PROP_MOUSE
ID PROP_MOUSE Reviewed; 464 AA.
AC P11680; Q3TB98; Q3U779;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Properdin;
DE AltName: Full=Complement factor P;
DE Flags: Precursor;
GN Name=Cfp; Synonyms=Pfc;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-464.
RC TISSUE=Macrophage;
RX PubMed=3045564; DOI=10.1038/335082a0;
RA Goundis A., Reid K.B.M.;
RT "Properdin, the terminal complement components, thrombospondin and the
RT circumsporozoite protein of malaria parasites contain similar sequence
RT motifs.";
RL Nature 335:82-85(1988).
RN [3]
RP FUNCTION, AND INTERACTION WITH C3.
RX PubMed=28264884; DOI=10.15252/embj.201696173;
RA Pedersen D.V., Roumenina L., Jensen R.K., Gadeberg T.A., Marinozzi C.,
RA Picard C., Rybkine T., Thiel S., Soerensen U.B., Stover C.,
RA Fremeaux-Bacchi V., Andersen G.R.;
RT "Functional and structural insight into properdin control of complement
RT alternative pathway amplification.";
RL EMBO J. 36:1084-1099(2017).
CC -!- FUNCTION: A positive regulator of the alternate pathway of complement
CC (PubMed:28264884). It binds to and stabilizes the C3- and C5-convertase
CC enzyme complexes (By similarity). Inhibits CFI-CFH mediated degradation
CC of Inhibits CFI-CFH mediated degradation of Complement C3 beta chain
CC (C3b) (By similarity). {ECO:0000250|UniProtKB:P27918,
CC ECO:0000269|PubMed:28264884}.
CC -!- SUBUNIT: In plasma, properdin exists as dimers, trimers or tetramers in
CC the relative proportions of 26:54:20 (By similarity). Interacts with
CC the pro-C3-convertase enzyme complex (C3b-Bb) comprised of Complement
CC C3 beta chain (C3b) and the Complement factor B Bb fragment (Bb), where
CC it binds (via its TSP type-1 5 domain) with C3b and Bb (By similarity).
CC This interaction stabilizes the complex and allows it to become the
CC active C3-convertase enzyme complex (C3b-Bb-FP) (By similarity).
CC Interacts with C3b (PubMed:28264884). Interacts with CFB (By
CC similarity). {ECO:0000250|UniProtKB:P27918,
CC ECO:0000269|PubMed:28264884}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P27918}.
CC -!- DOMAIN: TSP type-1 domain 0 binds to TSP type-1 domain 4, and TSP type-
CC 1 domain 1 binds to TSP type-1 domain 6 (By similarity). These
CC interactions mediate multimerization (By similarity).
CC {ECO:0000250|UniProtKB:P27918}.
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DR EMBL; AK150212; BAE29382.1; -; mRNA.
DR EMBL; AK152782; BAE31492.1; -; mRNA.
DR EMBL; AK159291; BAE34967.1; -; mRNA.
DR EMBL; AK171374; BAE42416.1; -; mRNA.
DR EMBL; X12905; CAA31389.1; -; mRNA.
DR CCDS; CCDS30047.1; -.
DR PIR; S05478; S05478.
DR RefSeq; NP_032849.2; NM_008823.4.
DR AlphaFoldDB; P11680; -.
DR SMR; P11680; -.
DR BioGRID; 202120; 5.
DR ComplexPortal; CPX-5896; Alternative pathway pathogen cell-bound C3 convertase complex C3bBbP.
DR ComplexPortal; CPX-5897; Alternative pathway pathogen cell-bound C5 convertase complex C3bBbC3bP.
DR IntAct; P11680; 3.
DR STRING; 10090.ENSMUSP00000001156; -.
DR GlyGen; P11680; 19 sites.
DR iPTMnet; P11680; -.
DR PhosphoSitePlus; P11680; -.
DR SwissPalm; P11680; -.
DR CPTAC; non-CPTAC-3605; -.
DR MaxQB; P11680; -.
DR PaxDb; P11680; -.
DR PeptideAtlas; P11680; -.
DR PRIDE; P11680; -.
DR ProteomicsDB; 291602; -.
DR Antibodypedia; 11427; 530 antibodies from 31 providers.
DR DNASU; 18636; -.
DR Ensembl; ENSMUST00000001156; ENSMUSP00000001156; ENSMUSG00000001128.
DR GeneID; 18636; -.
DR KEGG; mmu:18636; -.
DR UCSC; uc009sub.1; mouse.
DR CTD; 5199; -.
DR MGI; MGI:97545; Cfp.
DR VEuPathDB; HostDB:ENSMUSG00000001128; -.
DR eggNOG; KOG4475; Eukaryota.
DR GeneTree; ENSGT00940000161209; -.
DR HOGENOM; CLU_047129_0_0_1; -.
DR InParanoid; P11680; -.
DR OMA; RWRTCKG; -.
DR OrthoDB; 304371at2759; -.
DR PhylomeDB; P11680; -.
DR TreeFam; TF315491; -.
DR Reactome; R-MMU-173736; Alternative complement activation.
DR Reactome; R-MMU-174577; Activation of C3 and C5.
DR Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR BioGRID-ORCS; 18636; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Cfp; mouse.
DR PRO; PR:P11680; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P11680; protein.
DR Bgee; ENSMUSG00000001128; Expressed in granulocyte and 139 other tissues.
DR ExpressionAtlas; P11680; baseline and differential.
DR Genevisible; P11680; MM.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; IDA:MGI.
DR GO; GO:0006956; P:complement activation; IC:ComplexPortal.
DR GO; GO:0006957; P:complement activation, alternative pathway; IMP:MGI.
DR GO; GO:0050778; P:positive regulation of immune response; IC:ComplexPortal.
DR GO; GO:1903028; P:positive regulation of opsonization; IC:ComplexPortal.
DR Gene3D; 2.20.100.10; -; 6.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR Pfam; PF00090; TSP_1; 6.
DR SMART; SM00209; TSP1; 6.
DR SUPFAM; SSF82895; SSF82895; 6.
DR PROSITE; PS50092; TSP1; 6.
PE 1: Evidence at protein level;
KW Complement alternate pathway; Disulfide bond; Glycoprotein; Immunity;
KW Innate immunity; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..464
FT /note="Properdin"
FT /id="PRO_0000043369"
FT DOMAIN 24..72
FT /note="TSP type-1 0"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 73..130
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 132..187
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 189..251
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 253..309
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 311..372
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 374..457
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 346..354
FT /note="Interaction with Complement C3 beta chain"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 79
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 82
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 135
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 138
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 141
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 147
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 192
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 195
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 198
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 204
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 256
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 259
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 268
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 317
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 320
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 377
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 380
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 383
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..52
FT /evidence="ECO:0000250|UniProtKB:P27918,
FT ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 39..68
FT /evidence="ECO:0000250|UniProtKB:P27918,
FT ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 53..71
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT DISULFID 85..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 89..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 100..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 128..166
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT DISULFID 144..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 148..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 159..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 201..244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 205..250
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 220..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 265..302
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 269..308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 280..292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 323..365
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 332..371
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 345..355
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 386..450
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 390..456
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 402..434
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT CONFLICT 58
FT /note="Y -> N (in Ref. 1; BAE42416)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="C -> R (in Ref. 2; CAA31389)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="G -> D (in Ref. 2; CAA31389)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 464 AA; 50327 MW; C787F5493042379A CRC64;
MPAEMQAPQW LLLLLVILPA TGSDPVLCFT QYEESSGRCK GLLGRDIRVE DCCLNAAYAF
QEHDGGLCQA CRSPQWSAWS LWGPCSVTCS EGSQLRHRRC VGRGGQCSEN VAPGTLEWQL
QACEDQPCCP EMGGWSEWGP WGPCSVTCSK GTQIRQRVCD NPAPKCGGHC PGEAQQSQAC
DTQKTCPTHG AWASWGPWSP CSGSCLGGAQ EPKETRSRSC SAPAPSHQPP GKPCSGPAYE
HKACSGLPPC PVAGGWGPWS PLSPCSVTCG LGQTLEQRTC DHPAPRHGGP FCAGDATRNQ
MCNKAVPCPV NGEWEAWGKW SDCSRLRMSI NCEGTPGQQS RSRSCGGRKF NGKPCAGKLQ
DIRHCYNIHN CIMKGSWSQW STWSLCTPPC SPNATRVRQR LCTPLLPKYP PTVSMVEGQG
EKNVTFWGTP RPLCEALQGQ KLVVEEKRSC LHVPVCKDPE EKKP
