of cloned complementary and genomic DNA coding for the beta chain."
Lundwall A., Wetsel R.A., Domdey H., Tack B.F., Fey G.H.
J. Biol. Chem. 259:13851-13856(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-724 (ISOFORM LONG).
[4]"Isolation and analysis of genomic DNA clones encoding the third component of mouse complement."
Wiebauer K., Domdey H., Diggelmann H., Fey G.
Proc. Natl. Acad. Sci. U.S.A. 79:7077-7081(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
[5]"Common evolutionary origin of alpha 2-macroglobulin and complement components C3 and C4."
Sottrup-Jensen L., Stepanik T.M., Kristensen T., Lonblad P.B., Jones C.M., Wierzbicki D.M., Magnusson S., Domdey H., Wetsel R.A., Lundwall A., Tack B.F., Fey G.H.
Proc. Natl. Acad. Sci. U.S.A. 82:9-13(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-1663 (ISOFORM LONG).
[6]"Structure and expression of the C3 gene."
Fey G., Domdey H., Wiebauer K., Whitehead A.S., Odink K.
Springer Semin. Immunopathol. 6:119-147(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-240 (ISOFORM LONG).
[7]"A paracrine migration-stimulating factor for metastatic tumor cells secreted by mouse hepatic sinusoidal endothelial cells: identification as complement component C3b."
Hamada J., Cavanaugh P.G., Miki K., Nicolson G.L.
Cancer Res. 53:4418-4423(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-41 AND 749-760.
[8]"The specific production of the third component of complement by osteoblastic cells treated with 1 alpha,25-dihydroxyvitamin D3."
Sato T., Hong M.H., Jin C.H., Ishimi Y., Udagawa N., Shinki T., Abe E., Suda T.
FEBS Lett. 285:21-24(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-31 AND 671-680.
[9]"Amino acid sequences of mouse complement C3 derived from nucleotide sequences of cloned cDNA."
Fey G.H., Wiebauer K., Domdey H.
Ann. N. Y. Acad. Sci. 421:307-312(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 658-761.
[10]"Structure of murine complement component C3. II. Nucleotide sequence of cloned complementary DNA coding for the alpha chain."
Wetsel R.A., Lundwall A., Davidson F., Gibson T., Tack B.F., Fey G.H.
J. Biol. Chem. 259:13857-13862(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 671-1663 (ISOFORM LONG).
[11]"Characterization of the mRNA and cloned cDNA specifying the third component of mouse complement."
Domdey H., Wiebauer K., Kazmaier M., Mueller V., Odink K., Fey G.H.
Proc. Natl. Acad. Sci. U.S.A. 79:7619-7623(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 671-748.
[12]"The structure of an alternate form of complement C3 that displays costimulatory growth factor activity for B lymphocytes."
Cahen-Kramer Y., Martensson I.L., Melchers F.
J. Exp. Med. 180:2079-2088(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE INITIATION (ISOFORM SHORT).
[13]"Acylation-stimulating protein (ASP) deficiency induces obesity resistance and increased energy expenditure in ob/ob mice."
Xia Z., Sniderman A.D., Cianflone K.
J. Biol. Chem. 277:45874-45879(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Acylation-stimulating protein deficiency and altered adipose tissue in alternative complement pathway knockout mice."
Paglialunga S., Fisette A., Yan Y., Deshaies Y., Brouillette J.F., Pekna M., Cianflone K.
Am. J. Physiol. 294:E521-E529(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K02782 mRNA. Translation: AAC42013.1.
BC043338 mRNA. Translation: AAH43338.1.
M35659 mRNA. Translation: AAA37339.1.
M33032 mRNA. Translation: AAA37378.1.
J00369, J00367 Genomic DNA. Translation: AAA37336.1.
Z37998 Genomic DNA. Translation: CAA86099.2.
CCDSCCDS37670.1. [P01027-1]
PIRC3MS. A92459.
I48284.
RefSeqNP_033908.2. NM_009778.2. [P01027-1]
UniGeneMm.19131.

3D structure databases

ProteinModelPortalP01027.
SMRP01027. Positions 26-663, 672-1663.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198418. 1 interaction.
IntActP01027. 5 interactions.
MINTMINT-1858136.

Protein family/group databases

MEROPSI39.950.

PTM databases

PhosphoSiteP01027.

Proteomic databases

MaxQBP01027.
PaxDbP01027.
PRIDEP01027.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000024988; ENSMUSP00000024988; ENSMUSG00000024164. [P01027-1]
GeneID12266.
KEGGmmu:12266.
UCSCuc008deg.1. mouse. [P01027-1]

Organism-specific databases

CTD718.
MGIMGI:88227. C3.

Phylogenomic databases

eggNOGNOG241555.
GeneTreeENSGT00560000077078.
HOGENOMHOG000286028.
HOVERGENHBG005110.
InParanoidQ80XP1.
KOK03990.
OMAPGMPFDL.
OrthoDBEOG77HDCX.
TreeFamTF313285.

Gene expression databases

ArrayExpressP01027.
BgeeP01027.
CleanExMM_C3.
GenevestigatorP01027.

Family and domain databases

Gene3D1.20.91.20. 1 hit.
1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
InterProIPR009048. A-macroglobulin_rcpt-bd.
IPR011626. A2M_comp.
IPR002890. A2M_N.
IPR011625. A2M_N_2.
IPR000020. Anaphylatoxin/fibulin.
IPR018081. Anaphylatoxin_comp_syst.
IPR001840. Anaphylatoxn_comp_syst_dom.
IPR001599. Macroglobln_a2.
IPR019742. MacrogloblnA2_CS.
IPR019565. MacrogloblnA2_thiol-ester-bond.
IPR001134. Netrin_domain.
IPR018933. Netrin_module_non-TIMP.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR008993. TIMP-like_OB-fold.
[Graphical view]
PfamPF00207. A2M. 1 hit.
PF07678. A2M_comp. 1 hit.
PF01835. A2M_N. 1 hit.
PF07703. A2M_N_2. 1 hit.
PF07677. A2M_recep. 1 hit.
PF01821. ANATO. 1 hit.
PF01759. NTR. 1 hit.
PF10569. Thiol-ester_cl. 1 hit.
[Graphical view]
PRINTSPR00004. ANAPHYLATOXN.
SMARTSM00104. ANATO. 1 hit.
SM00643. C345C. 1 hit.
[Graphical view]
SUPFAMSSF47686. SSF47686. 1 hit.
SSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF50242. SSF50242. 1 hit.
PROSITEPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
PS01177. ANAPHYLATOXIN_1. 1 hit.
PS01178. ANAPHYLATOXIN_2. 1 hit.
PS50189. NTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSC3. mouse.
NextBio280714.
PMAP-CutDBQ80XP1.
PROP01027.
SOURCESearch...

Entry information

Entry nameCO3_MOUSE
AccessionPrimary (citable) accession number: P01027
Secondary accession number(s): Q61370, Q80XP1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 148 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