ID W5MRU4_LEPOC Unreviewed; 1639 AA.
AC W5MRU4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Complement C3 {ECO:0000313|Ensembl:ENSLOCP00000011103.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000011103.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000011103.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; AHAT01007483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01007484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01007485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01007486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSLOCT00000011119.1; ENSLOCP00000011103.1; ENSLOCG00000009084.1.
DR GeneTree; ENSGT00940000154063; -.
DR HOGENOM; CLU_001634_4_0_1; -.
DR Proteomes; UP000018468; Linkage group LG6.
DR Bgee; ENSLOCG00000009084; Expressed in liver and 11 other cell types or tissues.
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 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000018468};
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..1639
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004868191"
FT DOMAIN 683..718
FT /note="Anaphylatoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS01178"
FT DOMAIN 1495..1637
FT /note="NTR"
FT /evidence="ECO:0000259|PROSITE:PS50189"
FT REGION 638..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1639 AA; 183489 MW; 2EE6C79C4D437D22 CRC64;
MNVFVVCLTV LSLSYPTTVS CQPLYVLTAP NVLRVESEEN ILLQAHDYVG GDLNVDILVF
DFPGKKQQLY VGSVILKPDQ YQATHKIKIP EGSFNKESKL NQYVYLQAKF GGHVVESAVL
VSFQSGYIFV QTDKSIYTPT DTVLYRVFAL TNRLDPSKSS VSVEIMTPDG IVIQKDLLFS
ANGIISGSYK LPEILSTGTW KVVTKFESTP QKNFTADFEV KEYVLPNFEV KLEPHQLFFY
IDDEELTVSV TARYLYGKDV VGSAYVVFGV VLDNDEKRSF PDSLQRIEIT AGKGTATLKR
QHILKIYKEM KEILKKSIYV SATVLTSTGS DIVEAERRGI QIVQSPYAIH FTKTPKYFKP
GMPFDVMVLV TNPDGTPASN IDVEISPEIS GRTQQQGTTK MTVNTRGDAT RLPITVKTKA
PNLTPDRQAT GSMEALPYRT QLNSKNYLHI GIQAAELEPG TNLQVNLNLG NDAGVQDQIK
YFSYQIVNKG QIMTAGKQAR LPGQSLVTLS LRIEKEMIPS FRFVAYYYLR KGGQIEVVAD
SVWVDVKDTC MGTLMDRISS KLRVTPTTDR DSLTLIGDPG AKVGLVAVDK GVYVLNNKNR
LSQSKIWDIV EKNDIGCTAG SGSDNMNVFN DAGLMFKSSS GSETKPRTDP TCPEPPKRRR
RSLVLGDIIT SLVSNFSGPL QKCCRDGMAE NIMDYTCEKR TQFIIEGKEC IDAFLHCCKE
IAKRHKERQR EMLALARSEE DDDYISDDEI VSRTEFPESW LWQIETLPTA PKDKDGFLKD
SITTWEITAI SLSPLKGICV ADVYEITVLK NFFIDLKLPY SVVRNEQVEI KAVVYNYEDM
PIKVRVELME NEQVCSAASQ KRKYRVEVNI DPLSSRAVPF VIIPMEKGEL EIEVKASVFG
VAVYDGVKKK LRVVAEGVQT KKTIKTIELN PSVHGGVQSE KVDKIVLPSL VPKTEPQTFI
SVTGEILTET IESAISGEPL GSLITQPSGC GEQNMIYMTS PVIATHYLDS TQQWEKVGLE
RRAEAINYIN KGYTQQLAYR HPDDSYAAWL SRPSSTWLTA YVAKIFGLAY SLISVDDRVL
CGAIKWLILN KQQPDGIFKE DAPVIHGEMV GDVRGKDADA SLTAFVVIAM QESREICGQQ
IQSMEGSINK AVQFLQRRIR SLTNPYAVAM TSYALALNKQ NTIETLMKFA SADKSHWPVP
GSHLFSLEAS SYALLALLKY KEFDQAGAIV RWLTEQRFYG GGYGSTQATI MVFQAVAEYR
IQVPLFKDID LDVEISLAGR SKPTKWKIVN SNAYVAKSER ARLDQNFTLV ARGKGQGTMS
VMTLYNALPD EKKTPCKTFD LDVKIERAPN ARRPEGALDT FKLTIEITYQ KDTDATMSIL
DVTMLTGFIP DFEDLRKLSN GVDQYIQKFE MDKALSEKGS LIIYLDKVSH KLADRIAFKV
HKMYQVGLIQ PAAVAVYEYY ANENRCVKFY HPEKETGTLS RICQGDVCRC AEESCSKQKS
SKDELDIPVR LTAACDPGVD YVYKVKLVEF VQSSDKYIML IEDVIKEGSD TGVREKMRSF
VSHSTCRETL GFEKNRSYLI MGKSVDLINT NEGFVYFIGS GTWIELWPTD VECQSLIFQT
KCEQIKEVAS ELLNFGCPN
//
