PROP_CAVPO
ID PROP_CAVPO Reviewed; 470 AA.
AC Q64181;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Properdin;
DE AltName: Full=Complement factor P;
DE Flags: Precursor;
GN Name=CFP; Synonyms=PFC;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RX PubMed=8550088;
RA Maves K.K., Guenthner S.T., Densen P., Moser D.R., Weiler J.M.;
RT "Cloning and characterization of the cDNA encoding guinea-pig properdin: a
RT comparison of properdin from three species.";
RL Immunology 86:475-479(1995).
CC -!- FUNCTION: A positive regulator of the alternate pathway of complement
CC (By similarity). 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 -!- 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 (By similarity). Interacts with CFB (By similarity).
CC {ECO:0000250|UniProtKB:P27918}.
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; S81116; AAB35918.1; -; mRNA.
DR AlphaFoldDB; Q64181; -.
DR SMR; Q64181; -.
DR STRING; 10141.ENSCPOP00000006537; -.
DR eggNOG; KOG4475; Eukaryota.
DR InParanoid; Q64181; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.20.100.10; -; 5.
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 2: Evidence at transcript level;
KW Complement alternate pathway; Disulfide bond; Glycoprotein; Immunity;
KW Innate immunity; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT CHAIN 27..470
FT /note="Properdin"
FT /id="PRO_0000035862"
FT DOMAIN 27..75
FT /note="TSP type-1 0"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 76..133
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 135..190
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 192..254
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 256..312
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 314..376
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 380..463
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 350..358
FT /note="Interaction with Complement C3 beta chain"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 82
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 85
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 144
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 150
FT /note="O-linked (Fuc...) threonine"
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 201
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 207
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 259
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 262
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 271
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 320
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 323
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 386
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 389
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..55
FT /evidence="ECO:0000250|UniProtKB:P27918,
FT ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 42..71
FT /evidence="ECO:0000250|UniProtKB:P27918,
FT ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 56..74
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT DISULFID 88..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 92..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 103..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 131..169
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT DISULFID 147..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 151..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 162..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 204..247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 208..253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 223..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 268..305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 272..311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 283..295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 326..369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 336..375
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 349..359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 392..456
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 396..462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 408..440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
SQ SEQUENCE 470 AA; 51431 MW; FDC2B393DC7EC15F CRC64;
MTAPVQVPQS LLLLLMLLLT LPATGSDPVL CFSQYEDSSS KCKDLLGKDV SLEDCCLNAA
YAFKERDNGH CQACRSPRWS PWSSWAPCSV SCSEGSQLRH RRCIGWGGQC SENKAPGTLE
WQLQACEEQQ CCPEMGGWSN WEPWGPCTVT CSKGTRIRRR VCNNPAPKCG GHCPGVAQES
EACDTQQVCP THGAWGPWGP WSSCLSSCHG GPHKPVETRS RTCSAPEPSK NPPGNPCPGT
AYEQQSCAGL PPCPVAGGWG PWGSVSPCSV TCGLGQILEQ RKCDNPVPQH GGSFCTGDDT
RAHICNTAVP CPVDGEWEPW GDWSTCTRPH LSAIRCKEIV GQQTRVRICK GRKFNGQRCP
GKHQEIRHCY NIQNCIFGEK GSWSQWTPWG LCTPPCGANP TRVRQRRCMA SLPKFSPTVS
VVEGQGEKNV TFWGKPLAQC EELQGQKVLL EEKRPCLHVP ACKDPEEEEP
