ID A0A3Q3A2P0_KRYMA Unreviewed; 646 AA.
AC A0A3Q3A2P0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Complement factor I {ECO:0000313|Ensembl:ENSKMAP00000010055.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000010055.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000010055.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; A0A3Q3A2P0; -.
DR STRING; 37003.ENSKMAP00000010055; -.
DR Ensembl; ENSKMAT00000010217.1; ENSKMAP00000010055.1; ENSKMAG00000007558.1.
DR GeneTree; ENSGT00930000151042; -.
DR OMA; YECQQPK; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR023415; LDLR_class-A_CS.
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; PF00057; Ldl_recept_a; 2.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00057; FIMAC; 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; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 2.
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:UP000264800};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..646
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018536046"
FT DOMAIN 102..149
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 155..277
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 404..637
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 18..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 236..246
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 276..294
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 288..303
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 306..318
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 313..331
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 646 AA; 71703 MW; A47CC10329DE3BE0 CRC64;
MRPESLFLLF LLILHSETDS PPEQDRPSSL TEQTRKVQKR PPLPSLPPTT PATSAQVIPK
QEADEFLASH ECLDKKNQRL TRASCSLVFC PPWERCIDGQ CSCKPPYLCP FEDMKPICGT
NHRNYRSYCQ AMAVSCRNKN PLFSHFGENC KDNIPKFKSS VDTDTGMIRI FLPDGAGGGE
NLLVCQEMWD TAAANVACME QKHPLGAVSA DAVDYNTLTA DRDNPDLPSS CVSIRCQGYE
TSLAECEIFN KVKTVGRKVA AATCYKEAPE ECEFTCANQK CISRNQTCDG VDDCGDRSDE
MCCKKCRNGA FLCRTGVCVH KEAVGDGHID CLDGADESPK HTTALSSDNM NLTQTPLEYV
SRRNETRTNR KVLEAQLQCG IPNKDLVDDV DVVERGRSSR RKRVVGGIPA LPTQIQWQIA
LEENKRIDCG GAYIGGCWVL TAAHCVRPNP SAFRIKFSLW KKFRAQGTTD IVPVEDIQIH
PNYIPTTYEN DIALIKLQKL PFTDKCFEDN PAIRAVCVPW TTHLFQPNHT CSISGWGRTA
DGRSAQVLLW ANVSLIEGCE SSYKDRFKPG MMCAGDLEGS VDSCQGDSGG PLVCEDELGV
SYLWGIVSWG ERCGQPGFPG VYTQVAHYFE WIRLHTGWPA VTRFNS
//
