ID A0A2D0Q2S0_ICTPU Unreviewed; 1649 AA.
AC A0A2D0Q2S0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Complement C3 {ECO:0000313|RefSeq:XP_017313028.1};
GN Name=LOC108258708 {ECO:0000313|RefSeq:XP_017313028.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017313028.1};
RN [1] {ECO:0000313|RefSeq:XP_017313028.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017313028.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR RefSeq; XP_017313028.1; XM_017457539.3.
DR GeneID; 108258708; -.
DR KEGG; ipu:108258708; -.
DR OrthoDB; 4033541at2759; -.
DR Proteomes; UP000221080; Chromosome 26.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd00017; ANATO; 1.
DR CDD; cd02896; complement_C3_C4_C5; 1.
DR CDD; cd03583; NTR_complement_C3; 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; IPR047565; Alpha-macroglob_thiol-ester_cl.
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; IPR048848; C3_CUB2.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR019742; MacrogloblnA2_CS.
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; IPR035815; NTR_complement_C3.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR11412:SF81; COMPLEMENT C3; 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; PF21308; C3_CUB2; 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 SMART; SM01419; Thiol-ester_cl; 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; PS00477; ALPHA_2_MACROGLOBULIN; 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 Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Thioester bond {ECO:0000256|ARBA:ARBA00022966}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1649
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012903676"
FT DOMAIN 682..717
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS01178"
FT DOMAIN 1505..1647
FT /note="NTR"
FT /evidence="ECO:0000259|PROSITE:PS50189"
SQ SEQUENCE 1649 AA; 184077 MW; 59209FA48F85E0C4 CRC64;
MHVDLVWLTA TLLSFPLLTL CDPLNVLLAP NLLRIGTPER VFVEAQDYSG NDLQVKIIVK
NHPQGNTELT SESVTLNAAN NFQAVVNIVI PDNKNFFSDD PLEKQYVILQ AQFPSGLLEK
VALVSFQSGY IFVQTDKSIY TPGTEVRYRT FSLTPDLKPT DQTGGIYVEI LNSQGITINR
ETIFPKQGTI KGSYSIPEIA KPGIWSVVTR YKNTPQKNFT AEFEVKEYVL PSFEVALKSS
KSFFYVNDPD LQVDITAKYL FGRDVDGVAF VVFGVKRDDS KHPLPASLQR QTIRKGEGRA
VLTKEMIQRS FPNIVDLVGD SLYISVSVLT ETGSEIVEAE KGGIQIVTSP YTIQFKRTPK
FFHPGMSFDV TVYVTNPDQS PAENVEVLVK PGDVRGRTKS NGMAKVIVNT QGEDKTLQIT
ARTTAPDIPD ERQAENKMTA QAYTTKGNSN NYLHISIDAA ELKINDQINI NLNFKSSAQT
QDFTYLILSK GQIVRAERFK RQGQSLVTLS LPVTKDLVPS FRVVAYYHVG SSEVVSDSVW
VDVKDTCMGT LKLDVKESLN VKKVFEPGDE FHLIVTGDPS AKVGLVAVDK AVFVLNKNRL
TQSKVWDIIE KHDTGCTAGS GTNDMGVFYD AGLLFQSDKA GGTNIRSDPA CPAPPKRKRR
AVTLLQITQT LVGKYTGEQK KCCGDGLRSN RLGYSCDRRA NFILDGSECV QAFLDCCTEI
QKHRENQEEL LHLARSEDDD DDYISSDEIV TRTQFPESWL WDDIDLPACA RNLQCDSTSL
TLSTNYLKDS ITTWQVLAIS LSKTHGICVA DPYEITVAKD FFIDLKLPYS AVRNEQLEIK
AILYNFSNKK QKVRVEFFET EHVCSAASKK SKYRLTVNID PKSTRAIPYV IIPMEIGLHD
IEVQAATATL HDGVRKKLKV VSEGVLTELP EQNLELNPSR VPGGVQVLHL KTEVPNGQVP
NTPAQTYITV AGQEVSQTVE QAISGNFMGK LIVQPHGCGE QTMIYMTLPV IATHYLDTTK
QWEGVGVQRR SEAIQHIQTG YARELTFRKP DGSYAAWINR PSSTWLTAYV AKVFALASDL
ISIDENVLCG SIKWLILNAQ LPDGEFKESA PVYHAEMVGG VRGKDADASL TAFVLIALQE
ANHLCGKLVG SLPESSKKAI AYLERRLPSL TNQYAVAISS YALANAGNFN RDRLLQFSSE
DGAYWQVSGG HHFSLEATAY AVLALVKAKE FDAAGKAVNW LNRQSSPYGG HGTTQATIIV
FQAVAEYYKQ VRAGQNADLD VEVSVSGRKR AIRWTFTRNN AHLTRSDKVQ LKQEFNITAK
GTGAGVLKVV TLYYARPIEK KSDCTKYDLK VELKRERLVS YPDALESYEV IIDVLFKDPN
RDATMTILDI GLLTGFVVDE KDLTDLTSGR DKYIQKFEMD KQLSERGSLI IYVDKISHTV
PDRIAFRVHK ITSVALLQPA AVSVYEYYSP GERCVKFYHP VKKDGALNRL CSDQQDLCQC
AEENCSIQKK QKINEQDREK KACEADMDYV YKVKVLGVDQ NPNTDFYEMK IEEVLKEGSD
PDVREKVRSF MGHANCRESF GFEEGKSYLI MGRSVDLPRI DEKLQYILGE QTWIEYWPTR
EEGQTPAYKD KYIGISGLAQ TLTDFGCTT
//