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C4BPA_MOUSE
ID   C4BPA_MOUSE             Reviewed;         469 AA.
AC   P08607; Q91X48;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   03-AUG-2022, entry version 164.
DE   RecName: Full=C4b-binding protein;
DE            Short=C4bp;
DE   Flags: Precursor;
GN   Name=C4bpa; Synonyms=C4bp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3663616; DOI=10.1021/bi00389a012;
RA   Kristensen T., Ogata R.T., Chung L.P., Reid K.B.M., Tack B.F.;
RT   "cDNA structure of murine C4b-binding protein, a regulatory component of
RT   the serum complement system.";
RL   Biochemistry 26:4668-4674(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-275.
RC   STRAIN=C57BL/6J; TISSUE=Plasma;
RX   PubMed=17330941; DOI=10.1021/pr0604559;
RA   Bernhard O.K., Kapp E.A., Simpson R.J.;
RT   "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT   tryptic glycopeptides.";
RL   J. Proteome Res. 6:987-995(2007).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, and Heart;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Controls the classical pathway of complement activation. It
CC       binds as a cofactor to C3b/C4b inactivator (C3bINA), which then
CC       hydrolyzes the complement fragment C4b. It also accelerates the
CC       degradation of the C4bC2a complex (C3 convertase) by dissociating the
CC       complement fragment C2a. Alpha chain binds C4b. It interacts also with
CC       serum amyloid P component.
CC   -!- SUBUNIT: Homoheptamer; not covalently linked. Mouse lacks the beta
CC       chain of C4BP.
CC   -!- INTERACTION:
CC       P08607; Q13873: BMPR2; Xeno; NbExp=3; IntAct=EBI-527325, EBI-527196;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-44 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA37312.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; M17122; AAA37312.1; ALT_INIT; mRNA.
DR   EMBL; AK149468; BAE28899.1; -; mRNA.
DR   EMBL; AK149477; BAE28904.1; -; mRNA.
DR   EMBL; CH466520; EDL39738.1; -; Genomic_DNA.
DR   EMBL; BC012257; AAH12257.1; -; mRNA.
DR   CCDS; CCDS35700.1; -.
DR   PIR; A27117; NBMSC4.
DR   RefSeq; NP_031602.3; NM_007576.3.
DR   RefSeq; XP_011246208.1; XM_011247906.2.
DR   AlphaFoldDB; P08607; -.
DR   SMR; P08607; -.
DR   IntAct; P08607; 1.
DR   STRING; 10090.ENSMUSP00000027657; -.
DR   GlyConnect; 814; 1 N-Linked glycan (1 site).
DR   GlyGen; P08607; 7 sites, 2 N-linked glycans (1 site).
DR   iPTMnet; P08607; -.
DR   PhosphoSitePlus; P08607; -.
DR   CPTAC; non-CPTAC-3318; -.
DR   MaxQB; P08607; -.
DR   PaxDb; P08607; -.
DR   PeptideAtlas; P08607; -.
DR   PRIDE; P08607; -.
DR   Antibodypedia; 694; 300 antibodies from 29 providers.
DR   DNASU; 12269; -.
DR   Ensembl; ENSMUST00000027657; ENSMUSP00000027657; ENSMUSG00000026405.
DR   GeneID; 12269; -.
DR   KEGG; mmu:12269; -.
DR   UCSC; uc007cmc.1; mouse.
DR   CTD; 12269; -.
DR   MGI; MGI:88229; C4bp.
DR   VEuPathDB; HostDB:ENSMUSG00000026405; -.
DR   eggNOG; ENOG502SHRK; Eukaryota.
DR   GeneTree; ENSGT00940000154640; -.
DR   HOGENOM; CLU_020107_5_2_1; -.
DR   InParanoid; P08607; -.
DR   OMA; WKPQIPS; -.
DR   OrthoDB; 1058295at2759; -.
DR   PhylomeDB; P08607; -.
DR   TreeFam; TF334137; -.
DR   BioGRID-ORCS; 12269; 2 hits in 72 CRISPR screens.
DR   PRO; PR:P08607; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; P08607; protein.
DR   Bgee; ENSMUSG00000026405; Expressed in left lobe of liver and 41 other tissues.
DR   ExpressionAtlas; P08607; baseline and differential.
DR   Genevisible; P08607; MM.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0045959; P:negative regulation of complement activation, classical pathway; ISO:MGI.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR   GO; GO:1903027; P:regulation of opsonization; ISO:MGI.
DR   GO; GO:0009609; P:response to symbiotic bacterium; ISO:MGI.
DR   CDD; cd00033; CCP; 6.
DR   InterPro; IPR040514; C4bp_oligo.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   Pfam; PF18453; C4bp_oligo; 1.
DR   Pfam; PF00084; Sushi; 6.
DR   SMART; SM00032; CCP; 6.
DR   SUPFAM; SSF57535; SSF57535; 6.
DR   PROSITE; PS50923; SUSHI; 6.
PE   1: Evidence at protein level;
KW   Complement pathway; Disulfide bond; Glycoprotein; Immunity;
KW   Innate immunity; Reference proteome; Repeat; Secreted; Signal; Sushi.
FT   SIGNAL          1..56
FT   CHAIN           57..469
FT                   /note="C4b-binding protein"
FT                   /id="PRO_0000005889"
FT   DOMAIN          57..117
FT                   /note="Sushi 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          118..178
FT                   /note="Sushi 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          179..242
FT                   /note="Sushi 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          243..301
FT                   /note="Sushi 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          302..357
FT                   /note="Sushi 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          358..415
FT                   /note="Sushi 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        275
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17330941"
FT   CARBOHYD        292
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        366
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        381
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        428
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        58..103
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        88..115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        120..160
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        146..176
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        181..223
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        209..240
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        245..287
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        273..299
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        303..343
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        329..355
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        359..400
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        386..413
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
SQ   SEQUENCE   469 AA;  51524 MW;  14266B31430F7107 CRC64;
     MCAKQQQTLL PTRAAHGRLH RNRDAVAWPF STLCRVSGPT LFQMTFTAAL WVAVFGKCGP
     PPAIPNALPA SDVNRTDFES HTTLKYECLP GYGRGISRMM VYCKPSGEWE ISVSCAKKHC
     RNPGYLDNGY VNGETITFGS QIEFSCQEGF ILVGSSTSSC EVRGKGVAWS NPFPECVIVK
     CGPPPDISNG KHSGTEDFYP YNHGISYTCD PGFRLVGSPF IGCTVVNKTV PVWSSSPPTC
     EKIICSQPNI LHGVIVSGYK ATYTHRDSVR LACLNGTVLR GRHVIECQGN GNWSSLPTCE
     FDCDLPPAIV NGYYTSMVYS KITLVTYECD KGYRLVGKAI ISCSFSKWKG TAPQCKALCQ
     KPEVGNGTLS DEKDQYVESE NVTIQCDSGF AMLGSQSISC SESGTWYPEV PRCEQEASED
     LKPALTGNKT MQYVPNSHDV KMALEIYKLT LEVELLQLQI QKEKHTEAH
 
 
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