ID A0A093QX12_PYGAD Unreviewed; 1567 AA.
AC A0A093QX12;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 37.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 12 {ECO:0000313|EMBL:KFW63264.1};
DE Flags: Fragment;
GN ORFNames=AS28_06711 {ECO:0000313|EMBL:KFW63264.1};
OS Pygoscelis adeliae (Adelie penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW63264.1, ECO:0000313|Proteomes:UP000054081};
RN [1] {ECO:0000313|EMBL:KFW63264.1, ECO:0000313|Proteomes:UP000054081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW63264.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-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; KL224756; KFW63264.1; -; Genomic_DNA.
DR STRING; 9238.A0A093QX12; -.
DR MEROPS; M12.237; -.
DR Proteomes; UP000054081; 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; 8.
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:SF189; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 12; 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; 7.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 8.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 8.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 7.
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:KFW63264.1};
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:UP000054081};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2}.
FT DOMAIN 214..424
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1516..1556
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 986..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1035
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 361
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
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 308
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 360
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 364
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 370
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 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 422
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 422
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 290..344
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 319..326
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 338..419
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 377..403
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 446..469
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 457..475
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 464..494
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 488..499
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 522..559
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 526..564
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 537..549
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW63264.1"
FT NON_TER 1567
FT /evidence="ECO:0000313|EMBL:KFW63264.1"
SQ SEQUENCE 1567 AA; 175762 MW; A9FD43B9534B7BBE CRC64;
EQFIKTLPEY HVADPARVDA SGHFLSFNLH HHISNTRKKR DLSKKENVVY YKINHEEKDL
FFNLTVHMGF LSHNYVVERR RGNHTSAKIA TRSGVPCHFI GTVLQPGSGS GTAAISTCNG
LTGYFHLPHG DYFIEPIKKH PQKEGTPHPH IIYGANVLQN ALRRRRAIPM EKEQACGLND
TLSFFKQQLH WRERWEQNHM AVRKVSRRSV SKERWVETLV VADSKMVEYH GSDHVESYIL
TIMNMVTGLF HDPSIGNAIH IVLVRLILFE EEEQGLKIVH HADKTLASFC KWQKSVNPKS
DVNPTHHDVA VLLTRKDICA GMNRPCETLG LSHLSGMCQP HRSCNINEDS GLPLAFTIAH
ELGHSFGIQH DGKENDCEPV GKRPYIMSRQ LQYDPTPLTW SQCSKEYITR FLDRGWGFCL
DDIPQKEVLK SPIIAPGVIY DVHHQCQLQY GSNATFCEDV DNLCQTLWCS VKGSCRSKLD
AAADGTRCGE NKWCFSGECI TVGKTPEAIH GGWGIWSSWS HCTRTCGAGV QSAERPCDNP
EPQFGGDYCT GERKRYRMCN ISPCRKGLPT FRQMQCSEFD TVPYQNEFYH WVPVYNTANP
CELHCRPIDG HFSEKMLDAV TDGTPCFEGR HSRDICINGM CKAVGCDYEI NSNATEDQCG
VCLGDGSDCR TVKMMFNQSE GFGYVDIGLI PKGARGIKVM EVAEAGNFLA VRSKDPEKYY
LNGGFIIQWN GEYKVAGTVF QYDRTGDLEN LTAPGPTNES IWIQLLFQET NPGIKYEYTV
RKEESHENEI GESEYFWQYG DWTACSVTCG RGVRRQIAHC MRKGSGAIKN SFCDPATQPN
GRQKKCYEKD CPPRWWAGEW QKCSTTCGPT GQKKRTVLCI QTVGSDEQAL AVTECQHLLK
PKTQLSCNRD VLCPSDWTVS NWTECTVTCG GGIRTRNVTC AKNNDEPCDT SKRPNSKALC
GLQQCPSAGR FLIPPLAPRR GKIIIRKTST NPEWSPPRRI PIPNPRSHTT TKTPKPESVT
PCLPTSSGLG TVSEKEGTAN KTLQNIFSGP SDVYNYPVVS TENSSHQNTT SWPFHNNLST
EIIRHAENIS EREAVSTVES EVLRSEDTPV SSFTSSPEIT SSYDYLTEES DDIDGSVGGS
EKPTDLLYST ELNPEIRTRS TTLDTGSPVL QNESMTSQPT PVSHHREPSM LLPVSTTAQG
LAFPTTANYT SLQVDVPVVE VTTQETSVTV MPTVFGHVPR DQADNRREMK LLDTITSSTQ
SSAPEHVLRN KSATSEGVLT NVTPNSHLIT PNNLPGDTYW IVGNWSECST TCGMGAFWRH
VECSSRNTSH CQHMKKPDPA RKCYLRPCAS WKTGNWSKCS ASCNGGFKTR DVHCIDVREK
RLLRPFHCQL LGYKPQLNTS CNVEPCLQWH VEPWNECSRT CGGGQQKRRI YCPEEGYCDW
TKRPNAIASC NRQPCTQWIN QAWGPCTVSC GGGIQQRTVK CMNIETNETE DDSTCVDKPK
PTEIQKCNLQ ECRKSTGLPC SKDQLSVHFC QRLKGIGKCL LPSIQTQCCF TCSQPRIRNK
ARYWDQR
//
