PROP_PONAB
ID PROP_PONAB Reviewed; 469 AA.
AC Q5RBP8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Properdin;
DE AltName: Full=Complement factor P;
DE Flags: Precursor;
GN Name=CFP; Synonyms=PFC;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR858590; CAH90812.1; -; mRNA.
DR RefSeq; NP_001127338.1; NM_001133866.1.
DR RefSeq; XP_009233034.1; XM_009234759.1.
DR AlphaFoldDB; Q5RBP8; -.
DR SMR; Q5RBP8; -.
DR STRING; 9601.ENSPPYP00000022718; -.
DR Ensembl; ENSPPYT00000023680; ENSPPYP00000022718; ENSPPYG00000020298.
DR GeneID; 100174400; -.
DR KEGG; pon:100174400; -.
DR CTD; 5199; -.
DR eggNOG; KOG4475; Eukaryota.
DR GeneTree; ENSGT00940000161209; -.
DR HOGENOM; CLU_047129_0_0_1; -.
DR InParanoid; Q5RBP8; -.
DR OMA; RWRTCKG; -.
DR OrthoDB; 304371at2759; -.
DR TreeFam; TF315491; -.
DR Proteomes; UP000001595; Chromosome X.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0030141; C:secretory granule; IEA:Ensembl.
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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..469
FT /note="Properdin"
FT /id="PRO_0000043370"
FT DOMAIN 28..76
FT /note="TSP type-1 0"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 77..134
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 136..191
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 193..255
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 257..313
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 315..377
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 379..462
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 218..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..359
FT /note="Interaction with Complement C3 beta chain"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 83
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 86
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 139
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 142
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 145
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 151
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 196
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 199
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 202
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 208
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 260
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 263
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 272
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 321
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 324
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 382
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 385
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 388
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 32..56
FT /evidence="ECO:0000250|UniProtKB:P27918,
FT ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 43..72
FT /evidence="ECO:0000250|UniProtKB:P27918,
FT ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 57..75
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT DISULFID 89..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 93..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 104..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 132..170
FT /evidence="ECO:0000250|UniProtKB:P27918"
FT DISULFID 148..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 152..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 163..174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 205..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 209..254
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 224..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 269..306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 273..312
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 284..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 327..370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 337..376
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 350..360
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 391..455
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 395..461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 407..439
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
SQ SEQUENCE 469 AA; 51413 MW; FCFE26188199F4C3 CRC64;
MITEGAQAPR LLLPPLLLLL TLPATGSDPV LCFTRYEESS GKCKGLLGGG VSVKDCCLNT
ASAYQERSGG LCQPCRSPRW SLWSTWAPCS VTCSEGSQLR YRRCVGWNGQ CSEKVALGTL
EWQLQACEDQ QCCPEMGGWS GWGPWEPCSV TCSKGTRTRR RACNHPAPKC GGHCPGQAQE
SEACDTQQSC PTHGAWAAWG PWTPCSGSCH SGTHEPKETR SRKCSAPEPS QKPPGKPCPG
LAYEQRRCTG LPPCPVAGSW GPWGPVSPCP VTCGLGQTME QRTCDHPVPQ HGGPFCAGDA
TRTHICNTAV PCPVDGEWDS WGEWSTCVRR NMKSISCQEI PGQQSRWRTC KGRKFDGHRC
AGQQQDIRHC YSIQHCPLKG SWSEWSTWGL CIPPCGPNPT RARQRLCTPL LPKYPPTVSM
VEGQGEKNVT FWGRPLPRCE ELQGQKLVVE EKRPCLHVPA CKDPEEEKL