ID A0A2K5K0A2_COLAP Unreviewed; 967 AA.
AC A0A2K5K0A2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Peptidase M12B domain-containing protein {ECO:0000259|PROSITE:PS50215};
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:ENSCANP00000034528.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000034528.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_011781874.1; XM_011926484.1.
DR AlphaFoldDB; A0A2K5K0A2; -.
DR STRING; 336983.ENSCANP00000034528; -.
DR Ensembl; ENSCANT00000057761.1; ENSCANP00000034528.1; ENSCANG00000040930.1.
DR GeneID; 105500811; -.
DR KEGG; cang:105500811; -.
DR CTD; 9510; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0031012; C: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; 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 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:UP000233080};
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 258..467
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 402
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 198
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 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 261
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 401
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 405
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 411
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 CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR613274-4"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR613274-4"
FT CARBOHYD 764
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR613274-4"
FT DISULFID 333..385
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 362..367
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 379..462
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 417..446
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 488..511
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 499..521
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 506..540
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 534..545
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 571..608
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 575..613
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 586..598
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 967 AA; 105462 MW; A2399CAB026B4276 CRC64;
MQRAVPEGFG RRKLGSDMGN ADRAPGSRSF GPVPALLLLA AALLAVSDAL GRPAEEDEEL
VVPELERAPG HGTTRLRLHA FDQQLDLELR PDSSFLAPGF TLQNVGRKPG SETPLPEPDL
AHCFYSGTVN GDPSSAAALS LCEGVRGAFY LRGEAYFIQP LPAASERLAT VAPGEKPPAP
LQFHLLRRNR QGDGGGTCGV VDDEPRPTGK AETEDEDEGN EGEDEGAQWS LQDPALQRVG
QPTGTGSIRK KRFVSSHRYV ETMLVADQSM AEFHGSGLKH YLLTLFSVAA RLYKHPSIRN
SVSLVVVKIL VIHDEQKGPE VTSNAALTLR NFCNWQKQHN PPSDRDAEHY DTAILFTRQD
LCGSQTCDTL GMADVGTVCD PSRSCSVIED DGLQAAFTTA HELGHVFNMP HDDAKQCASL
NGVSQDSHMM ASMLSNLDHS QPWSPCSAYM ITSFLDNGHG ECLMDKPQNP IQLPGDLPGT
SYDANRQCQF TFGEDSKHCP DAASTCSTLW CTGTSGGVLV CQTKHFPWAD GTSCGEGKWC
INGKCVNKTD RKHFDTPFHG SWGMWGPWGD CSRTCGGGVQ YTMRECDNPV PKNGGKYCEG
KRVRYRSCNI EDCPDNNGKT FREEQCEAHN EFSKASFGSG PAVEWIPKYA GVSPKDRCKL
ICQAKGIGYF FVLQPKVVDG TPCSPDSTSV CVQGQCVKAG CDRIIDSKKK FDKCGVCGGN
GSTCKKISGS VTSAKPGYHD IITIPTGATN IEVKQRNQRG SRNNGSFLAI KAVDGTYILN
GDYTLSTLEQ DIMYKGVVLR YSGSSAALER IRSFSPLKEP LTIQVLTVGN ALRPKIKYTY
FVKKKKESFN AIPTFSAWVI EEWGECSKSC ELGWQRRLVE CRDINGQPAS ECAKEVKPAS
TRPCADHPCP QWQLGEWSSC SKTCGKGYKK RSLKCLSHDG GVLSHESCDP LKKPKHFIDF
CTMAECS
//
