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Complement component C7

 CO7_PONAB               Reviewed;         843 AA.
Q5RAD0;
24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 1.
28-FEB-2018, entry version 66.
RecName: Full=Complement component C7;
Flags: Precursor;
Name=C7;
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pongo.
NCBI_TaxID=9601;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
The German cDNA consortium;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Constituent of the membrane attack complex (MAC) that
plays a key role in the innate and adaptive immune response by
forming pores in the plasma membrane of target cells. C7 serves as
a membrane anchor (By similarity). {ECO:0000250}.
-!- SUBUNIT: Monomer or dimer; as a C5b-7 complex it can also form
multimeric rosettes (By similarity). Component of the membrane
attack complex (MAC). MAC assembly is initiated by proteolytic
cleavage of C5 into C5a and C5b. C5b binds sequentially C6, C7, C8
and multiple copies of the pore-forming subunit C9 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- PTM: C7 has 28 disulfide bridges. {ECO:0000250}.
-!- PTM: C-, N- and O-glycosylated. {ECO:0000250|UniProtKB:P10643}.
-!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
{ECO:0000305}.
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EMBL; CR859088; CAH91280.1; -; mRNA.
RefSeq; NP_001125756.1; NM_001132284.1.
ProteinModelPortal; Q5RAD0; -.
SMR; Q5RAD0; -.
STRING; 9601.ENSPPYP00000017232; -.
GeneID; 100172681; -.
KEGG; pon:100172681; -.
CTD; 730; -.
eggNOG; ENOG410IDXP; Eukaryota.
eggNOG; ENOG410YJ70; LUCA.
HOVERGEN; HBG005367; -.
InParanoid; Q5RAD0; -.
KO; K03996; -.
Proteomes; UP000001595; Unplaced.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005579; C:membrane attack complex; IEA:UniProtKB-KW.
GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
CDD; cd00033; CCP; 2.
CDD; cd00112; LDLa; 1.
Gene3D; 2.20.100.10; -; 2.
InterPro; IPR037564; Complement_C7.
InterPro; IPR003884; FacI_MAC.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
InterPro; IPR001862; MAC_perforin.
InterPro; IPR020864; MACPF.
InterPro; IPR020863; MACPF_CS.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
InterPro; IPR000884; TSP1_rpt.
InterPro; IPR036383; TSP1_rpt_sf.
PANTHER; PTHR19325:SF389; PTHR19325:SF389; 1.
Pfam; PF00057; Ldl_recept_a; 1.
Pfam; PF01823; MACPF; 1.
Pfam; PF00084; Sushi; 2.
Pfam; PF00090; TSP_1; 2.
PRINTS; PR00764; COMPLEMENTC9.
SMART; SM00032; CCP; 2.
SMART; SM00057; FIMAC; 2.
SMART; SM00192; LDLa; 1.
SMART; SM00457; MACPF; 1.
SMART; SM00209; TSP1; 2.
SUPFAM; SSF57535; SSF57535; 2.
SUPFAM; SSF82895; SSF82895; 2.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS01209; LDLRA_1; 1.
PROSITE; PS50068; LDLRA_2; 1.
PROSITE; PS00279; MACPF_1; 1.
PROSITE; PS51412; MACPF_2; 1.
PROSITE; PS50923; SUSHI; 2.
PROSITE; PS50092; TSP1; 2.
2: Evidence at transcript level;
Complement alternate pathway; Complement pathway; Complete proteome;
Cytolysis; Disulfide bond; EGF-like domain; Glycoprotein; Immunity;
Innate immunity; Membrane attack complex; Reference proteome; Repeat;
Secreted; Signal; Sushi.
SIGNAL 1 22 {ECO:0000250}.
CHAIN 23 843 Complement component C7.
/FTId=PRO_0000045782.
DOMAIN 27 80 TSP type-1 1. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 83 121 LDL-receptor class A.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 124 456 MACPF. {ECO:0000255|PROSITE-
ProRule:PRU00745}.
DOMAIN 457 487 EGF-like.
DOMAIN 500 549 TSP type-1 2. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 569 628 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 629 690 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
REGION 545 615 CCP 1.
REGION 616 693 CCP 2.
REGION 695 770 Factor I module (FIM) 1.
REGION 771 843 Factor I module (FIM) 2.
CARBOHYD 36 36 C-linked (Man) tryptophan.
{ECO:0000250|UniProtKB:P10643}.
CARBOHYD 202 202 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 503 503 C-linked (Man) tryptophan.
{ECO:0000250|UniProtKB:P10643}.
CARBOHYD 506 506 C-linked (Man) tryptophan.
{ECO:0000250|UniProtKB:P10643}.
CARBOHYD 509 509 C-linked (Man) tryptophan.
{ECO:0000250|UniProtKB:P10643}.
CARBOHYD 696 696 O-linked (GalNAc...) threonine.
{ECO:0000250|UniProtKB:P10643}.
CARBOHYD 754 754 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 85 96 {ECO:0000250}.
DISULFID 91 109 {ECO:0000250}.
DISULFID 103 119 {ECO:0000250}.
DISULFID 128 165 {ECO:0000250}.
DISULFID 337 353 {ECO:0000250}.
DISULFID 571 613 {ECO:0000250}.
DISULFID 599 626 {ECO:0000250}.
DISULFID 631 673 {ECO:0000250}.
DISULFID 659 688 {ECO:0000250}.
DISULFID 702 713 {ECO:0000250}.
DISULFID 715 750 {ECO:0000250}.
DISULFID 721 743 {ECO:0000250}.
DISULFID 728 763 {ECO:0000250}.
DISULFID 773 782 {ECO:0000250}.
DISULFID 776 789 {ECO:0000250}.
DISULFID 791 825 {ECO:0000250}.
DISULFID 797 818 {ECO:0000250}.
DISULFID 805 838 {ECO:0000250}.
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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