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Database: UniProt
Entry: A0A2R9BVQ4_PANPA
LinkDB: A0A2R9BVQ4_PANPA
Original site: A0A2R9BVQ4_PANPA 
ID   A0A2R9BVQ4_PANPA        Unreviewed;       583 AA.
AC   A0A2R9BVQ4;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Complement factor I {ECO:0000313|Ensembl:ENSPPAP00000033541.1};
GN   Name=CFI {ECO:0000313|Ensembl:ENSPPAP00000033541.1};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000033541.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000033541.1, ECO:0000313|Proteomes:UP000240080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22722832; DOI=10.1038/nature11128;
RA   Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA   Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA   Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA   Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA   Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA   Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA   Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA   Paabo S.;
RT   "The bonobo genome compared with the chimpanzee and human genomes.";
RL   Nature 486:527-531(2012).
RN   [2] {ECO:0000313|Ensembl:ENSPPAP00000033541.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR   EMBL; AJFE02105128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02105129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02105130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02105131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003830060.1; XM_003830012.3.
DR   AlphaFoldDB; A0A2R9BVQ4; -.
DR   Ensembl; ENSPPAT00000056417.1; ENSPPAP00000033541.1; ENSPPAG00000039592.1.
DR   GeneID; 100972456; -.
DR   KEGG; pps:100972456; -.
DR   CTD; 3426; -.
DR   GeneTree; ENSGT00930000151042; -.
DR   OMA; YECQQPK; -.
DR   OrthoDB; 4629979at2759; -.
DR   Proteomes; UP000240080; Chromosome 4.
DR   Bgee; ENSPPAG00000039592; Expressed in liver and 6 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: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; 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; 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; 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; 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   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:UP000240080};
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..583
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015337476"
FT   DOMAIN          60..108
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          114..215
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          340..574
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DISULFID        186..196
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        229..247
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        241..256
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        259..271
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        266..284
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        278..293
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   583 AA;  65918 MW;  41446B71DBFADAB4 CRC64;
     MKLLHVFLLF LCFHLRFCKV TYTSQEDLVE KKCLAKKYTH LSCDKVFCQP WQRCIEGTCI
     CKLPYQCPKN GTAVCATNRR SFPTYCQQKS LECLRPGTKF LNNGTCTAEG KFSVSLKHGI
     TDSEGIVEVK LVDQDKTMFI CKSSWSMREA NVACLDLGFQ QGADTQRRFK LSDLSINSTE
     CLHVHCRGLE TSLAECTFTK RRTMGYQDLA DVVCYTQKAD SPMNDFFQCV NGKYISQMKA
     CDGINDCGDQ SDELCCKACQ GKSFHCKSGV CIPSQYQCNG EVDCITGEDE VGCEGFASVA
     QEETEILTAD MDAERRRIKS LLPKLSCGVK NRMHIRRKRI VGGKRAQLGD LPWQVAIKDA
     SGITCGGIYI GGCWILTAAH CLRASKTHRY QIWTRVVDWI HPDRKRIVIE YVDRIIFHEN
     YNAGTYQNDI ALIEMKKDGN KKDCELPRSI PACIPWSPYL FQPNDTCIVS GWGREKDNER
     VFSLQWGEVK LISNCSKFYG NRFYEKEMEC AGTYDGSIDA CKGDSGGPLV CMDANNVTYV
     WGVVSWGENC GKPEFPGVYT KVANYFDWIS YHVGRPFISQ YNV
//
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