ID A0A0A0AUN3_CHAVO Unreviewed; 1195 AA.
AC A0A0A0AUN3;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 22-FEB-2023, entry version 37.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 18 {ECO:0000313|EMBL:KGL97572.1};
DE Flags: Fragment;
GN ORFNames=N301_11772 {ECO:0000313|EMBL:KGL97572.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL97572.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL97572.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL97572.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) 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 -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR EMBL; KL872993; KGL97572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0AUN3; -.
DR STRING; 50402.A0A0A0AUN3; -.
DR MEROPS; M12.028; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
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; 6.
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; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF167; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 18; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF08686; PLAC; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 4.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 6.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 6.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 6.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Integrin {ECO:0000313|EMBL:KGL97572.1};
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:UP000053858};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..1195
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012226843"
FT DOMAIN 264..469
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1158..1195
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT ACT_SITE 408
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 355
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 407
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 411
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 417
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 464
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 467
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 467
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 340..391
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 366..373
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 385..464
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 424..448
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 492..517
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 503..524
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 512..543
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 537..548
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 572..609
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 576..614
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 587..599
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL97572.1"
FT NON_TER 1195
FT /evidence="ECO:0000313|EMBL:KGL97572.1"
SQ SEQUENCE 1195 AA; 133667 MW; 3836E8E8537BE441 CRC64;
LQTLQLCCLC CMSHAATLTS DSISELNHDY VFVTPVKVDS SGSYISHDVL HSTRRKRSTQ
SSKSSLHYKF SAFGQELHLE LKPSTILSNS FIVQVLGKDG VSNSQEHEIE QCFYQGFIRN
DSTSSVAIST CVGLSGLIRT RKIEFLISPL PQQLAQEHNY TSPAGHHPHV LYKRTAEEKV
HRYTVESNPK YFSFGHHRIH TSHKYHAQAN GYHHGRFQKQ HFCGRRKKYA PKPPTEETYI
RSDEYGTSAR FKRSSAKIQK NGSLNVETLV VADKKMLEKH GKENVTTYIL TVMNMVSSLF
KDGTIGSDIN IIVVSLLLLE QEPGGLLINH HADQSLNSFC QWQSALVGKN GKRHDHAILL
TGFDICSWKN EPCDTLGFAP ISGMCSKYRS CTINEDTGLG LAFTIAHESG HNFGMIHDGE
GNPCRKAEGN IMSPTLTGNN GVFSWSVCSR QYLNKFLSTA QAACLIDEPK QTGQYKYPDK
LPGQIYDADT QCKWQFGMKA KLCNLSFVKD ICKSLWCHKV GHRCETKFMP AAEGTACGIS
MWCRRGQCVK YGDHGPKPVN GQWSAWSEWS ECTRTCGGGV TYQERHCNNP KPQYGGKFCQ
GSSRIYQLCN NQPCPANSLD FRAQQCAEYN SKPFRGWYYK WKPYTKVEEE DRCKLYCTAE
DFDFFFAMSS KVKDGTLCSP NKYDVCIDGI CEQVGCDHGL GSKAVLDACG VCKGDNSTCK
FFKGQYLIQH KANDYYAVVT VPAGARSIQL QELQISTSYL AVRNLSKKYY LTGDWTIDWP
GKFSFAGTVF DYQRSFNHPE SLYAAGPTNE TLVFEILLQG KNPGIAWEYT FSKTNNENKT
SVKKHSYSWV TVQSECSATC GGGHITAKAI CLEDHRTRVN SSFCGPRMKP LTETKLCNTN
PCPAYWSTGE WSACSKSCGG GQQSRLIQCV QKKTFQREEV VAHSLCPVST PTQVQMCNSQ
DCPPEWSPGL WSQCSKTCGR GVKKRDVYCK STGSPKVKIL PESMCSGDHK PESQQTCVLG
RCPKNDRLQW VISSWSECSA SCGPGVQKRE LKCGEKSIHG KLITFPQRRC RNIKKPNTDL
EEACNKGACP SQMLYNMVSG WYSSPWQQCT VTCGGGVQTR SVQCLRQGRP AAGCLPHQKP
AVLRACNTNF CPVPMKRDDP SCVDFFTWCH LVPQHGVCNH KFYGKQCCKS CTKKN
//
