Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P01027 (CO3_MOUSE)

Protein

Complement C3

Gene

C3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.
Derived from proteolytic degradation of complement C3, C3a anaphylatoxin is a mediator of local inflammatory process. In chronic inflammation, acts as a chemoattractant for neutrophils (By similarity). It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. The short isoform has B-cell stimulatory activity.By similarity
C3-beta-c: Acts as a chemoattractant for neutrophils in chronic inflammation.By similarity
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.

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Biological processComplement alternate pathway, Complement pathway, Fatty acid metabolism, Immunity, Inflammatory response, Innate immunity, Lipid metabolism

Enzyme and pathway databases

ReactomeiR-MMU-173736 Alternative complement activation
R-MMU-174577 Activation of C3 and C5
R-MMU-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-MMU-375276 Peptide ligand-binding receptors
R-MMU-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-MMU-418594 G alpha (i) signalling events
R-MMU-6798695 Neutrophil degranulation
R-MMU-8957275 Post-translational protein phosphorylation
R-MMU-977606 Regulation of Complement cascade

Protein family/group databases

MEROPSiI39.950

Names & Taxonomyi

Protein namesi
Gene namesi
Name:C3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:88227 C3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 242 PublicationsAdd BLAST24
ChainiPRO_000000591725 – 1663Complement C3Add BLAST1639
ChainiPRO_000000591825 – 666Complement C3 beta chainAdd BLAST642
ChainiPRO_0000430431569 – 666C3-beta-cBy similarityAdd BLAST98
ChainiPRO_0000005919671 – 1663Complement C3 alpha chainAdd BLAST993
ChainiPRO_0000005920671 – 748C3a anaphylatoxinAdd BLAST78
ChainiPRO_0000419936671 – 747Acylation stimulating proteinAdd BLAST77
ChainiPRO_0000005921749 – 1663Complement C3b alpha' chainAdd BLAST915
ChainiPRO_0000005922749 – 954Complement C3c alpha' chain fragment 1Add BLAST206
ChainiPRO_0000005923955 – 1303Complement C3dg fragmentAdd BLAST349
ChainiPRO_0000005924955 – 1001Complement C3g fragmentAdd BLAST47
ChainiPRO_00000059251002 – 1303Complement C3d fragmentAdd BLAST302
PeptideiPRO_00000059271304 – 1320Complement C3f fragmentAdd BLAST17
ChainiPRO_00002739491321 – 1663Complement C3c alpha' chain fragment 2Add BLAST343

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40PhosphoserineBy similarity1
Disulfide bondi559 ↔ 816Interchain (between beta and alpha chains)PROSITE-ProRule annotation
Disulfide bondi626 ↔ 661By similarity
Modified residuei671PhosphoserineBy similarity1
Disulfide bondi693 ↔ 720By similarity
Disulfide bondi694 ↔ 727By similarity
Disulfide bondi707 ↔ 728By similarity
Disulfide bondi873 ↔ 1513By similarity
Glycosylationi939N-linked (GlcNAc...) asparagine1
Modified residuei968PhosphoserineBy similarity1
Cross-linki1010 ↔ 1013Isoglutamyl cysteine thioester (Cys-Gln)By similarity
Disulfide bondi1101 ↔ 1158By similarity
Modified residuei1321PhosphoserineBy similarity1
Disulfide bondi1358 ↔ 1489By similarity
Disulfide bondi1389 ↔ 1458By similarity
Disulfide bondi1506 ↔ 1511By similarity
Disulfide bondi1518 ↔ 1590By similarity
Disulfide bondi1537 ↔ 1661By similarity
Modified residuei1573PhosphoserineBy similarity1
Glycosylationi1617N-linked (GlcNAc...) asparagine1
Disulfide bondi1637 ↔ 1646By similarity

Post-translational modificationi

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.
Phosphorylated by FAM20C in the extracellular medium.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei747 – 748Cleavage; by carboxypeptidasesBy similarity2
Sitei748 – 749Cleavage; by C3 convertase2
Sitei954 – 955Cleavage; by factor ISequence analysis2
Sitei1303 – 1304Cleavage; by factor I2
Sitei1320 – 1321Cleavage; by factor I2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Thioester bond

Proteomic databases

MaxQBiP01027
PaxDbiP01027
PeptideAtlasiP01027
PRIDEiP01027

PTM databases

iPTMnetiP01027
PhosphoSitePlusiP01027
SwissPalmiP01027

Miscellaneous databases

PMAP-CutDBiP01027

Expressioni

Gene expression databases

BgeeiENSMUSG00000024164 Expressed in 182 organ(s), highest expression level in uterine cervix
CleanExiMM_C3
ExpressionAtlasiP01027 baseline and differential
GenevisibleiP01027 MM

Interactioni

Subunit structurei

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).By similarity

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi198418, 2 interactors
ComplexPortaliCPX-988 Complement C3b complex
IntActiP01027, 7 interactors
MINTiP01027
STRINGi10090.ENSMUSP00000024988

Structurei

3D structure databases

ProteinModelPortaliP01027
SMRiP01027
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini693 – 728Anaphylatoxin-likePROSITE-ProRule annotationAdd BLAST36
Domaini1518 – 1661NTRPROSITE-ProRule annotationAdd BLAST144

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1424 – 1456Properdin-bindingBy similarityAdd BLAST33

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1366 Eukaryota
ENOG410XRED LUCA
GeneTreeiENSGT00760000118982
HOGENOMiHOG000286028
HOVERGENiHBG005110
InParanoidiP01027
KOiK03990
OMAiQDGEQRI
OrthoDBiEOG091G00FJ
TreeFamiTF313285

Family and domain databases

CDDicd00017 ANATO, 1 hit
cd03583 NTR_complement_C3, 1 hit
Gene3Di2.60.40.10, 2 hits
2.60.40.690, 1 hit
InterProiView protein in InterPro
IPR009048 A-macroglobulin_rcpt-bd
IPR036595 A-macroglobulin_rcpt-bd_sf
IPR011626 A2M_comp
IPR002890 A2M_N
IPR011625 A2M_N_2
IPR000020 Anaphylatoxin/fibulin
IPR018081 Anaphylatoxin_comp_syst
IPR001840 Anaphylatoxn_comp_syst_dom
IPR035711 Complement_C3-like
IPR013783 Ig-like_fold
IPR001599 Macroglobln_a2
IPR019742 MacrogloblnA2_CS
IPR019565 MacrogloblnA2_thiol-ester-bond
IPR001134 Netrin_domain
IPR018933 Netrin_module_non-TIMP
IPR035815 NTR_complement_C3
IPR008930 Terpenoid_cyclase/PrenylTrfase
IPR008993 TIMP-like_OB-fold
PANTHERiPTHR11412:SF81 PTHR11412:SF81, 1 hit
PfamiView protein in Pfam
PF00207 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
PRINTSiPR00004 ANAPHYLATOXN
SMARTiView protein in SMART
SM01360 A2M, 1 hit
SM01359 A2M_N_2, 1 hit
SM01361 A2M_recep, 1 hit
SM00104 ANATO, 1 hit
SM00643 C345C, 1 hit
SUPFAMiSSF47686 SSF47686, 1 hit
SSF48239 SSF48239, 1 hit
SSF49410 SSF49410, 1 hit
SSF50242 SSF50242, 1 hit
PROSITEiView protein in PROSITE
PS00477 ALPHA_2_MACROGLOBULIN, 1 hit
PS01177 ANAPHYLATOXIN_1, 1 hit
PS01178 ANAPHYLATOXIN_2, 1 hit
PS50189 NTR, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform Long (identifier: P01027-1) [UniParc]FASTAAdd to basket

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

« Hide
        10         20         30         40         50
MGPASGSQLL VLLLLLASSP LALGIPMYSI ITPNVLRLES EETIVLEAHD 
        60         70         80         90        100
AQGDIPVTVT VQDFLKRQVL TSEKTVLTGA SGHLRSVSIK IPASKEFNSD 
       110        120        130        140        150
KEGHKYVTVV ANFGETVVEK AVMVSFQSGY LFIQTDKTIY TPGSTVLYRI 
       160        170        180        190        200
FTVDNNLLPV GKTVVILIET PDGIPVKRDI LSSNNQHGIL PLSWNIPELV 
       210        220        230        240        250
NMGQWKIRAF YEHAPKQIFS AEFEVKEYVL PSFEVRVEPT ETFYYIDDPN 
       260        270        280        290        300
GLEVSIIAKF LYGKNVDGTA FVIFGVQDGD KKISLAHSLT RVVIEDGVGD 
       310        320        330        340        350
AVLTRKVLME GVRPSNADAL VGKSLYVSVT VILHSGSDMV EAERSGIPIV 
       360        370        380        390        400
TSPYQIHFTK TPKFFKPAMP FDLMVFVTNP DGSPASKVLV VTQGSNAKAL 
       410        420        430        440        450
TQDDGVAKLS INTPNSRQPL TITVRTKKDT LPESRQATKT MEAHPYSTMH 
       460        470        480        490        500
NSNNYLHLSV SRMELKPGDN LNVNFHLRTD PGHEAKIRYY TYLVMNKGKL 
       510        520        530        540        550
LKAGRQVREP GQDLVVLSLP ITPEFIPSFR LVAYYTLIGA SGQREVVADS 
       560        570        580        590        600
VWVDVKDSCI GTLVVKGDPR DNHLAPGQQT TLRIEGNQGA RVGLVAVDKG 
       610        620        630        640        650
VFVLNKKNKL TQSKIWDVVE KADIGCTPGS GKNYAGVFMD AGLAFKTSQG 
       660        670        680        690        700
LQTEQRADLE CTKPAARRRR SVQLMERRMD KAGQYTDKGL RKCCEDGMRD 
       710        720        730        740        750
IPMRYSCQRR ARLITQGENC IKAFIDCCNH ITKLREQHRR DHVLGLARSE 
       760        770        780        790        800
LEEDIIPEED IISRSHFPQS WLWTIEELKE PEKNGISTKV MNIFLKDSIT 
       810        820        830        840        850
TWEILAVSLS DKKGICVADP YEIRVMQDFF IDLRLPYSVV RNEQVEIRAV 
       860        870        880        890        900
LFNYREQEEL KVRVELLHNP AFCSMATAKN RYFQTIKIPP KSSVAVPYVI 
       910        920        930        940        950
VPLKIGQQEV EVKAAVFNHF ISDGVKKTLK VVPEGMRINK TVAIHTLDPE 
       960        970        980        990       1000
KLGQGGVQKV DVPAADLSDQ VPDTDSETRI ILQGSPVVQM AEDAVDGERL 
      1010       1020       1030       1040       1050
KHLIVTPAGC GEQNMIGMTP TVIAVHYLDQ TEQWEKFGIE KRQEALELIK 
      1060       1070       1080       1090       1100
KGYTQQLAFK QPSSAYAAFN NRPPSTWLTA YVVKVFSLAA NLIAIDSHVL 
      1110       1120       1130       1140       1150
CGAVKWLILE KQKPDGVFQE DGPVIHQEMI GGFRNAKEAD VSLTAFVLIA 
      1160       1170       1180       1190       1200
LQEARDICEG QVNSLPGSIN KAGEYIEASY MNLQRPYTVA IAGYALALMN 
      1210       1220       1230       1240       1250
KLEEPYLGKF LNTAKDRNRW EEPDQQLYNV EATSYALLAL LLLKDFDSVP 
      1260       1270       1280       1290       1300
PVVRWLNEQR YYGGGYGSTQ ATFMVFQALA QYQTDVPDHK DLNMDVSFHL 
      1310       1320       1330       1340       1350
PSRSSATTFR LLWENGNLLR SEETKQNEAF SLTAKGKGRG TLSVVAVYHA 
      1360       1370       1380       1390       1400
KLKSKVTCKK FDLRVSIRPA PETAKKPEEA KNTMFLEICT KYLGDVDATM 
      1410       1420       1430       1440       1450
SILDISMMTG FAPDTKDLEL LASGVDRYIS KYEMNKAFSN KNTLIIYLEK 
      1460       1470       1480       1490       1500
ISHTEEDCLT FKVHQYFNVG LIQPGSVKVY SYYNLEESCT RFYHPEKDDG 
      1510       1520       1530       1540       1550
MLSKLCHSEM CRCAEENCFM QQSQEKINLN VRLDKACEPG VDYVYKTELT 
      1560       1570       1580       1590       1600
NIELLDDFDE YTMTIQQVIK SGSDEVQAGQ QRKFISHIKC RNALKLQKGK 
      1610       1620       1630       1640       1650
KYLMWGLSSD LWGEKPNTSY IIGKDTWVEH WPEAEECQDQ KYQKQCEELG 
      1660 
AFTESMVVYG CPN
Length:1,663
Mass (Da):186,484
Last modified:July 27, 2011 - v3
Checksum:i7E5546CC7C314779
GO
Isoform Short (identifier: P01027-2) [UniParc]FASTAAdd to basket

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

Show »
Length:535
Mass (Da):60,952
Checksum:i6F6187342DC868CD
GO

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H3BKW9H3BKW9_MOUSE
Complement C3
C3
185Annotation score:
H3BL60H3BL60_MOUSE
Complement C3
C3 mCG_140909
102Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti137K → Q in AAA37339 (PubMed:6356427).Curated1
Sequence conflicti858E → Q in AAC42013 (PubMed:6208565).Curated1
Sequence conflicti1553E → K in AAC42013 (PubMed:6208565).Curated1
Sequence conflicti1553E → K in AAA37336 (PubMed:6094532).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0187081 – 1128Missing in isoform Short. CuratedAdd BLAST1128

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
CCDSiCCDS37670.1 [P01027-1]
PIRiA92459 C3MS
I48284
RefSeqiNP_033908.2, NM_009778.3 [P01027-1]
UniGeneiMm.19131

Genome annotation databases

EnsembliENSMUST00000024988; ENSMUSP00000024988; ENSMUSG00000024164 [P01027-1]
GeneIDi12266
KEGGimmu:12266
UCSCiuc008deg.2 mouse [P01027-1]

Keywords - Coding sequence diversityi

Alternative initiation

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
CCDSiCCDS37670.1 [P01027-1]
PIRiA92459 C3MS
I48284
RefSeqiNP_033908.2, NM_009778.3 [P01027-1]
UniGeneiMm.19131

3D structure databases

ProteinModelPortaliP01027
SMRiP01027
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198418, 2 interactors
ComplexPortaliCPX-988 Complement C3b complex
IntActiP01027, 7 interactors
MINTiP01027
STRINGi10090.ENSMUSP00000024988

Protein family/group databases

MEROPSiI39.950

PTM databases

iPTMnetiP01027
PhosphoSitePlusiP01027
SwissPalmiP01027

Proteomic databases

MaxQBiP01027
PaxDbiP01027
PeptideAtlasiP01027
PRIDEiP01027

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024988; ENSMUSP00000024988; ENSMUSG00000024164 [P01027-1]
GeneIDi12266
KEGGimmu:12266
UCSCiuc008deg.2 mouse [P01027-1]

Organism-specific databases

CTDi718
MGIiMGI:88227 C3

Phylogenomic databases

eggNOGiKOG1366 Eukaryota
ENOG410XRED LUCA
GeneTreeiENSGT00760000118982
HOGENOMiHOG000286028
HOVERGENiHBG005110
InParanoidiP01027
KOiK03990
OMAiQDGEQRI
OrthoDBiEOG091G00FJ
TreeFamiTF313285

Enzyme and pathway databases

ReactomeiR-MMU-173736 Alternative complement activation
R-MMU-174577 Activation of C3 and C5
R-MMU-198933 Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell
R-MMU-375276 Peptide ligand-binding receptors
R-MMU-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-MMU-418594 G alpha (i) signalling events
R-MMU-6798695 Neutrophil degranulation
R-MMU-8957275 Post-translational protein phosphorylation
R-MMU-977606 Regulation of Complement cascade

Miscellaneous databases

ChiTaRSiC3 mouse
PMAP-CutDBiP01027
PROiPR:P01027
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024164 Expressed in 182 organ(s), highest expression level in uterine cervix
CleanExiMM_C3
ExpressionAtlasiP01027 baseline and differential
GenevisibleiP01027 MM

Family and domain databases

CDDicd00017 ANATO, 1 hit
cd03583 NTR_complement_C3, 1 hit
Gene3Di2.60.40.10, 2 hits
2.60.40.690, 1 hit
InterProiView protein in InterPro
IPR009048 A-macroglobulin_rcpt-bd
IPR036595 A-macroglobulin_rcpt-bd_sf
IPR011626 A2M_comp
IPR002890 A2M_N
IPR011625 A2M_N_2
IPR000020 Anaphylatoxin/fibulin
IPR018081 Anaphylatoxin_comp_syst
IPR001840 Anaphylatoxn_comp_syst_dom
IPR035711 Complement_C3-like
IPR013783 Ig-like_fold
IPR001599 Macroglobln_a2
IPR019742 MacrogloblnA2_CS
IPR019565 MacrogloblnA2_thiol-ester-bond
IPR001134 Netrin_domain
IPR018933 Netrin_module_non-TIMP
IPR035815 NTR_complement_C3
IPR008930 Terpenoid_cyclase/PrenylTrfase
IPR008993 TIMP-like_OB-fold
PANTHERiPTHR11412:SF81 PTHR11412:SF81, 1 hit
PfamiView protein in Pfam
PF00207 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
PRINTSiPR00004 ANAPHYLATOXN
SMARTiView protein in SMART
SM01360 A2M, 1 hit
SM01359 A2M_N_2, 1 hit
SM01361 A2M_recep, 1 hit
SM00104 ANATO, 1 hit
SM00643 C345C, 1 hit
SUPFAMiSSF47686 SSF47686, 1 hit
SSF48239 SSF48239, 1 hit
SSF49410 SSF49410, 1 hit
SSF50242 SSF50242, 1 hit
PROSITEiView protein in PROSITE
PS00477 ALPHA_2_MACROGLOBULIN, 1 hit
PS01177 ANAPHYLATOXIN_1, 1 hit
PS01178 ANAPHYLATOXIN_2, 1 hit
PS50189 NTR, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCO3_MOUSE
AccessioniPrimary (citable) accession number: P01027
Secondary accession number(s): Q61370, Q80XP1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 27, 2011
Last modified: November 7, 2018
This is version 189 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again