ID A0A0V1KZN4_9BILA Unreviewed; 2156 AA.
AC A0A0V1KZN4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs gon-1 {ECO:0000313|EMBL:KRZ52492.1};
GN Name=gon-1 {ECO:0000313|EMBL:KRZ52492.1};
GN ORFNames=T02_3442 {ECO:0000313|EMBL:KRZ52492.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ52492.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ52492.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ52492.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR613273-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR613273-2};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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:KRZ52492.1}.
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DR EMBL; JYDW01000191; KRZ52492.1; -; Genomic_DNA.
DR STRING; 6335.A0A0V1KZN4; -.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 3.40.1620.60; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 13.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR012314; Pept_M12B_GON-ADAMTSs.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR PANTHER; PTHR13723:SF281; NO LONG NERVE CORD, ISOFORM C; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF08685; GON; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 14.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 15.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 14.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS51046; GON; 1.
DR PROSITE; PS50092; TSP1; 14.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR613273-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}.
FT SIGNAL 1..43
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 44..2156
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039952417"
FT DOMAIN 298..509
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1941..2140
FT /note="GON"
FT /evidence="ECO:0000259|PROSITE:PS51046"
FT REGION 222..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 443
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 442
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 452
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 504
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 507
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 507
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 373..426
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 402..408
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 420..504
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 458..488
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 534..556
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 545..568
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 551..587
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 581..592
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 616..653
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 620..658
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 631..643
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 2156 AA; 243099 MW; 49111147FE86BB16 CRC64;
MQAVRCCCCC CCCCCYCCCC CGRLLASALF LLPLLLLFFS VSADSQKLSP TSNSPSRIVV
FPRLLSSQWS ARSRIKRGAG ATPDSCLYAL DNFGAPLLFN VTRQDNLVGN LLAPNFIVQH
LSANYTWADE LDHTLHNCLY NGDVLVDEKP IRGAVRLLNL CQGMYGTVEL NDGTYFIEPL
NTANNENGSS STATITPTAS LLLHSRPHLL YKSAPANFND QYPEENWSDS KQRKYNSTDK
INNNNNSTHD VTNTAKKNTT SQAENCSEKL SQHLNCPFST CEKKNSSARY KRSYSREYFV
ELLVVADARM RLYHRHNLEN YILTLISLVA TVYRHPSLEA SLSINLVRLL IVDFENAGPR
VSDNAQETLR EFCRWQQTMN DPDDDSLNHH DVAVLLTRHD ICRMPGKCDT LGLAELGTMC
DPYRSCAIIE DNGLSAAFTI AHELGHIFNV PHDDEKKCAQ FMTLNKENYH IMAPTLEFNT
HPWSWSPCST ALLNKFLESG QVHCMLDKPV QQKYTERLTT NPAPGLTFDA DQQCRFVFGP
TSNLCPYMPT CKRLWCTTVY GFGHSVGCRT QHMPWADGTP CGHERWCYRG DCVGIAPEHM
TAVDGAWGEW KAWSECSRTC GGGIKRARRE CDSPRPANGG KYCVGERVRF RSCNTQECPI
DSPDFREVQC SEFNGKPVGI YGLSSDVKWV PKYNGIVATD RCKLYCRVFS SAAFYLLKDK
VVDGTPCGRY TDDICVDGIC RKAGCDNRLG SQLKRDDCGV CGGDGTTCRK VSGVYNEVPQ
YGYNFVMKIP IGASNIDIRQ VAWNGKMEDD NYLALRNSKG DYLLNGQFQV SVYFKEIQVQ
GTVIEYSGSD SPVERINTSR PIMEELFLHV LSVGNLHSPD IRYNYSIPNN AGNVQTVSNF
LWRMTDEWTD CSSECHGEQD LKIVCSSVHN EEQIVDDRYC ERMKKPYRVM RVCNLHCQIS
WEQEPLSDCS AVCGEGEQVM RVLCVRKMSD QTVYPVDNSL CRDLEKPSDR RPCYKDCAGR
RWTHSDWQPV KDSNNNVIDD RYCENVINDI TEQPCNMEPC PNWSYGDWMQ CSASCDGGIQ
SRHAVCLDAS GREVDSILCD HSEKLVIQKC NEHTCTHWKF GPWSECSKTC GDGIAVRAAW
CVDSKGVTLD ELKCPKEQKI ISKSCQHLTA CPKWKLSEWS PCSRTCMDGW RTRRVHCVDG
NDQPLDSKYC ADPHQSHPPT HQPCNLGQCP FWRRQQWGPC SVTCGVGVQQ RAVECVYKDE
VVDTGYCRDI AQPDRHRSCE LIPCPEWEVS PWEQCSVTCG TGYQQRSVQC IYQENRMPAE
SGACVESKRP KVIRTCTKAP CPDKGYDSKA SSSRQHPANV LTSNQIFRTT IFTQVSDGQS
PTKWETGSWT DVNPGYFFLF ICSFKYANAY SLQCSAICGL GRRSRLVACR DMFGRFLPDQ
YCNHLQPPAR EEACESTAHC GNWKTGPWQS CSELCGVNVK TYRQVVCVSP QTDDHLEEAD
CDVRKKPSNE RSCNLPPCGQ SSPSEIDNEK YEWRVGDWSE CSRSCGGGQQ QRLVQCVQSI
ILSEPVENSA SCSNSNRPNS IRLCNTQACT TSRGKWRPLQ WSACSSTCGR GYRRRQVHCV
DADTLQLLDD NHCDPLDKPL PVHRCRMRAC PRWRTSKWSP NSGSQTFLGC DPLLKTTLNE
ESSDKLINSP SAFVDMAART TSACSERADR NSNDSQCSVT CGEGVRTRKL NCVVGRHHLL
PDTDCQASLK PDTVAKCFLK ECPKYRWLVS DWSKCTKFCG EENRVREVYC VNNYNQRAPP
ALCDESNKPP AVQLCLNDLC PYTWVPGPWS TCSKTCGHGE EFRLLFCVKK GSDAGGAEVP
AHLCKALPEP ITKRQCFHGP CDSKYFWHPE PWTACSVHCG WGIQERRLKC VDRNGLKMAK
EYCSLELRPK KRRRCFVKNC EPRDCDEVRE TRNATTDGHY HVWVYGNKVK VYCYGMASLH
PKEYLTVNPE TNFAEFYDKR LLYPFTCPYN GMRNDSCQCA DELTPNPGMT RFHKIQVDLH
NMRVKLDDKL FSTTERGGFV PYATAGDCYS AVNCPQGRFS IDLRGTGFRV SPKTAWMHEG
HRAFSEVKRN TNSVLVIGSC GGYCGKCAPH KRIGLLIETL VESSSVNKIN NKSDTD
//
