ID A0A091P3G4_HALAL Unreviewed; 554 AA.
AC A0A091P3G4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Complement factor I {ECO:0000313|EMBL:KFQ02532.1};
DE Flags: Fragment;
GN ORFNames=N329_05610 {ECO:0000313|EMBL:KFQ02532.1};
OS Haliaeetus albicilla (White-tailed sea-eagle) (Falco albicilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC Accipitrinae; Haliaeetus.
OX NCBI_TaxID=8969 {ECO:0000313|EMBL:KFQ02532.1, ECO:0000313|Proteomes:UP000054379};
RN [1] {ECO:0000313|EMBL:KFQ02532.1, ECO:0000313|Proteomes:UP000054379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N329 {ECO:0000313|EMBL:KFQ02532.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK652329; KFQ02532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091P3G4; -.
DR Proteomes; UP000054379; Unassembled WGS sequence.
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:0045087; P:innate immune response; IEA:UniProtKB-KW.
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; 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; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF7; HYALIN; 1.
DR Pfam; PF21286; CFAI_FIMAC_N; 1.
DR Pfam; PF21287; CFAI_KAZAL; 1.
DR Pfam; PF00057; Ldl_recept_a; 2.
DR Pfam; PF00530; SRCR; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00057; FIMAC; 1.
DR SMART; SM00192; LDLa; 2.
DR SMART; SM00202; SR; 1.
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; 2.
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 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:UP000054379};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 29..77
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 81..196
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 312..545
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 153..163
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 188..200
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 195..213
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 207..222
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 225..237
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 232..250
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ02532.1"
FT NON_TER 554
FT /evidence="ECO:0000313|EMBL:KFQ02532.1"
SQ SEQUENCE 554 AA; 62473 MW; F0016D8893C28C82 CRC64;
ECLINQYTHK SCEKVFCHPW ERCVEGKCLC KLPYQCPKNG SSVCSTNGRY FPTYCHLKSY
ECQQPKAKFL HKGKCMSEET FSISVGHGDS NLLRVKPMNQ KNYIFVCDGE WTMNEANVAC
KHLGFESGAE YYQTNSSITE SASNSLHCVQ ITCRGLETSL AECHIEMKSR DSNEGFVSLQ
CHENLRACSD GEFRCVNKKC ISLNKTCDGI NDCGDLSDEL CCRECRDNSF HCRSNICIPN
KNVCNKEVDC LTGEDEARIL CAGKGTDKGA EKHSMDEDTF FLFVKERKMI KTLLRQVHCG
LTNHTLTRRK RIVGGEIARK GEFPWQVAIK ETGSEGATVY CGGVYIGGCW VLTAAHCVRA
NRVHLYRVWV GLLHTILYDQ ETDTFSLNRL IIHENYNAST YENDIALLEL KGFGKGECSL
QQITPACIPW SEYMFKAGDR CKVSGWGLEK GYTKQYILKW GNVNLFQNCS EMYPGRFFKQ
MACTYDGSID SCKGDSGGPL VCFDAENVAY VWGIVSWGEN CGEAGHPGVY TKVASYYDWI
SHHVTRSLIA RYNI
//