ID A0A2I3LUQ8_PAPAN Unreviewed; 552 AA.
AC A0A2I3LUQ8;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Matrix metallopeptidase 17 {ECO:0000313|Ensembl:ENSPANP00000027172.2};
GN Name=MMP17 {ECO:0000313|Ensembl:ENSPANP00000027172.2};
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000027172.2, ECO:0000313|Proteomes:UP000028761};
RN [1] {ECO:0000313|Ensembl:ENSPANP00000027172.2, ECO:0000313|Proteomes:UP000028761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT "Whole Genome Assembly of Papio anubis.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPANP00000027172.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR621190-2};
CC Note=Can bind about 5 Ca(2+) ions per subunit.
CC {ECO:0000256|PIRSR:PIRSR621190-2};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR621190-2};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR621190-
CC 2};
CC -!- SIMILARITY: Belongs to the peptidase M10A family.
CC {ECO:0000256|ARBA:ARBA00010370}.
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DR AlphaFoldDB; A0A2I3LUQ8; -.
DR Ensembl; ENSPANT00000045055.2; ENSPANP00000027172.2; ENSPANG00000003977.3.
DR GeneTree; ENSGT00940000158699; -.
DR OMA; WLVCGDP; -.
DR OrthoDB; 2225278at2759; -.
DR Proteomes; UP000028761; Chromosome 9.
DR Bgee; ENSPANG00000003977; Expressed in postnatal subventricular zone and 29 other cell types or tissues.
DR ExpressionAtlas; A0A2I3LUQ8; baseline.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00094; HX; 1.
DR CDD; cd04278; ZnMc_MMP; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.110.10.10; Hemopexin-like domain; 1.
DR InterPro; IPR000585; Hemopexin-like_dom.
DR InterPro; IPR036375; Hemopexin-like_dom_sf.
DR InterPro; IPR018487; Hemopexin-like_repeat.
DR InterPro; IPR033739; M10A_MMP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001818; Pept_M10_metallopeptidase.
DR InterPro; IPR021190; Pept_M10A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1.
DR PANTHER; PTHR10201:SF21; MATRIX METALLOPROTEINASE-17; 1.
DR Pfam; PF00045; Hemopexin; 4.
DR Pfam; PF00413; Peptidase_M10; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00120; HX; 4.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF50923; Hemopexin-like domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 4.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR621190-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001191-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000028761};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001191-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 76..243
FT /note="Peptidase metallopeptidase"
FT /evidence="ECO:0000259|SMART:SM00235"
FT REPEAT 280..325
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 329..374
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 375..422
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 423..470
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REGION 248..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 196
FT /evidence="ECO:0000256|PIRSR:PIRSR001191-1"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001191-2"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001191-2"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001191-2"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 333
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 381
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 427
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT MOD_RES 364
FT /note="Phosphotyrosine; by PKDCC"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-4"
SQ SEQUENCE 552 AA; 61780 MW; 19A0CC389B25034B CRC64;
EWLSRFGYLP PADPTTGQLQ TQEELSKAIT AMQQFGGLEA TGILDEATLA LMRTPRCSLP
DLPVLTQARR RRQAPAPTKW NKRNLSWRVR TFPRDSPLGR DTVRALMYYA LKVWSDIAPL
NFHEVAGSAA DIQIDFSKAD HNDGYPFDGP GGTVAHAFFP GDHHTAGDTH FDDDEAWTFR
SSDAHGMDLF AVAVHEFGHA IGLSHVAATH SIMRPYYQGP VGDPLRYGLP YEDRVRVWQL
YGVRESVSPT AQPEEPPLLP EPPDNRSSIP PRKDVPHRCS THFDAVAQIR GEAFFFKGKY
FWRLTRDRHL VSLQPAQMHR FWRGLPLHLD SVDAVYERTS DHKIVFFKGD RYWVFKDNNV
EEGYPRPVSD FSLPPGGIDA AFSWAHNDRT YFFKDQLYWR YDDHTRRMDP GYPAQSPLWR
GVPSTLDDAM RWSDGASYFF RGQEYWKVLD GELEAAPGYP QSTARDWLVC GDPQADGSAA
AGIDGAEGPR APPGQHDQSR SEDGYEVCSC TSQASSLPGA PGPLVATTSL LLLLLLPLSP
GALWTAAQAL VL
//
