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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
 
 
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