ID A0A2T7PUE2_POMCA Unreviewed; 1741 AA.
AC A0A2T7PUE2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Activin-binding protein {ECO:0000256|ARBA:ARBA00042260};
GN ORFNames=C0Q70_04038 {ECO:0000313|EMBL:PVD37045.1};
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD37045.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD37045.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD37045.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD37045.1};
RA Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA Zhang G., Qian W., Fan W.;
RT "The genome of golden apple snail Pomacea canaliculata provides insight
RT into stress tolerance and invasive adaptation.";
RL Submitted (APR-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PVD37045.1}.
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DR EMBL; PZQS01000002; PVD37045.1; -; Genomic_DNA.
DR STRING; 400727.A0A2T7PUE2; -.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg2.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00055; EGF_Lam; 2.
DR CDD; cd00104; KAZAL_FS; 7.
DR CDD; cd00110; LamG; 3.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 3.30.60.30; -; 9.
DR Gene3D; 2.10.25.10; Laminin; 6.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
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; 2.
DR Pfam; PF07648; Kazal_2; 9.
DR Pfam; PF00053; Laminin_EGF; 2.
DR Pfam; PF00054; Laminin_G_1; 2.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00180; EGF_Lam; 2.
DR SMART; SM00274; FOLN; 8.
DR SMART; SM00280; KAZAL; 9.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 9.
DR PROSITE; PS00022; EGF_1; 4.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 1.
DR PROSITE; PS51465; KAZAL_2; 9.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
PE 4: Predicted;
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
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:UP000245119};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1741
FT /note="Activin-binding protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015500260"
FT DOMAIN 82..134
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 154..213
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 229..283
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 294..357
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 382..428
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 443..497
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 515..562
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 605..663
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 738..790
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 860..917
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 1027..1064
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1069..1253
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1254..1291
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1293..1331
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1338..1518
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1514..1550
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1559..1740
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 926..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..969
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 738..750
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 740..757
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 759..768
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1054..1063
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1281..1290
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1302..1319
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1321..1330
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1540..1549
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1741 AA; 189575 MW; DFE2D6AAB065DCED CRC64;
MAVGVTVERR GGGAAFSALL LTSCLAFNKF LPLTCSEQSV RCVISREISR APHSQAGIKD
RVAVRSVLLC FRGGVYGQLE QQHAVLSCQH RCQPVFAPVC GSDNVTYASE CLLQKAACVH
QKRIKVKQPG VCGKRDPCEG KVCNYGAKCQ PSVDGKTARC QCPSECYRYG DNLGSKPVCG
SDGMDYNNIC ELHKAACNKL QDIRVKYYGK CDPCAGVKCN SPEICQVDEQ RKPVCRCKFL
CFKELDPVCG TDGKTYSNTC YMHKEACKLH KQISVLYKGE CSAANNPCNK VQCGPMEECS
VDRNGMASCV CPLHCEPVIR YVCGNNSRTY DSDCELRKQA CLLKEYVAVA HTGQCGQDIP
CKGHTCTRGM VCQVIDGQPT CVCPQCSEQY NPVCGDDGIT YENECKLQQE NCETGKAVQV
KQRGLCNGCG DHRCEFYAIC ESIGNQPRCV CPSSCVQVDL PVCGSDGRTY SNECLMRVES
CHRRQLITIK SRGSCDVCAD VVCEHGSRCE NGVCVCPIIC PTAGEAVCGT DGRTYVNRCE
LWKISCTQHI DIEVAKAGEC EGDIDQSGSG EGSGFIVDDE DCDEETCSKY GGRCVVQING
NFHCVCSLGC EAIRSPVCGS NGQSYGNECQ MRQAACMLRQ TITAVSMENC GDSEFDSDEP
CDGAIPLVDE ATGHDYDCSS GMDMCPSGSY CHITPNFAKC CKEDVHLSMQ CSDTPFGCCK
DGFMPAKGPN NAGCPESCHC NSLGSYGTTC DPVTRQCVCK SGVGGLRCDR CEIGFWGMQK
IAEGNSGCIP CNCNPLGSER DDCAQMNGRC MCKANISGMK CDQCNNGNVL GPLGCLGPSS
SPMHSCDDLN CKYGATCHMK NGVPECTCDF QCDNSEKSRD IVCGTDNQNY GSECELKLLG
CRLGLEIDVA YRGPCRALPA TRTTTALPST SRSRKTTRHI TGETSESDNY SSGTRRPEHE
AEKPSEEKCS GSYIDGLCLS DDNCCSNNSH CRLGLCRCLP GFVASVDNRR CIELKREEPS
IITLAPEKDV CADNPCYANG KCELDEILGY RCVCPLERSG PLCNRQSEFK VPSFSGRSYI
QLPHIQKASR DLSIEVVFQT LNTDGIILFN AQNPDGTGDF VSLTVNGGFV EFRFDLGAGE
AILRSRNPVE PGRSHRVIAR RIQASGYLIV DSDPDVTGNS PITHVSLNLN DPLYLGFVPK
VSQEVYNRIG VTLGLVGCIH SLRAGSRDEM IPFNLELNSP ESDILSGADV SECGSNPCKS
MPCKNGGTCL VLDAEMFDCK CQTGYRGVLC DDLVDSCASQ PCQHGGTCTK IRSPDGFECK
CTEGREGARC EKESMPQVFV PKFTGSSYME IPLLDKVEDS LSIEIWFRPL QPNGVLFFAS
QLPGGVGDFI SLNLVQKKLQ YKYYLGGGVG ILESKKTVQL DTFHKVLVSR EGQDGMMIVN
DQPAVKGQAQ GILTQLNLAQ SLFIGGFDNI RNTPAESGIE TGFTGAIQRV IINGKTVDNL
MASARKMSNI TSYNGPPCNI NPCMNNGICI PILNKAECHC PYNFMGQHCE KRADHIDKDQ
PVKFEGNTFL NYPNEVQRRQ PAQRSNEVYV RFKTTSDNGM ILFQHKGNTV RGDYLALAVI
RGQVEFSYNL GKQTENNLHI LRSTVDVADG QWHTATATRD LRDGMLKVDM EPEVRLSSAE
GSSQLDTDGT LWVGGKASMP LGFPQEYYDG FQGCIEEIKV NGQQLHLVDH RNGHGTIAFC
S
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