ID F1KUR2_ASCSU Unreviewed; 864 AA.
AC F1KUR2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Zonadhesin {ECO:0000313|EMBL:ADY41616.1};
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY41616.1};
RN [1] {ECO:0000313|EMBL:ADY41616.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21685128; DOI=10.1101/gr.121426.111;
RA Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA Davis R.E.;
RT "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT functional diversification, and novel developmental profiles.";
RL Genome Res. 21:1462-1477(2011).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; JI166212; ADY41616.1; -; mRNA.
DR AlphaFoldDB; F1KUR2; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd19941; TIL; 1.
DR Gene3D; 3.90.215.10; Gamma Fibrinogen, chain A, domain 1; 1.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR036084; Ser_inhib-like_sf.
DR InterPro; IPR002919; TIL_dom.
DR InterPro; IPR014853; VWF/SSPO/ZAN-like_Cys-rich_dom.
DR InterPro; IPR001846; VWF_type-D.
DR NCBIfam; NF040941; GGGWT_bact; 1.
DR PANTHER; PTHR46160; ALPHA-TECTORIN-RELATED; 1.
DR PANTHER; PTHR46160:SF5; PROTEIN CBG11501; 1.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR Pfam; PF01826; TIL; 1.
DR Pfam; PF00094; VWD; 1.
DR SMART; SM00832; C8; 1.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00186; FBG; 1.
DR SMART; SM00216; VWD; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR SUPFAM; SSF57567; Serine protease inhibitors; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR PROSITE; PS51233; VWFD; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..864
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003265187"
FT DOMAIN 67..104
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 148..351
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 528..574
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 575..615
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 614..821
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT DISULFID 94..103
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 605..614
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 864 AA; 96816 MW; BD1C828E82DF6C46 CRC64;
MCIHFAMFLL IVQLLCCIIY VSAWQETNRD EFCDGSTLDC RSHREISHMI NELRKENQNL
REAVNPNCTV CWSAPCLNGG SCVPIDYSKY RCECPGDYGG SDCQTHIECS SKSCGKNTEC
YVANHQINCV CKVGYSGNPK YGCNMRTVEA CMSGDPHYTT FDGQVYEYQG TCPYVFTQPC
NGTFAPPYAY FSVKAKNELS YKMAHVSTVS EVEVLMYEQT LHVDSKYNLY VNGVRTLMPF
YYPSKANQKI AVTYGSSKVT IKNDQFVKVT FGQGRLCVEI PDVPMLQGED VLCGLAGNRD
SNCKDDFRNR YGFVYTNVTR CSNRNKLFTE VFGDTWITKD FLPLQTDTAC LTGEEVFNDT
LNCDLLTVKK ECGHILDAAL GKGPFAACKD LGNDTIENAY ENCVFDVCSS SEQFCKSMTT
FAKICQITLP NTPLEWRGPL NCPELHCPLH SKPSPCATGC PNTCTDPDYS ESCLEGCAEG
CECEAGYVLD TNDPTDAKCI LLEQCGCVDP NGNPHRPDDR WLTENCTRLN YCSNGTYHYR
YQPCSSNAYC GVDETHSYKC FCNKGFVGDG YNCTDINECL DETKCNADKG KGKCINTPGS
YECDCNGYYG GEECAFYLPK RHCADLYVYH HNTTNGAYII KPPYPYSDKQ AFTELTVYCD
MTTSGGGWTL MTNSLSNSMS NKTFKDYVDG FGNPSIMDVW IGLDVLHGMT NEVETSLRVD
LHRCKYNSRP EISTNCTYPY FKVLDARNVY AVVIPIECSG TENIYFDGWA RWDLSAVGPT
FLAYDTDTST AHCSATYKNT GWWFDTKQRC GSANLNGVRY QCSDQPPVDL LAHYLQWNGN
PLSAAQLFLR PTLYPDYDPH VEKA
//
