ID A0A2K5KFG4_COLAP Unreviewed; 1061 AA.
AC A0A2K5KFG4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 2 {ECO:0008006|Google:ProtNLM};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000039831.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000039831.1}
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 AlphaFoldDB; A0A2K5KFG4; -.
DR STRING; 336983.ENSCANP00000039831; -.
DR Ensembl; ENSCANT00000063092.1; ENSCANP00000039831.1; ENSCANG00000043593.1.
DR OMA; ICPRNIS; -.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
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; 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; IPR013275; Pept_M12B_ADAM-TS2.
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:SF141; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 2; 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; PR01859; ADAMTS2.
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; 3.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 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 Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW 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:UP000233080};
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};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 219..423
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 909..947
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 1021..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 362
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 314
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 361
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 365
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 371
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 418
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 421
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 421
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 296..345
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 339..418
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 378..404
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 445..470
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 456..479
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 465..498
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 492..503
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 526..563
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 530..568
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 541..553
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1061 AA; 118419 MW; FD54323ECAB3AFCC CRC64;
GPLGHGAERI LAVPVRTDAQ GRLVSHVVSA ATARAGVRAR RAAPVRTPSF PGGNEEDPGS
HLFYNVTVFG RDLHLRLRPN ARLVAPGATM EWQGETGTTR VEPLLGSCLY VGDVAGLAEA
SSVALSNCDG LAGLIRMEEE EFFIEPLEKG LAAQEAEQDR VHVVYRRPPK SPPLVGPQAL
DTGASLGNLD SLSRALGVLE ERVNSSRRRA RRHAADDDYN IEVLLGVDDS VVQFHGKEHV
QKYLLTLMNI VNEIYHDESL GAHINVVLVR IILLSYGKSM SLIEIGNPSQ SLENVCRWAY
LQQKPDTDHD EYHDHAIFLT RQDFGPSGMQ GYAPVTGMCH PVRSCTLNHE DGFSSAFVVA
HETGHVLGME HDGQGNRCGD EVRLGSIMAP LVQAAFHRFH WSRCSQQELS RYLHSYDCLR
DDPFAHDWPA LPQLPGLHYS MNEQCRFDFG LGYMMCTAFR TFDPCKQLWC SHPDNPYFCK
TKKGPPLDGT MCAPGKHCFK GHCIWLTPDI LKRDGNWGAW SPFGSCSRTC GTGVKFRTRQ
CDNPHPANGG RTCSGLAYDF QLCSRQDCPD SLADFREEQC RQWDLYFEHG DAQHHWLPHE
HRDAKERCHL YCESRETGEV VSMKRMVHDG TRCSYKDAFS LCVRGDCRKV GCDGVIGSSK
QEDKCGVCGG DNSHCKVVKG TFTRSPKKHG YIKMFEIPAG ARHLLIQEVD ATSHHLVIPA
GDTRVSLTYK YMIHEDSLNV DDNNVLEDDS VVYEWALKKW SPCSKPCGGG SQFTKYGCRR
RLDHKMVHRG FCAALSKPKA IRRACNPQEC SQPVWVTGEW EPCSHSCGRT GMQVRSCSVT
CGNGTQERPV LCRTADDSFG ICQEERPETA RICRLGPCPR NISDPSKKSY VVQWLSRPDP
DSPIQKISSK GHCQGDKSIF CRMEVLSRYC SIPGYNKLCC KSCDLHNNLT SVEGRTQPPP
GKHNDIDVFM PTLPVPTVVT EVQPSPSTPL DVPLNASSTN ATEDHPETNA VDEPYKIHGL
EDEVQPPNLI PRRPSPYEKT RNQRIQELID EMRKKEMLGK F
//
