CO7_PONAB
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 25-MAY-2022, entry version 77.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 plays a
CC key role in the innate and adaptive immune response by forming pores in
CC the plasma membrane of target cells. C7 serves as a membrane anchor (By
CC 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 attack
CC complex (MAC). MAC assembly is initiated by proteolytic cleavage of C5
CC into C5a and C5b. C5b binds sequentially C6, C7, C8 and multiple copies
CC of the pore-forming subunit C9 (By 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}.
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DR EMBL; CR859088; CAH91280.1; -; mRNA.
DR RefSeq; NP_001125756.1; NM_001132284.1.
DR AlphaFoldDB; Q5RAD0; -.
DR BMRB; Q5RAD0; -.
DR SMR; Q5RAD0; -.
DR STRING; 9601.ENSPPYP00000017232; -.
DR GeneID; 100172681; -.
DR KEGG; pon:100172681; -.
DR CTD; 730; -.
DR eggNOG; ENOG502QU3G; Eukaryota.
DR InParanoid; Q5RAD0; -.
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 Gene3D; 4.10.400.10; -; 1.
DR InterPro; IPR037564; Complement_C7.
DR InterPro; IPR003884; FacI_MAC.
DR InterPro; IPR040729; Kazal_3.
DR InterPro; IPR036055; LDL_receptor-like_sf.
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; PTHR45742:SF2; PTHR45742:SF2; 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; Cytolysis;
KW Disulfide bond; EGF-like domain; Glycoprotein; Immunity; Innate immunity;
KW Membrane attack complex; Reference proteome; Repeat; Secreted; Signal;
KW Sushi.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..843
FT /note="Complement component C7"
FT /id="PRO_0000045782"
FT DOMAIN 27..80
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 83..121
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 124..456
FT /note="MACPF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT DOMAIN 457..487
FT /note="EGF-like"
FT DOMAIN 500..549
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 569..628
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 629..690
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 106..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..615
FT /note="CCP 1"
FT REGION 616..693
FT /note="CCP 2"
FT REGION 695..770
FT /note="Factor I module (FIM) 1"
FT REGION 771..843
FT /note="Factor I module (FIM) 2"
FT CARBOHYD 36
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P10643"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P10643"
FT CARBOHYD 506
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P10643"
FT CARBOHYD 509
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000250|UniProtKB:P10643"
FT CARBOHYD 696
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P10643"
FT CARBOHYD 754
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 85..96
FT /evidence="ECO:0000250"
FT DISULFID 91..109
FT /evidence="ECO:0000250"
FT DISULFID 103..119
FT /evidence="ECO:0000250"
FT DISULFID 128..165
FT /evidence="ECO:0000250"
FT DISULFID 337..353
FT /evidence="ECO:0000250"
FT DISULFID 571..613
FT /evidence="ECO:0000250"
FT DISULFID 599..626
FT /evidence="ECO:0000250"
FT DISULFID 631..673
FT /evidence="ECO:0000250"
FT DISULFID 659..688
FT /evidence="ECO:0000250"
FT DISULFID 702..713
FT /evidence="ECO:0000250"
FT DISULFID 715..750
FT /evidence="ECO:0000250"
FT DISULFID 721..743
FT /evidence="ECO:0000250"
FT DISULFID 728..763
FT /evidence="ECO:0000250"
FT DISULFID 773..782
FT /evidence="ECO:0000250"
FT DISULFID 776..789
FT /evidence="ECO:0000250"
FT DISULFID 791..825
FT /evidence="ECO:0000250"
FT DISULFID 797..818
FT /evidence="ECO:0000250"
FT DISULFID 805..838
FT /evidence="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
