ID A0A091ID96_CALAN Unreviewed; 1016 AA.
AC A0A091ID96;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 36.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 9 {ECO:0000313|EMBL:KFP06589.1};
DE Flags: Fragment;
GN ORFNames=N300_15070 {ECO:0000313|EMBL:KFP06589.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFP06589.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFP06589.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP06589.1};
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR EMBL; KL218562; KFP06589.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091ID96; -.
DR STRING; 9244.A0A091ID96; -.
DR Proteomes; UP000054308; 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; -; 2.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 1.
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; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF33; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 9; 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; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 1.
DR Pfam; PF00090; TSP_1; 2.
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; 3.
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 Integrin {ECO:0000313|EMBL:KFP06589.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000054308};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}.
FT DOMAIN 286..494
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 87..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 430
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 429
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 433
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 439
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 489
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 492
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 492
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 361..413
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 389..395
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 407..489
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 445..473
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 516..538
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 527..548
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 533..567
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 561..572
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 595..632
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 599..637
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 610..622
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT NON_TER 1016
FT /evidence="ECO:0000313|EMBL:KFP06589.1"
SQ SEQUENCE 1016 AA; 114021 MW; 786BF5B485806CA6 CRC64;
MQLAPLALAL TTLFIDGLRT GARRQKLHPR QAKLLEKLSE YEIVTTTRVN GFFFFYFIIS
HTAFINPPGS GTGVNLSCSG GFGGKNTPQR ARSVGTAHGH PPAKGWLGGS SSVPPPQSSC
TQGQDPRGRE VSLAAPPAIL LPLQHRGNVD KGMSRTDCLL LSGPSQLGTF KSDDGDYFVE
PLLSLEEQEY EEEHNKPHLV YRHRTPPTNT SGDRQTCDTP DHEHSHKKNK RKHWRRQWAE
SSILSDVEML KHSLEVNSFS ADSNKTGNIS EKKSHRRTKR FLSYPRFVEV MVVADSRMVA
YHGANLQHYV LTLMSIVASI YKDPSIGNLI NIVIVKLVVI HNEQDGPAIS YNAQTTLKNF
CQWQQSQNHP EGSHLQHDTA VLVTRQDICR AHDKCDTLGL AELGTVCDPY RSCSISEDNG
LSTAFTIAHE LGHVFNMPHD DNHKCKEDGG KNQQHVMAPT LNFYTNPWMW SKCSRKYITE
FLDTGYGECL LDEPSSRTYT LPQQLPGLIY DVNKQCELIF GPGSQVCPYM MQCRRLWCIN
IDGAHKGCRT QHTPWADGTE CEPGKHCRFG MCVPKEREAP VTDGAWGTWS PFGTCSRTCG
GGIKTAIREC NRPEPKNGGK YCVGRRMKFK SCNTEPCSKL KKDFRDEQCA DFDGKHFNIN
GLPTNVRWVP KYSGILMKDR CKLFCRVAGN TAYYQLRDRV IDGTPCGPDT NDICVQGLCR
QAGCDHVLNS KARRDKCGVC GGDNSSCKTV AGTFNTVHYG YNVVVRIPAG ATNIDVRQHS
YSGKPEDDNY LALSNSQGDF ILNGDFVVSM FKREIKVGNA VIEYSGSDNT IERINSTDRI
EQEITLQVLS VGNLYNPDVR YTFNIPIEDK PQQFYWNAYG PWQPCSKLCQ GERRRKPVCT
RESDQLTVSD QRCDRMPQPD PITEPCGTEC ELRWHIARRS ECTAQCGLGY RTLEIFCSKY
SRVEGKIEKV DDRFCNSQPK PSTREKCTGD CNVGGWRYSA WTECSKSCGG GTRRRR
//
