ID A0A2K6FX30_PROCO Unreviewed; 965 AA.
AC A0A2K6FX30;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 1 {ECO:0000313|Ensembl:ENSPCOP00000018530.1};
GN Name=ADAMTS1 {ECO:0000313|Ensembl:ENSPCOP00000018530.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000018530.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000018530.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 RefSeq; XP_012495607.1; XM_012640153.1.
DR AlphaFoldDB; A0A2K6FX30; -.
DR STRING; 379532.ENSPCOP00000018530; -.
DR Ensembl; ENSPCOT00000029173.1; ENSPCOP00000018530.1; ENSPCOG00000021162.1.
DR GeneID; 105806916; -.
DR KEGG; pcoq:105806916; -.
DR CTD; 9510; -.
DR GeneTree; ENSGT00940000156815; -.
DR OMA; VNRDSHM; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR GO; GO:0060347; P:heart trabecula formation; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0001542; P:ovulation from ovarian follicle; IEA:Ensembl.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IEA:Ensembl.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
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; 3.
DR InterPro; IPR006586; ADAM_Cys-rich.
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; IPR013274; Pept_M12B_ADAM-TS1.
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:SF40; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 1; 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; 2.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01858; ADAMTS1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR PRINTS; PR01705; TSP1REPEAT.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 3.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 3.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
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, ECO:0000256|PIRSR:PIRSR613274-
KW 4}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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:UP000233160};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 256..465
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 198..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 400
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 203
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 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 349
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 399
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 403
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 409
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 460
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 463
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 463
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR613274-4"
FT CARBOHYD 718
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR613274-4"
FT CARBOHYD 762
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR613274-4"
FT DISULFID 331..383
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 360..365
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 377..460
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 415..444
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 486..509
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 497..519
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 504..538
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 532..543
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 569..606
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 573..611
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 584..596
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 965 AA; 105083 MW; 21FBA875C0ABAA57 CRC64;
MQRAVRAVSR RRKLGGDMGK AEWAPRSWSV RPAPTLLLLA AAAALLAVPG ARGRPAEEDE
ELVLPALERA PGHGTTLLRL DAFGRWLHLE LQPDRGFLAP GFTLQTVGRR PEPEAPRSDP
AGDLAHCFYS GTVNGDPSSA AALSLCEGVR GAFYLQGEEY FIQPAPAAAT ERLAPAAAGE
EPLAGPQFHL LRRRRRGGSG AKCGVMDDET LPARGAGPEG EDAGAQWLPR DRAPPGAGQT
AGTGSIRKKR FVSSPRYVET MLVADQSMAE FHGSGLKHYL LTLFSVAARL YKHPSIRNSV
SLVVVKILVI YEEQKGPEVT SNAALTLRNF CNWQKQHNPP SDRDAEHYDT AILFTRQDLC
GAQTCDTLGM ADVGTVCDPS RSCSVIEDDG LQAAFTTAHE LGHVFNMPHD DAKQCASLNS
VNQDSHMMAS MLSNLDRSQP WSPCSAYMIT SFLDNGHGEC LLDKPQSPIQ LPADLPGTLY
DANRQCQFTF GEESKHCPDA ASTCTTLWCT GTSGGLLVCQ TKHFPWADGT SCGEGKWCVN
GKCVNKTDKK HFDTPIHGSW GQWGPWGECS RTCGGGVQYT MRECDNPVPK NGGKYCEGKR
VRYRSCNIED CPDNNGKTFR EEQCEAHNEF SKPSFGSGPA VEWTPKYAGV SPKDRCKLIC
QAKLIGYFFV LQPKVIDGTP CSPDSTSVCV QGQCVKAGCD RIIDSKKKFD KCGICGGNGS
TCKKISGSVT SAKPGYHDIV TIPTGATNIE VKQRNQRGSR NNGSFLAIKA ADGTYILNGD
FTLSTLEQDI TYKGVVLRYS GSSAALERIR SFSPLKEPLT IQVLTVGNAL RPKIKYTYFV
KKKKESFNAI PTFSEWVIEE WGECSKSCGL GWQRRVVECR DINGQPASEC AKEVKPASTR
PCADLPCPHW QVGDWSPCSK TCGKGYKKRT LKCLSHDGGV LSPESCDPLK KPKHYIDFCM
MAECS
//
