ID A0A3P8XJE0_ESOLU Unreviewed; 615 AA.
AC A0A3P8XJE0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Complement factor I-like {ECO:0000313|Ensembl:ENSELUP00000003764.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000003764.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000003764.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000003764.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR AlphaFoldDB; A0A3P8XJE0; -.
DR Ensembl; ENSELUT00000013476.2; ENSELUP00000003764.2; ENSELUG00000004967.2.
DR GeneTree; ENSGT00930000151042; -.
DR Proteomes; UP000265140; LG24.
DR Bgee; ENSELUG00000004967; Expressed in liver and 11 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00104; KAZAL_FS; 1.
DR CDD; cd00112; LDLa; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 3.30.60.30; -; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR048722; CFAI_FIMAC_N.
DR InterPro; IPR048719; CFAI_KAZAL.
DR InterPro; IPR003884; FacI_MAC.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24264:SF40; HYALURONAN-BINDING PROTEIN 2; 1.
DR PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR Pfam; PF21286; CFAI_FIMAC_N; 1.
DR Pfam; PF21287; CFAI_KAZAL; 1.
DR Pfam; PF00530; SRCR; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00057; FIMAC; 1.
DR SMART; SM00280; KAZAL; 1.
DR SMART; SM00192; LDLa; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 2.
DR SUPFAM; SSF56487; SRCR-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50287; SRCR_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Digestion {ECO:0000256|ARBA:ARBA00022757};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..615
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028258186"
FT DOMAIN 84..133
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 138..252
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 372..606
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 212..222
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 255..273
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 267..282
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 615 AA; 68204 MW; 8F46FD52A5C1FE4F CRC64;
MEKTAFKLLL LGVLYISHVA MGAPGNVKFP KKPPSHLQTT TTPAPPMTDA FLGPAECLDQ
NYTRLSCNRV FCPPWMRCLE GRCVCKLPYL CPKDEKMLPV CGNDGRTYYS YCMAMAVSCR
SGRPIMSHFE GEGCSKDSEK VESSIDDQTG VVSLKIPGKG TLLVCGEAGW NMAAANVLCR
NKNHLLGAVE ASSVDYTDKE TTGADHCVNV RCQGYENSLA ECSFSDRTSR GRGDKIATVT
CFQEPKEGSK CEFRCVNRKC VLLEQTCDGV DHCGDRSDEM CCTACRGDSA FWCKSGVCVS
REAVRDGIRD CLGGEDEMKT HPVQPVSGHS EFRSPLNELK ASRDILEGKI HCGIPKATAT
EEIREGRRQK RVVGGLEAKP TQIQWQVAIR ERGLSNDCGG AYIGGCWVLT AAHCVRPEPK
AYIIMFSLWK KKFLQATTDI VPVKNIIIHH KFNANTYEND IALIEMKKLP FREDCFLPNP
AVSAVCVPWS LQQFNPNHTC SISGWGRMRD GYSANVLMWA NVSLIDNCQQ YYRERFKDGM
MCAGDLEGHV DSCQGDSGGP LVCQDSLGIS YLWGIIGWRE KCGQANYPGV YTQVAHYFEW
IRGHTTWSAV TKYNV
//
