LOCUS       NP_033908               1663 aa            linear   ROD 12-JUN-2025
DEFINITION  complement C3 preproprotein [Mus musculus].
ACCESSION   NP_033908
VERSION     NP_033908.2
DBSOURCE    REFSEQ: accession NM_009778.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1663)
  AUTHORS   Liu,D.H., Li,F., Yang,R.Z., Wu,Z., Meng,X.Y., Li,S.M., Li,W.X.,
            Li,J.K., Wang,D.D., Wang,R.Y., Li,S.A., Liu,P.P. and Kang,J.S.
  TITLE     Pulmonary mitochondrial DNA release and activation of the
            cGAS-STING pathway in Lethal Stx12 knockout mice
  JOURNAL   Cell Commun Signal 23 (1), 174 (2025)
   PUBMED   40200300
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1663)
  AUTHORS   Smith-Jackson,K., Walsh,P., Zelek,W.M., Hoyler,T., Martinic,M.M.,
            Thompson,G., Gibson,B.G., Connelly,C., Pappworth,I.Y., Murphy,M.J.,
            Kavanagh,D. and Marchbank,K.J.
  TITLE     The membrane attack complex drives thrombotic microangiopathy in
            complement mediated atypical hemolytic uremic syndrome
  JOURNAL   Kidney Int 107 (4), 700-713 (2025)
   PUBMED   39848404
REFERENCE   3  (residues 1 to 1663)
  AUTHORS   Hsu,A.Y., Huang,Q., Pi,X., Fu,J., Raghunathan,K., Ghimire,L.,
            Balasubramanian,A., Xie,X., Yu,H., Loison,F., Haridas,V., Zha,J.,
            Liu,F., Park,S.Y., Bagale,K., Ren,Q., Fan,Y., Zheng,Y.,
            Cancelas,J.A., Chai,L., Stowell,S.R., Chen,K., Xu,R., Wang,X.,
            Xu,Y., Zhang,L., Cheng,T., Ma,F., Thiagarajah,J.R., Wu,H., Feng,S.
            and Luo,H.R.
  TITLE     Neutrophil-derived vesicles control complement activation to
            facilitate inflammation resolution
  JOURNAL   Cell 188 (6), 1623-1641 (2025)
   PUBMED   39938514
REFERENCE   4  (residues 1 to 1663)
  AUTHORS   Yang,Y., Treger,R.S., Hernandez-Bird,J., Lu,P., Mao,T. and
            Iwasaki,A.
  TITLE     A B cell screen against endogenous retroviruses identifies
            glycan-reactive IgM that recognizes a broad array of enveloped
            viruses
  JOURNAL   Sci Immunol 9 (101), eadd6608 (2024)
   PUBMED   39514636
REFERENCE   5  (residues 1 to 1663)
  AUTHORS   Paglialunga,S., Fisette,A., Yan,Y., Deshaies,Y., Brouillette,J.F.,
            Pekna,M. and Cianflone,K.
  TITLE     Acylation-stimulating protein deficiency and altered adipose tissue
            in alternative complement pathway knockout mice
  JOURNAL   Am J Physiol Endocrinol Metab 294 (3), E521-E529 (2008)
   PUBMED   18160458
  REMARK    GeneRIF: reduction/deficiency in acylation stimulating protein
            (ASP) is associated with an antiadipogenic state and ASP may
            provide a target for controlling fat storage
REFERENCE   6  (residues 1 to 1663)
  AUTHORS   Sahu,A. and Lambris,J.D.
  TITLE     Structure and biology of complement protein C3, a connecting link
            between innate and acquired immunity
  JOURNAL   Immunol Rev 180, 35-48 (2001)
   PUBMED   11414361
  REMARK    Review article
REFERENCE   7  (residues 1 to 1663)
  AUTHORS   Fey,G., Domdey,H., Wiebauer,K., Whitehead,A.S. and Odink,K.
  TITLE     Structure and expression of the C3 gene
  JOURNAL   Springer Semin Immunopathol 6 (2-3), 119-147 (1983)
   PUBMED   6356427
  REMARK    Review article
REFERENCE   8  (residues 1 to 1663)
  AUTHORS   Rubinstein,P., Vienne,K. and Hoecker,G.F.
  TITLE     The location of the C3 and GLO (glyoxalase 1) loci of the IXth
            linkage group in mice
  JOURNAL   J Immunol 122 (6), 2584-2589 (1979)
   PUBMED   448134
REFERENCE   9  (residues 1 to 1663)
  AUTHORS   Natsuume-Sakai,S., Amano,S., Hayakawa,J.I. and Takahashi,M.
  TITLE     Preparation of an alloantiserum to murine C3 and demonstration of
            multiple alleles
  JOURNAL   J Immunol 121 (5), 2025-2029 (1978)
   PUBMED   101594
REFERENCE   10 (residues 1 to 1663)
  AUTHORS   Da Silva,F.P., Hoecker,G.F., Day,N.K., Vienne,K. and Rubinstein,P.
  TITLE     Murine complement component 3: genetic variation and linkage to H-2
  JOURNAL   Proc Natl Acad Sci U S A 75 (2), 963-965 (1978)
   PUBMED   273258
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CT025692.15.
            
            On Mar 2, 2007 this sequence version replaced NP_033908.1.
            
            Summary: This gene encodes complement protein C3 which plays a
            central role in the classical, alternative and lectin activation
            pathways of the complement system. The encoded preproprotein
            undergoes a multi-step processing to generate various functional
            peptides. Mice deficient in the encoded protein fail to clear
            bacteria from the blood stream upon infection, display diminished
            airway hyperresponsiveness and lung eosinophilia upon
            allergen-induced pulmonary allergy, and develop severe lung injury
            after deposition of IgG immune complexes. Deficiency of the homolog
            of the encoded protein in humans was found to be associated with
            increased susceptibility to infections, age-related macular
            degeneration, and atypical hemolytic uremic syndrome. [provided by
            RefSeq, Mar 2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC043338.1, K02782.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849381, SAMN00849382
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1663
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="17"
                     /map="17 29.72 cM"
     Protein         1..1663
                     /product="complement C3 preproprotein"
                     /EC_number="3.4.21.43"
                     /note="complement C3; complement component 3d; complement
                     factor 3; acylation stimulating protein"
                     /calculated_mol_wt=184181
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2322
     mat_peptide     25..1663
                     /product="Complement C3. /id=PRO_0000005917"
                     /note="propagated from UniProtKB/Swiss-Prot (P01027.3)"
                     /calculated_mol_wt=184181
     mat_peptide     25..666
                     /product="Complement C3 beta chain. /id=PRO_0000005918"
                     /note="propagated from UniProtKB/Swiss-Prot (P01027.3)"
                     /calculated_mol_wt=70640
     Region          26..125
                     /region_name="MG1"
                     /note="Macroglobulin domain MG1; pfam17790"
                     /db_xref="CDD:465508"
     Site            40
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P01024; propagated from
                     UniProtKB/Swiss-Prot (P01027.3)"
     Region          130..225
                     /region_name="MG2"
                     /note="MG2 domain; pfam01835"
                     /db_xref="CDD:426464"
     Region          227..308
                     /region_name="MG3"
                     /note="Macroglobulin domain MG3; pfam17791"
                     /db_xref="CDD:465509"
     Region          356..446
                     /region_name="MG4"
                     /note="Macroglobulin domain MG4; pfam17789"
                     /db_xref="CDD:465507"
     Region          456..604
                     /region_name="A2M_BRD"
                     /note="Alpha-2-macroglobulin bait region domain;
                     pfam07703"
                     /db_xref="CDD:462235"
     mat_peptide     569..666
                     /product="C3-beta-c. /evidence=ECO:0000250.
                     /id=PRO_0000430431"
                     /note="propagated from UniProtKB/Swiss-Prot (P01027.3)"
                     /calculated_mol_wt=10470
     mat_peptide     671..1663
                     /product="Complement C3 alpha chain. /id=PRO_0000005919"
                     /note="propagated from UniProtKB/Swiss-Prot (P01027.3)"
                     /calculated_mol_wt=112934
     mat_peptide     671..748
                     /product="C3a anaphylatoxin. /id=PRO_0000005920"
                     /note="propagated from UniProtKB/Swiss-Prot (P01027.3)"
                     /calculated_mol_wt=9225
     mat_peptide     671..747
                     /product="Acylation stimulating protein.
                     /id=PRO_0000419936"
                     /note="propagated from UniProtKB/Swiss-Prot (P01027.3)"
                     /calculated_mol_wt=9069
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P01024; propagated from
                     UniProtKB/Swiss-Prot (P01027.3)"
     Region          678..747
                     /region_name="ANATO"
                     /note="Anaphylatoxin homologous domain; C3a, C4a and C5a
                     anaphylatoxins are protein fragments generated
                     enzymatically in serum during activation of complement
                     molecules C3, C4, and C5. They induce smooth muscle
                     contraction. These fragments are homologous to...;
                     cd00017"
                     /db_xref="CDD:237984"
     Site            747..748
                     /site_type="cleavage"
                     /note="Cleavage, by carboxypeptidases.
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P01027.3)"
     Site            748..749
                     /site_type="cleavage"
                     /note="Cleavage, by C3 convertase; propagated from
                     UniProtKB/Swiss-Prot (P01027.3)"
     mat_peptide     749..1663
                     /product="Complement C3b alpha' chain. /id=PRO_0000005921"
                     /note="propagated from UniProtKB/Swiss-Prot (P01027.3)"
                     /calculated_mol_wt=103727
     mat_peptide     749..954
                     /product="Complement C3c alpha' chain fragment 1.
                     /id=PRO_0000005922"
                     /note="propagated from UniProtKB/Swiss-Prot (P01027.3)"
                     /calculated_mol_wt=23683
     Region          770..866
                     /region_name="A2M"
                     /note="Alpha-2-macroglobulin family; pfam00207"
                     /db_xref="CDD:459711"
     Site            939
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P01027.3)"
     Site            954..955
                     /site_type="cleavage"
                     /note="Cleavage, by factor I. /evidence=ECO:0000255;
                     propagated from UniProtKB/Swiss-Prot (P01027.3)"
     mat_peptide     955..1303
                     /product="Complement C3dg fragment. /id=PRO_0000005923"
                     /note="propagated from UniProtKB/Swiss-Prot (P01027.3)"
                     /calculated_mol_wt=38820
     mat_peptide     955..1001
                     /product="Complement C3g fragment. /id=PRO_0000005924"
                     /note="propagated from UniProtKB/Swiss-Prot (P01027.3)"
                     /calculated_mol_wt=4950
     Site            968
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P01024; propagated from
                     UniProtKB/Swiss-Prot (P01027.3)"
     Region          996..1282
                     /region_name="complement_C3_C4_C5"
                     /note="Proteins similar to C3, C4 and C5 of vertebrate
                     complement. The vertebrate complement system, comprised of
                     a large number of distinct plasma proteins, is an effector
                     of both the acquired and innate immune systems. The point
                     of convergence of the...; cd02896"
                     /db_xref="CDD:239226"
     mat_peptide     1002..1303
                     /product="Complement C3d fragment. /id=PRO_0000005925"
                     /note="propagated from UniProtKB/Swiss-Prot (P01027.3)"
                     /calculated_mol_wt=33888
     Site            order(1010,1012..1013,1016,1059,1069,1072,1123,1125..1126,
                     1266)
                     /site_type="other"
                     /note="surface patch"
                     /db_xref="CDD:239226"
     Site            order(1010..1013,1126)
                     /site_type="active"
                     /db_xref="CDD:239226"
     Site            1010..1013
                     /site_type="active"
                     /note="thioester region [active]"
                     /db_xref="CDD:239226"
     Site            order(1112,1116,1118,1126,1131..1132)
                     /site_type="other"
                     /note="specificity defining residues"
                     /db_xref="CDD:239226"
     Site            1303..1304
                     /site_type="cleavage"
                     /note="Cleavage, by factor I; propagated from
                     UniProtKB/Swiss-Prot (P01027.3)"
     mat_peptide     1304..1320
                     /product="Complement C3f fragment. /id=PRO_0000005927"
                     /note="propagated from UniProtKB/Swiss-Prot (P01027.3)"
                     /calculated_mol_wt=1978
     Site            1320..1321
                     /site_type="cleavage"
                     /note="Cleavage, by factor I; propagated from
                     UniProtKB/Swiss-Prot (P01027.3)"
     mat_peptide     1321..1663
                     /product="Complement C3c alpha' chain fragment 2.
                     /id=PRO_0000273949"
                     /note="propagated from UniProtKB/Swiss-Prot (P01027.3)"
                     /calculated_mol_wt=39300
     Site            1321
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P01024; propagated from
                     UniProtKB/Swiss-Prot (P01027.3)"
     Region          1397..1494
                     /region_name="A2M_recep"
                     /note="A-macroglobulin receptor binding domain; pfam07677"
                     /db_xref="CDD:462226"
     Region          1513..1661
                     /region_name="NTR_complement_C3"
                     /note="NTR/C345C domain, complement C3 subfamily; The NTR
                     domain found in complement C3 is also known as the C345C
                     domain because it occurs at the C-terminus of complement
                     C3, C4 and C5. Complement C3 plays a pivotal role in the
                     activation of the complement...; cd03583"
                     /db_xref="CDD:239638"
     Site            1573
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P01024; propagated from
                     UniProtKB/Swiss-Prot (P01027.3)"
     Site            1617
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine; propagated from
                     UniProtKB/Swiss-Prot (P01027.3)"
     Region          1634..1659
                     /region_name="Interaction with CFP/properdin.
                     /evidence=ECO:0000250|UniProtKB:P01024"
                     /note="propagated from UniProtKB/Swiss-Prot (P01027.3)"
     Site            1663
                     /site_type="other"
                     /note="Coordinates Mg2+ for interaction with Complement
                     factor B Bb fragment.
                     /evidence=ECO:0000250|UniProtKB:P01024; propagated from
                     UniProtKB/Swiss-Prot (P01027.3)"
     CDS             1..1663
                     /gene="C3"
                     /gene_synonym="ASP; HSE-MSF; Plp"
                     /coded_by="NM_009778.3:102..5093"
                     /db_xref="CCDS:CCDS37670.1"
                     /db_xref="GeneID:12266"
                     /db_xref="MGI:MGI:88227"
ORIGIN      
        1 mgpasgsqll vlllllassp lalgipmysi itpnvlrles eetivleahd aqgdipvtvt
       61 vqdflkrqvl tsektvltga sghlrsvsik ipaskefnsd keghkyvtvv anfgetvvek
      121 avmvsfqsgy lfiqtdktiy tpgstvlyri ftvdnnllpv gktvviliet pdgipvkrdi
      181 lssnnqhgil plswnipelv nmgqwkiraf yehapkqifs aefevkeyvl psfevrvept
      241 etfyyiddpn glevsiiakf lygknvdgta fvifgvqdgd kkislahslt rvviedgvgd
      301 avltrkvlme gvrpsnadal vgkslyvsvt vilhsgsdmv eaersgipiv tspyqihftk
      361 tpkffkpamp fdlmvfvtnp dgspaskvlv vtqgsnakal tqddgvakls intpnsrqpl
      421 titvrtkkdt lpesrqatkt meahpystmh nsnnylhlsv srmelkpgdn lnvnfhlrtd
      481 pgheakiryy tylvmnkgkl lkagrqvrep gqdlvvlslp itpefipsfr lvayytliga
      541 sgqrevvads vwvdvkdsci gtlvvkgdpr dnhlapgqqt tlriegnqga rvglvavdkg
      601 vfvlnkknkl tqskiwdvve kadigctpgs gknyagvfmd aglafktsqg lqteqradle
      661 ctkpaarrrr svqlmerrmd kagqytdkgl rkccedgmrd ipmryscqrr arlitqgenc
      721 ikafidccnh itklreqhrr dhvlglarse leediipeed iisrshfpqs wlwtieelke
      781 pekngistkv mniflkdsit tweilavsls dkkgicvadp yeirvmqdff idlrlpysvv
      841 rneqveirav lfnyreqeel kvrvellhnp afcsmatakn ryfqtikipp kssvavpyvi
      901 vplkigqqev evkaavfnhf isdgvkktlk vvpegmrink tvaihtldpe klgqggvqkv
      961 dvpaadlsdq vpdtdsetri ilqgspvvqm aedavdgerl khlivtpagc geqnmigmtp
     1021 tviavhyldq teqwekfgie krqealelik kgytqqlafk qpssayaafn nrppstwlta
     1081 yvvkvfslaa nliaidshvl cgavkwlile kqkpdgvfqe dgpvihqemi ggfrnakead
     1141 vsltafvlia lqeardiceg qvnslpgsin kageyieasy mnlqrpytva iagyalalmn
     1201 kleepylgkf lntakdrnrw eepdqqlynv eatsyallal lllkdfdsvp pvvrwlneqr
     1261 yygggygstq atfmvfqala qyqtdvpdhk dlnmdvsfhl psrssattfr llwengnllr
     1321 seetkqneaf sltakgkgrg tlsvvavyha klkskvtckk fdlrvsirpa petakkpeea
     1381 kntmfleict kylgdvdatm sildismmtg fapdtkdlel lasgvdryis kyemnkafsn
     1441 kntliiylek ishteedclt fkvhqyfnvg liqpgsvkvy syynleesct rfyhpekddg
     1501 mlsklchsem crcaeencfm qqsqekinln vrldkacepg vdyvyktelt niellddfde
     1561 ytmtiqqvik sgsdevqagq qrkfishikc rnalklqkgk kylmwglssd lwgekpntsy
     1621 iigkdtwveh wpeaeecqdq kyqkqceelg aftesmvvyg cpn
//
