ID A0A093QXP9_PHACA Unreviewed; 1683 AA.
AC A0A093QXP9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Complement C5 {ECO:0000313|EMBL:KFW88707.1};
GN ORFNames=N336_06216 {ECO:0000313|EMBL:KFW88707.1};
OS Phalacrocorax carbo (Great cormorant) (Pelecanus carbo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Suliformes; Phalacrocoracidae;
OC Phalacrocorax.
OX NCBI_TaxID=9209 {ECO:0000313|EMBL:KFW88707.1, ECO:0000313|Proteomes:UP000053238};
RN [1] {ECO:0000313|EMBL:KFW88707.1, ECO:0000313|Proteomes:UP000053238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N336 {ECO:0000313|EMBL:KFW88707.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; KL421070; KFW88707.1; -; Genomic_DNA.
DR MEROPS; I39.952; -.
DR Proteomes; UP000053238; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd00017; ANATO; 1.
DR CDD; cd02896; complement_C3_C4_C5; 1.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 2.20.130.20; -; 1.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 2.60.120.1540; -; 1.
DR Gene3D; 2.60.40.1930; -; 3.
DR Gene3D; 2.60.40.1940; -; 1.
DR Gene3D; 6.20.50.160; -; 1.
DR Gene3D; 2.60.40.690; Alpha-macroglobulin, receptor-binding domain; 1.
DR Gene3D; 1.20.91.20; Anaphylotoxins (complement system); 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR000020; Anaphylatoxin/fibulin.
DR InterPro; IPR018081; Anaphylatoxin_comp_syst.
DR InterPro; IPR041425; C3/4/5_MG1.
DR InterPro; IPR048843; C5_CUB.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR041555; MG3.
DR InterPro; IPR040839; MG4.
DR InterPro; IPR001134; Netrin_domain.
DR InterPro; IPR018933; Netrin_module_non-TIMP.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR11412:SF83; COMPLEMENT C5; 1.
DR PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF01821; ANATO; 1.
DR Pfam; PF21309; C5_CUB; 1.
DR Pfam; PF17790; MG1; 1.
DR Pfam; PF01835; MG2; 1.
DR Pfam; PF17791; MG3; 1.
DR Pfam; PF17789; MG4; 1.
DR Pfam; PF01759; NTR; 1.
DR Pfam; PF07678; TED_complement; 1.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SMART; SM01361; A2M_recep; 1.
DR SMART; SM00104; ANATO; 1.
DR SMART; SM00643; C345C; 1.
DR SUPFAM; SSF49410; Alpha-macroglobulin receptor domain; 1.
DR SUPFAM; SSF47686; Anaphylotoxins (complement system); 1.
DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR SUPFAM; SSF50242; TIMP-like; 1.
DR PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
DR PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
DR PROSITE; PS50189; NTR; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000053238};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1683
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001890114"
FT DOMAIN 701..736
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS01178"
FT DOMAIN 1539..1683
FT /note="NTR"
FT /evidence="ECO:0000259|PROSITE:PS50189"
SQ SEQUENCE 1683 AA; 188726 MW; 0B22972C8D3D9986 CRC64;
MNILISFFVL MFSGMTFGQT KTYVLTAPKI FRAGASEKVV VQAFGYEKEF PVDIAIRSFP
DKLTVYSSGR ISLTPANKFQ DAVTLTLQPA DLPRTENSVN YVYLEAVSPY FTRFKKIPVS
YENGFLFIHT DKPVYTPDQS VKVRVYSLNE ELQPARRATV LTFVDPEGVK VDIIEEEDFT
GIVSFPDFKI PPNPKYGIWK IEAKYKKNFV TSAVAKFEVK EYAMPSFSIV IEPESNFISF
DKFESFRIVV KASYFYNKRL ASADVFLRFG IIEETGKRMM PQAMHVTRIE NGIAEINFNS
KKAVSFIGFQ SLEELDGSYL YIVASVLESM GGLSGEAEFA GVRFAISPYK LSLIATPLFV
KPGLPFFIKV QVKDTVDHFV GNIPITVTAK SLSEQMDETQ LISEGSESGR SKTSMNDGTA
LFVVNIPADS KMLEFEVKTA DPHLSDENQA SRTYEARAYS SLSQSYLYID WASNHKVLEV
GDFISINVYP HSHYIDKIDH YSYLIMSKGK IVSFGTQKRI KDLEYEHLAF QITQEMVPSA
RLVVYYIVTG EQTAELVADS VWLNVEQKCG NSLDIKLQSS KEILNPAGVV SLNMKTQFNS
FVALSSIDKA IYGVTGRGKR AMEKIMLQLE KSDRGCGAGG GRNNIDVFRI AGLTFLTNAN
ADDSNEADET CSEVLRTKRS EFEERIHKEV AKYAHQEIRK CCMAGVKAYP VTETCSDRAQ
RIRRSAKCIS AFKNCCEFAN RLREEEPNKI LILARMHFEA VLELDEAEVR SYFPESWLWE
VHQVSPRSKT LSVTLPDSLT TWEIQGVGIS DKGICVAAPL ELQVVKDIFL SIYVPYSVVR
GEQIELKGSV YNHKASPIKF CVKLAAGNGI CSFGGSATTG SGIHRCNFKN LGGGSSSPVT
FRILPLELGL HTINFTLLTA RNSETVVKTL RVMPEGIKKE LHAGFTLDPQ GVYGSMKRRQ
EFRYKIPLNL VPKTKIDRSV SVKGHLMGEV IATVLSPSGV DALTNLPKGS AEAELMSIAP
VFYVFRYLEE SNNWQLLGPE ILTSRTQMRR KMKEGIVSIL SFRNPDFSYS MWKNGLASTW
LTAFALRILG QVNQYINLDQ ISVCNSLLWL IDNCQMPDGS FSEFSNYQPV KLQGTLPREA
EEKSLYLTAF SVIGIEKSIK MCSTQKIHDA KNKAGDYLMK NVGSAQSPFT MAITSYALAL
VDLNHHSARS AFSALKKEAS VIGDPPLYRF WKDTFKTADQ HTPSSVTAQT VETTAYALLT
TLLRGDKNYA NPIIKWLSEE QRHGGGFHST QDTINALEAL TEYSLLVKRL HLDMNVKVAY
KNHGDVDLFK LTEDNFVGRT MTVPFDDDIY VSTGSSTGIA TVNVRTVYNT IGTSEESCNF
DLKIVPKRDD GYRREDGEPL GRLEACAKYR PRAREPQSGS AHAVMDIGLV SGLEANTEDL
STLASGVDQL IEDYEIRDGH VILQIDSVCY PFHNSNNFLC VGFRISELFQ VGMLNPATFT
VYEYHAPDKR CTIFYNPYGI EKLVRLCEGD ECKCMEAECS KLQERLNLSI SADTRREAAC
QDDIAYVYKV NILSRSEEGY FVKYSAVLLD VYKRGQAFAQ KNNEITFVKK KTCTDVELSP
GEQYLIMGKE ALKISVGYNF KFQYPLDSST WIEWWPSNTA CTFCQDFLNT MEDFAEDLII
SGC
//
