ID A0A195B0F6_9HYME Unreviewed; 1153 AA.
AC A0A195B0F6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 7 {ECO:0000313|EMBL:KYM77684.1};
GN ORFNames=ALC53_11694 {ECO:0000313|EMBL:KYM77684.1};
OS Atta colombica.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=520822 {ECO:0000313|EMBL:KYM77684.1, ECO:0000313|Proteomes:UP000078540};
RN [1] {ECO:0000313|EMBL:KYM77684.1, ECO:0000313|Proteomes:UP000078540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Treedump-2 {ECO:0000313|EMBL:KYM77684.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYM77684.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Atta colombica WGS genome.";
RL Submitted (SEP-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 -!- 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; KQ976692; KYM77684.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A195B0F6; -.
DR STRING; 520822.A0A195B0F6; -.
DR Proteomes; UP000078540; 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; 2.
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; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF200; ADAM METALLOPEPTIDASE WITH THROMBOSPONDIN TYPE 1 MOTIF B, ISOFORM B; 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; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 3.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 2.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 2.
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:KYM77684.1};
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:UP000078540};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1153
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008269202"
FT DOMAIN 255..467
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 403
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 258
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 258
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 351
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 402
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 406
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 412
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 462
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 465
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 465
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 362..368
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 380..462
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 420..446
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 491..514
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 501..520
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 509..539
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 533..544
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 567..604
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 571..609
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 582..594
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1153 AA; 129951 MW; 996CAA377F918C94 CRC64;
MIIFLVLLTL FVATIDGGLL EKYTNAPGNV YHGRFTRDIH GPELLIPKRV LADGSFSTYF
LPNFYNRREI SERGKRSLGS ADKLHLVLPF NQIDHHVELS PYHEFISPDM VVETRGAGIS
TNLNEGLKFK KASDRQCHYR GIVRGHANSR AALSLCDGVV GYVQTNHGRY FIEPVYQAEP
EPDGQHIHVA YKRDAPHEKK GQTDTVSKRH CGTSDNWESA WAEQLAKRQM QLMENNSLGE
KHNITVSTGT HSIHRYIEIG LIADRRFLDF HNNTDYEQYL LTIMNMVSDF YHDRSVGNQI
DVVLVRVIYL EKEKEEIDLL ISPAAEKTLE SFAKWAEKMN PKDDTHPNHY DIAVLVTRYD
ICSEETNCDL MGLAHMAAAC DPTQAACINE DSGLLLGIVI AHEVGHVMGC SHDEPEISGC
QSKDMDDSYF IMSPIVFLYT IRWSSCSRKF ITAFLESGLG ECLNDNPRTP PEKLKYPNML
PGAMYDAAFQ CNMQFPGSKV CPQPQVNSCE NLWCLTNTSC YSQGSPKADG TKCGENKWCI
HKKCVDMGTR PAAVHGGWGE WGPMGSCSRT CGGGLKYSER ECDRPEPANR GRYCIGERRR
LFTCNTTPCD PTKPPYRAVQ CSEHDNEEIL TDGLHQWKPY MDPKLEPCAL YCINEKQTYV
KISPTANDST PCKAGTNYMC ISGTCRRVGC DWVIDSYAIE DKCGICKGDG TKCSPVVGEF
TETALRSAYV KIVTIPKGAR SVQVSERKPS QNILAVKLEK DKTYCINGDN REFKSGDYEC
AGTMIIYTHP EPDKEVVEMK GPISEDIEIQ YAFFNPRDNP GINYRYYVSS TNTSYTPKYM
WDFIEWSQCS AKCDGGTMIS EASCIEEQGG RVTPNFCDGI PRPEAKSRIC NQVPCPAKWR
VSQWSKCNAC DGKKGMKHRK VQCVRPGARP GEDDVQANLD ACKGRVPRQK EECIGTRPCR
IMCSKKTRRS DEQELIDEKE KESLSLDDQR RMIDRFVDLG LARYLEKSRD KLRDDDRLED
RSAARNFRQE VYDWAMTNED KHKRTCDTEE KFTTPKPGSI ILDSVPIENV VLIQAPYMDE
SLQANLSDKA FQEAGDLVGV GIDTSKKKVY KGAEALKLIQ QLSHRNQTAS PPAVIANKAL
NSSQFVDNAE KKR
//
