ID A0A075AF72_9TREM Unreviewed; 1813 AA.
AC A0A075AF72;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Activin-binding protein {ECO:0000256|ARBA:ARBA00042260};
GN ORFNames=T265_05535 {ECO:0000313|EMBL:KER27429.1};
OS Opisthorchis viverrini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX NCBI_TaxID=6198 {ECO:0000313|EMBL:KER27429.1, ECO:0000313|Proteomes:UP000054324};
RN [1] {ECO:0000313|EMBL:KER27429.1, ECO:0000313|Proteomes:UP000054324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT "Opisthorchis viverrini - life in the bile duct.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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; KL596723; KER27429.1; -; Genomic_DNA.
DR RefSeq; XP_009168833.1; XM_009170569.1.
DR STRING; 6198.A0A075AF72; -.
DR GeneID; 20319717; -.
DR KEGG; ovi:T265_05535; -.
DR CTD; 20319717; -.
DR OrthoDB; 2878505at2759; -.
DR Proteomes; UP000054324; Unassembled WGS sequence.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00055; EGF_Lam; 2.
DR CDD; cd00104; KAZAL_FS; 5.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 3.30.60.30; -; 6.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR003645; Fol_N.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10913:SF45; AGRIN; 1.
DR PANTHER; PTHR10913; FOLLISTATIN-RELATED; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF07648; Kazal_2; 6.
DR Pfam; PF00053; Laminin_EGF; 2.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00180; EGF_Lam; 2.
DR SMART; SM00274; FOLN; 2.
DR SMART; SM00280; KAZAL; 6.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 6.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01248; EGF_LAM_1; 2.
DR PROSITE; PS50027; EGF_LAM_2; 2.
DR PROSITE; PS51465; KAZAL_2; 6.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000054324};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1813
FT /note="Activin-binding protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001704603"
FT DOMAIN 202..265
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 312..360
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 396..450
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 499..548
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 564..620
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 637..689
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 713..760
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 761..807
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1099..1137
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1141..1368
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1486..1812
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 811..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..850
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 713..725
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 733..742
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 761..773
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 763..780
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 782..791
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1127..1136
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1785..1812
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 1813 AA; 200027 MW; 892242648D9FAAA9 CRC64;
MTTRKRVPTT DNWIIVILLC LTFTSNPTSA CLSKEQFLAS LNRRKTLVFE AILLQTSASY
LNSNGYEAYI QITKIYQQSR LGWQLSPNSI AHVRGIRPRA VDTALCLPRM VNGRTYLWIT
WNTGLNVKTA EGSLEFYPGG LFLPEESKQA ELEAVFKPKP PQGTRVGSPL QSPFEDRLQQ
DAGYGAQALI SSPNADVSQQ QGRNLNPCDP IPCSLELRPV CGTDGVMYQN ECLLRKRSCA
GGSLLPYSPS RPVMVNVDYT NKCLNQYYAR QTRQSYALCD GNNLCNYGAK CPTTNPSNNW
RHVAPAPFNG CDCQHINCLN EWPDPVCGTD GETYSNECYL RKSMCVTQLP KRILYRGNCA
CSMMMDIEIK YRGKCASNPC LSHTCRWPGE RCEIDETGQP KCVCPDSCPK VMLPVCGSDG
LTYDSHCHLE LTACMKMRQL WVVYSGQCSQ EPQCQAIGLH CQGYEVCTRI KAPPVYQIHS
PQYSGSQPSK FQPMVAHCVC PTCPEKGLGD QVCGTDGQTY RSECHLRASV CQRQLYGVKV
RSIGPCDACN NKECKYYAIC QKNADGEPQC ICPTDCPYVQ GGKTVCGSDG NTYEDECVLK
VRSCAEQREI YVIHEGPCKT CPSGCPLGYQ CRNGQCVCRD ACPTTSSLLD AEVCGTDGLL
YRSECELKRQ ACLQGKDISA DPSGASCRKQ LGSHSEDVVA VRPQADEVQV SQCTCNKVGA
LSEFCDHRGR CRCKWYVQGD KCDQCVAGYW GLQNGHECIA CSCHPDGSVS TNCDQTSGQC
DCRPGVVGRQ CSICPDGGYV TKSGCNVENV TSGHRATENP SVKAEAKSKS DNNTSPPDSP
QTNEIITGRQ FSPETTLLIP APKSFEQPIT IELDVVLSGQ DGNLLQYRIA PTEQEQMLVK
NLRDHQFRLG ISGGRVECSY LNGRIPDRLY VVQAPETIRP NTLHQIRVGV INNKPWLQLD
GVQTTLVTEA PILQHPTAEN ITQPVGGYKT IVIGRPLFPA IQRTWPPPSA KENDGFGGCL
LRVNLIAGSN KQPQRIDLLS GAGTELAWIG MKRVSSGLSE APLCSANEEF SSPPAVVHED
DRTKSIQSDG STVEQSQAPA TICTRGQSCQ NGGICVSTRP NEYDCICQPG WQGQRCEQVV
TVIPQFGGNS FIRLPGPKGP QAMNGKKLRI GLTFLATQVP GLLFFLPPKT RMGPFLGVYI
DPNGYVVVAC RTELRALNAK FPDSVGRSSD TVLLQYRIPL QLRRWHMLTI DKRPRAMSLK
IDENQSQRIR LVPAALRRYL KKWRGLSLPS FDLSSSPIYL GGYDFHNSPI PPMDIRTGLV
GAIQQMNING ADIFLVGPPS PNMEVTQNSL SDDSEYWLNV SQWQGPPCGP AYSPCRIGEL
QSVCRPLGTT ASCACSTQSQ LIRFMREHGT NDAKWAENLA CQQKQAEIDA MRENSQKSHD
ETPLKPWSQD DVQYDALPKT VESPGTDTKL RKDALAATPE TRNCAQLAVR FSGNTIFKYF
NLLKTDYYMR LQLQTASQDG LILMIGDTLP ETKRPGYPHS ELYDQRELTM IALRKGRVEF
GIFIVSEITT AASDRRIALI TGRTSTSLLQ IQSKMELNDG KCHTVNVVRS GRRATLIVDH
QMASGEFSIP SQSMHRDNYV LMGAAEEQHS LSIIKWLPVN SLFHLRACIG TTTRATSMVR
DTVRHGPVAP LNGAHASKLL PSLHSSLPNS PHLTVQYLRT NLSATASNAC STLSVPSCHV
SRRKHEGCDN VKLPRPRQKK PRCIGGAMLN ITGIPWEYQH NFTGCIGDMF LNEQKVHMLT
SAFEIRGPIM SCS
//
