ID B0LCZ8_GINCI Unreviewed; 673 AA.
AC B0LCZ8;
DT 18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT 18-MAR-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Complement component factor I {ECO:0000313|EMBL:ABV21978.1};
GN Name=If-2 {ECO:0000313|EMBL:ABV21978.1};
OS Ginglymostoma cirratum (Nurse shark) (Squalus cirratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes;
OC Ginglymostomatidae; Ginglymostoma.
OX NCBI_TaxID=7801 {ECO:0000313|EMBL:ABV21978.1};
RN [1] {ECO:0000313|EMBL:ABV21978.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Liver {ECO:0000313|EMBL:ABV21978.1};
RA Shin D.-H., Webb B., Smith S.L.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABV21978.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Liver {ECO:0000313|EMBL:ABV21978.1};
RX PubMed=19423168; DOI=10.1016/j.molimm.2009.04.002;
RA Shin D.H., Webb B.M., Nakao M., Smith S.L.;
RT "Characterization of shark complement factor I gene(s): genomic analysis of
RT a novel shark-specific sequence.";
RL Mol. Immunol. 46:2299-2308(2009).
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; EF647998; ABV21978.1; -; mRNA.
DR AlphaFoldDB; B0LCZ8; -.
DR MEROPS; S01.199; -.
DR BRENDA; 3.4.21.45; 2434.
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; 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 2: Evidence at transcript level;
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 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..673
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002751863"
FT DOMAIN 144..192
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 190..308
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 431..664
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 30..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 274..284
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 316..328
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 323..341
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 335..350
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 359..377
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 371..386
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 673 AA; 75917 MW; B85B4BDE18E665BC CRC64;
MIFSEALLFL MSLLVTVGQQ QDILTGERAE TAINSRASPP SSDSTEAQYC NHTSPPSSES
TEAQYSSHTD LTPRGSNQTV NNNHTFPQPK ESNETVNNSH TISNSSNVHL QRLAADCRDK
NFTYKSCQKI FCQPWEKCIH GNCVCKLPYQ CPKNGENVCS SNEKKYRTYC QLKSVECSRN
SEKFSHFGAC SLGHAAVSWQ SDHNSQGIVL FSFNQTLQEL SICMNQKNWT MHEANVFCRQ
LKFQLGAEKI LTQTELTNRP MVTNFMNWSN RMRCRGFETS LSECFRLTDI EKLQKKCRKE
KIAAVKCYDY PPDKKCTNEE FTCVNGKCIP LENLCNGIDD CADLSDETCC KSCSNSHHCK
SDICIPYFSR CDGEDDCLDG SDEKNCTETS KPKDHNEERH LLKSSLAKIS CGISNVTGDF
EVHTLKRSKR LVGGEEALQG QFPWQIAVYD GTRLNCGGVF IGGCWILTAA HCLRLYHMSD
YVVRIAKYNK RDVAVNEEIL PVEKIIIHHD YVPKTYQNDI ALIKVVHVFS EKECIPLSHD
VLPVCVPWSE YLFRPKKTCV ISGWGYASGD RVSILRWAEL NIFGNCSEIY KSDFYAGMEC
AGKMDGTVDA CKGDSGGPLV CTDERNEAYV WGLVSWGEEC GKYGRPGVYT KVSHYFEWIS
NHVGRALISK YNV
//
