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Database: UniProt
Entry: I3M7U1_ICTTR
LinkDB: I3M7U1_ICTTR
Original site: I3M7U1_ICTTR 
ID   I3M7U1_ICTTR            Unreviewed;      1036 AA.
AC   I3M7U1;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Presequence protease, mitochondrial {ECO:0000256|ARBA:ARBA00020167};
DE   AltName: Full=Pitrilysin metalloproteinase 1 {ECO:0000256|ARBA:ARBA00032857};
GN   Name=PITRM1 {ECO:0000313|Ensembl:ENSSTOP00000005709.3};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000005709.3, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Proteomes:UP000005215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000005709.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBUNIT: Monomer and homodimer; homodimerization is induced by binding
CC       of the substrate. {ECO:0000256|ARBA:ARBA00011853}.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. PreP subfamily.
CC       {ECO:0000256|ARBA:ARBA00007575}.
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DR   EMBL; AGTP01017010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005320388.1; XM_005320331.2.
DR   AlphaFoldDB; I3M7U1; -.
DR   STRING; 43179.ENSSTOP00000005709; -.
DR   Ensembl; ENSSTOT00000006387.3; ENSSTOP00000005709.3; ENSSTOG00000006348.3.
DR   GeneID; 101956820; -.
DR   CTD; 10531; -.
DR   eggNOG; KOG2019; Eukaryota.
DR   GeneTree; ENSGT00390000018381; -.
DR   HOGENOM; CLU_009165_0_0_1; -.
DR   InParanoid; I3M7U1; -.
DR   OrthoDB; 5477696at2759; -.
DR   TreeFam; TF300333; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR   GO; GO:0006508; P:proteolysis; IEA:Ensembl.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR013578; Peptidase_M16C_assoc.
DR   PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR   PANTHER; PTHR43016:SF13; PRESEQUENCE PROTEASE, MITOCHONDRIAL; 1.
DR   Pfam; PF08367; M16C_assoc; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SMART; SM01264; M16C_associated; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000005215}.
FT   DOMAIN          504..752
FT                   /note="Peptidase M16C associated"
FT                   /evidence="ECO:0000259|SMART:SM01264"
FT   REGION          803..835
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        803..826
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1036 AA;  117778 MW;  ED04CD9454CE1BFF CRC64;
     MWRCGGRRVR EALQRLRGCS TQHRVWRGMS NPACERALQY KVGEKIHGFT VNQVTSIPEL
     FLTAVKLSHD NTGARYLHLA REDTNNVFSV QFRTTPMDST GVPHVLEHTV LCGSQKYPCR
     DPFFKMLNRS LSTFMNAFTA SDFTQYPFST QNHKDFQNLL SVYLDATFFP CLRELDFWQE
     GWRLEHEDPS DPQTPLIFKG VVFNEMKGAF TDNERIFSQH LQNKILPDHT YSVISGGDPL
     CIPELTWEQL KQFHATHYHP SNARFFTYGN FQLEQHLRQI HEEALSKFQK IEPNTAVPAQ
     KHWDKPREFQ ITCGPHSLAA NTSKQTMVSV SFLLPDITDT FEAFTLSLLS SLLVAGPNSP
     FYKALIESGL GTDFSPDVGY NGNTREAYFS VGLQGIAEKD IQKVRDLVDS TFDEVVEKGF
     EDDQIEALLH KIEIQMKHQS TSFGRALISY VASCWNHDGD PVELLQLGNQ LTKFRQCLKE
     NPKFLQEKVK QYFMNNQHKL TLSMKPDDKY YEKQTQIETE KLKQKVDSLS PEDKQQIYEK
     GLELRSQQSK PQDASCLPAL KVSDIEPSMP FTSLDVALTA GEIPVQYCAQ PTNGLVYFRA
     FSSLNTLPEE LRPYVPLFCS VLTKLGCGTL NYRELAQQLE LKTGDMTVSP HVLPDESNPD
     TYEQGVLFSS FCLNRNLPDM MHLWSEIFNN PSFEEDEHFK VLVKMTAQEL SNGIPDSGHF
     YATLRASRTL TPAGDLQETF SGMNQVRLMK RIAEMTDIKP ILRKFPRIKK HVLNCDNMRC
     SVNATPQQMS QAEKEVEKFI RSLGRSKKER KPVRPHVVEK PAHSGSGERA HGNGSQIIRK
     LITDPTFKPC QIKTHFQLPF PVYYVGECIR TVPYVHPDHA SLRILARVMT AKFLHTEIRE
     KGGAYGGGAK LNYNGIFTFY SYRDPNSIET LQSFEKAIDW AKSGKFTEQD IDEAKLSVFS
     AVDAPVAPSD KGMDHFLLGL SDEMKQTHRE QLFAVSHDKL VAVSNEYLGI GKSTHGLAIL
     GPEIAKIAKD PSWIIR
//
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