GenomeNet

Database: UniProt
Entry: Q5RAD0
LinkDB: Q5RAD0
Original site: Q5RAD0 
ID   CO7_PONAB               Reviewed;         843 AA.
AC   Q5RAD0;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   13-FEB-2019, entry version 69.
DE   RecName: Full=Complement component C7;
DE   Flags: Precursor;
GN   Name=C7;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Constituent of the membrane attack complex (MAC) that
CC       plays a key role in the innate and adaptive immune response by
CC       forming pores in the plasma membrane of target cells. C7 serves as
CC       a membrane anchor (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer or dimer; as a C5b-7 complex it can also form
CC       multimeric rosettes (By similarity). Component of the membrane
CC       attack complex (MAC). MAC assembly is initiated by proteolytic
CC       cleavage of C5 into C5a and C5b. C5b binds sequentially C6, C7, C8
CC       and multiple copies of the pore-forming subunit C9 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- PTM: C7 has 28 disulfide bridges. {ECO:0000250}.
CC   -!- PTM: C-, N- and O-glycosylated. {ECO:0000250|UniProtKB:P10643}.
CC   -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC       {ECO:0000305}.
DR   EMBL; CR859088; CAH91280.1; -; mRNA.
DR   RefSeq; NP_001125756.1; NM_001132284.1.
DR   ProteinModelPortal; Q5RAD0; -.
DR   SMR; Q5RAD0; -.
DR   STRING; 9601.ENSPPYP00000017232; -.
DR   PRIDE; Q5RAD0; -.
DR   GeneID; 100172681; -.
DR   KEGG; pon:100172681; -.
DR   CTD; 730; -.
DR   eggNOG; ENOG410IDXP; Eukaryota.
DR   eggNOG; ENOG410YJ70; LUCA.
DR   HOVERGEN; HBG005367; -.
DR   InParanoid; Q5RAD0; -.
DR   KO; K03996; -.
DR   OrthoDB; 100680at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005579; C:membrane attack complex; IEA:UniProtKB-KW.
DR   GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
DR   GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   CDD; cd00033; CCP; 2.
DR   CDD; cd00112; LDLa; 1.
DR   Gene3D; 2.20.100.10; -; 2.
DR   InterPro; IPR037564; Complement_C7.
DR   InterPro; IPR003884; FacI_MAC.
DR   InterPro; IPR040729; Kazal_3.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR001862; MAC_perforin.
DR   InterPro; IPR020864; MACPF.
DR   InterPro; IPR020863; MACPF_CS.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   PANTHER; PTHR19325:SF389; PTHR19325:SF389; 1.
DR   Pfam; PF18434; Kazal_3; 1.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   Pfam; PF01823; MACPF; 1.
DR   Pfam; PF00084; Sushi; 2.
DR   Pfam; PF00090; TSP_1; 2.
DR   PRINTS; PR00764; COMPLEMENTC9.
DR   SMART; SM00032; CCP; 2.
DR   SMART; SM00057; FIMAC; 2.
DR   SMART; SM00192; LDLa; 1.
DR   SMART; SM00457; MACPF; 1.
DR   SMART; SM00209; TSP1; 2.
DR   SUPFAM; SSF57535; SSF57535; 2.
DR   SUPFAM; SSF82895; SSF82895; 2.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
DR   PROSITE; PS00279; MACPF_1; 1.
DR   PROSITE; PS51412; MACPF_2; 1.
DR   PROSITE; PS50923; SUSHI; 2.
DR   PROSITE; PS50092; TSP1; 2.
PE   2: Evidence at transcript level;
KW   Complement alternate pathway; Complement pathway; Complete proteome;
KW   Cytolysis; Disulfide bond; EGF-like domain; Glycoprotein; Immunity;
KW   Innate immunity; Membrane attack complex; Reference proteome; Repeat;
KW   Secreted; Signal; Sushi.
FT   SIGNAL        1     22       {ECO:0000250}.
FT   CHAIN        23    843       Complement component C7.
FT                                /FTId=PRO_0000045782.
FT   DOMAIN       27     80       TSP type-1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN       83    121       LDL-receptor class A.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      124    456       MACPF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00745}.
FT   DOMAIN      457    487       EGF-like.
FT   DOMAIN      500    549       TSP type-1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      569    628       Sushi 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      629    690       Sushi 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   REGION      545    615       CCP 1.
FT   REGION      616    693       CCP 2.
FT   REGION      695    770       Factor I module (FIM) 1.
FT   REGION      771    843       Factor I module (FIM) 2.
FT   CARBOHYD     36     36       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P10643}.
FT   CARBOHYD    202    202       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    503    503       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P10643}.
FT   CARBOHYD    506    506       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P10643}.
FT   CARBOHYD    509    509       C-linked (Man) tryptophan.
FT                                {ECO:0000250|UniProtKB:P10643}.
FT   CARBOHYD    696    696       O-linked (GalNAc...) threonine.
FT                                {ECO:0000250|UniProtKB:P10643}.
FT   CARBOHYD    754    754       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     85     96       {ECO:0000250}.
FT   DISULFID     91    109       {ECO:0000250}.
FT   DISULFID    103    119       {ECO:0000250}.
FT   DISULFID    128    165       {ECO:0000250}.
FT   DISULFID    337    353       {ECO:0000250}.
FT   DISULFID    571    613       {ECO:0000250}.
FT   DISULFID    599    626       {ECO:0000250}.
FT   DISULFID    631    673       {ECO:0000250}.
FT   DISULFID    659    688       {ECO:0000250}.
FT   DISULFID    702    713       {ECO:0000250}.
FT   DISULFID    715    750       {ECO:0000250}.
FT   DISULFID    721    743       {ECO:0000250}.
FT   DISULFID    728    763       {ECO:0000250}.
FT   DISULFID    773    782       {ECO:0000250}.
FT   DISULFID    776    789       {ECO:0000250}.
FT   DISULFID    791    825       {ECO:0000250}.
FT   DISULFID    797    818       {ECO:0000250}.
FT   DISULFID    805    838       {ECO:0000250}.
SQ   SEQUENCE   843 AA;  93524 MW;  E73CA154FAE97E62 CRC64;
     MKVISLFILV GFIGESQIFS SASSPVNCQW DSYTPWSECN GCTKTQTRRR SVAVYGQYGG
     QPCVGNAFET QSCEPTRGCP TEEGCGERFR CFSGQCISKS LVCNGDSDCD EDSADEDRCE
     DSERRPSCDI DKPPPNIELT GNGYNELTGQ FRNRVINTKS FGGQCRKVFS GDGKRFYRLS
     GNVLSYTFQV KINNDFNYEF YNSTWSYVKH TSTEHTSSSR KRSFFRSSSS SSRSYTTHTN
     EIHKGKSYQL LVVENTVEVT QFINNNPEFL QLAEPFWKEL SHLPSLYDYS AYRRLIDQYG
     THYLQSGSLG GEYRVLFYVD SEKLKQNGFT SVEEKKCKSS GWHFVVKFSS HGCKELENAL
     KAASGTQNNV LRGNPFIRGG GAGFISSLSY LELDNPAGNK RRYSAWAKSV TDLPKVIKQK
     LTPLYELVKE VPCVSVKKLY LKRALEEYLD EFDPCHCRPC QNGGLATVEG THCLCHCKPY
     TFGAACEQGV LVGNQAGGVD GGWSCWSSWS SCVQGKKTRS RECNNPPPSG GGRSCIGETT
     ESTQCEDEEL EHLRLLEPHC FPLSLVPTEF CPSPPALKDG FVQDEGTMFP VGKNVVYTCN
     EGYSLIGNPV ARCGEDLQWL VGEMHCQKIA CVLPVLMDGI QSHPQKPFYT VGEKVTVSCS
     GGMSLEGPSA FLCGSSLKWS PEMKNAHCVQ KENPLTQAVP KCQRWEKLQN SRCVCKMPYE
     CVPSLDVCAR DERSKRILPL TVCKMHVLHC QGRNYTLTGR DSCTLPASAE KACGACPLWG
     KCDAESSKCV CREASECEEE GFSICVEVNG KEQTMSECEA GSLRCRGQSI SVTSIRPCAA
     ETQ
//
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