ID A0A2K5H909_COLAP Unreviewed; 1676 AA.
AC A0A2K5H909;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 7 {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:ENSCANP00000000828.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000000828.1}
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 STRING; 336983.ENSCANP00000000828; -.
DR Ensembl; ENSCANT00000003504.1; ENSCANP00000000828.1; ENSCANG00000002890.1.
DR OMA; YCSERQA; -.
DR Proteomes; UP000233080; Unplaced.
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: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; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR PANTHER; PTHR13723:SF281; NO LONG NERVE CORD, ISOFORM C; 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; 7.
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 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, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1676
FT /note="ADAM metallopeptidase with thrombospondin type 1
FT motif 7"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014434339"
FT DOMAIN 232..442
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1622..1662
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 182..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1102
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 379
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 194
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 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 319
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 319
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 378
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 382
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 388
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 437
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 440
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 440
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 308..362
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 337..344
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 356..437
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 395..421
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 464..487
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 475..493
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 482..512
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 506..517
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 540..577
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 544..582
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 555..567
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1676 AA; 183387 MW; 710813C4246C4BCA CRC64;
APSLRPLFLL LCALVPGAPG PAPGRATEGR AALDIVHPVR VDAGGSFLSY ELWPRALRKR
DVSVRRDAPA FYQLQYRGRE LRFNLTANQH LLAPGFVSET RRRGGLGRAH IQAHTPACHL
LGEVQDPELE GGLAAISACD GLKGVFQLSN EDYFIEPLDG ALAWPGHAQP HVVYKRQVPE
RLAQRGDSSA PSTCGVQVSP ELEPRRERWE QRQQWQRPRL RRLHQRSVSK EKWVETLVVA
DAKMVEYHGQ PQVESYVLTI MNMVAGLFHD PSIGNPIHIT IVRLVLLEDE EEDLKITHHA
DNTLKNFCKW QKSINMKGDA HPLHHDTAIL LTRKDLCAAM NRPCETLGLS HVAGMCQPHR
SCSINEDTGL PLAFTVAHEL GHSFGIQHDG SGNDCEPVGK RPFIMSPQLL YDAAPLTWSR
CSRQYITRFL DRGWGLCLDD PPAKDIIDFP SVPPGVLYDV SHQCRLQYGA YSAFCEDMDN
VCHTLWCSVG TTCHSKLDAA VDGTRCGENK WCLNGECVPV GFRPEAVDGG WSGWSAWSIC
SRSCGVGVQS AERQCTQPTP KYKGRYCVGE RKRFRLCNLQ ACPAGRPSFR HVQCSHFDAM
LYKGQLHTWV PVVNDVNPCE LHCRPSNEYF AEKLRDAVVD GTPCYQVRAS RDLCINGICK
NVGCDFEIDS GAMEDRCGVC HGNGSTCHTV SGTFEEAEGL GYVDVGLIPA GAREIRIQEV
AEAANFLALR SEDPEKYFLN GGWTIQWNGD YQVAGTTFTY ARRGNWENLT SPGPTNEPVW
IQLLFQESNP GVRYEYTIHR EAGGHGEAPP PEFSWHYGPW TTCTVTCGRG VQRQSVYCSE
RQAGPVDEEH CDPLGRPDDR QRKCSEQPCP ARWWAGEWQL CSSSCGPWGL SQRAVLCIRS
VGLDEQSALE PPACEHLPRP PTETPCNRHV PCPATWAVGN WSQCSVTCGE GTQHRNVLCT
NDTGVPCDEA QQPASQVTCS LPPCQWPLDT LGPEGSGSGS SSHELFNEAD FIPRHLAPRP
SPVSSPKPAT MGNAIEEEAL ELDLLGPVFV DDFYYDYNFI NFHEDLSYGP SEGPDLDLVE
TGDQTPPPHS GPAVPSTGSP VPATEPPAAK EEGAPAPWSP SPWPSQAGSS PLPPSEQTPG
NSLINFLPEE DAPIGAPDLG LPSLPWPRVS IDGLQTPAAP ESQNDFPVGK DSQSQLPPPW
RDRTNEVFKD DEEPEGRGAP HPPLRPSPTL PPLSSVGSTH SSPSPDVMEL WTGGTVAWEP
ALEGGLGPVD SELWPTVGVA PPPPPPIAHL PEMKGRDNPL EPRTPTFPTP GPGSWDVQTV
AVWGTFLPTT LTGLGHTPEP ALNPGPKGQP ESLSPEVPLS SRLLSTPAWD SPANSHRTPE
TQPLAPSLAE AVSPADLLAV RNASWQAGNW SQCSTTCGLG AVWRPVRCSS GRDEDCAPAG
RPQPARRCHL RPCATWHSGN WSKCSRSCGG GSSVRDVQCV DTRDLRLLRP FHCQPGPAKP
PAHRPCGAQP CLSWYTSSWR ECSEACGGGE QQRLVTCPEP GLCEEALRPN TTRPCNTHPC
TQWVVGPWGQ CSAPCGGGVQ RRLVKCVNTQ TGLPEEDSDQ CGHEAWPENS RPCGTEDCEP
VELPRCERDR LSFGFCERLR LLGHCQLPTI RMQCCRSCSP PSYGAPSRGH QRVARR
//
