ID G7PPQ0_MACFA Unreviewed; 851 AA.
AC G7PPQ0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Suppressor of tumorigenicity 14 protein homolog {ECO:0000256|PIRNR:PIRNR036370};
DE EC=3.4.21.109 {ECO:0000256|PIRNR:PIRNR036370};
DE AltName: Full=Serine protease 14 {ECO:0000256|PIRNR:PIRNR036370};
GN ORFNames=EGM_06420 {ECO:0000313|EMBL:EHH56919.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1] {ECO:0000313|EMBL:EHH56919.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH56919.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
CC -!- FUNCTION: Exhibits trypsin-like activity as defined by cleavage of
CC synthetic substrates with Arg or Lys as the P1 site.
CC {ECO:0000256|PIRNR:PIRNR036370}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleaves various synthetic substrates with Arg or Lys at the P1
CC position and prefers small side-chain amino acids, such as Ala and
CC Gly, at the P2 position.; EC=3.4.21.109;
CC Evidence={ECO:0000256|PIRNR:PIRNR036370};
CC -!- SUBUNIT: Interacts with CDCP1. May interact with TMEFF1.
CC {ECO:0000256|PIRNR:PIRNR036370}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|PIRNR:PIRNR036370}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR EMBL; CM001289; EHH56919.1; -; Genomic_DNA.
DR AlphaFoldDB; G7PPQ0; -.
DR eggNOG; KOG3627; Eukaryota.
DR Proteomes; UP000009130; Chromosome 14.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00112; LDLa; 4.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 4.
DR Gene3D; 3.30.70.960; SEA domain; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR017051; Peptidase_S1A_matripase.
DR InterPro; IPR000082; SEA_dom.
DR InterPro; IPR036364; SEA_dom_sf.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR PANTHER; PTHR24252:SF8; ACROSIN; 1.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00057; Ldl_recept_a; 4.
DR Pfam; PF01390; SEA; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF036370; ST14; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00192; LDLa; 4.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 4.
DR SUPFAM; SSF82671; SEA domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 4.
DR PROSITE; PS50024; SEA; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Hydrolase {ECO:0000256|PIRNR:PIRNR036370};
KW Membrane {ECO:0000256|PIRNR:PIRNR036370, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|PIRNR:PIRNR036370};
KW Serine protease {ECO:0000256|PIRNR:PIRNR036370};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 86..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 117..234
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 245..365
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 371..478
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 646..851
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 490..508
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 502..517
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 527..545
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 539..554
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 556..568
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 563..581
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 575..590
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 598..610
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 618..633
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 851 AA; 94691 MW; C983A3A9A95F6838 CRC64;
MLVYPNDGIN AAATKRHALL CTQEPGAPTY VKDDSLKERP RRPGFDSPSL RFNLNEQFKV
NGLEEGVEFL PVNNVKKVEK RGPGRWVVLA AVLIGLLLVS LGIGFLVWHL QYRDVRVQKI
FNGYLRITNE NFLDAYENSN STEFVSLASK VKDALKLLYS GVPFLGPYHK ESAVTAFSEG
SVIAYYWSEF SIPQHLVEEA ERVMAEERVV MLPPRARSLK SFVVTSVVAF PTDPKTVQRT
QDNSCSFALH ARGVEVMRFT TPGFPDSPYP AHARCQWALR GDADSVLSLT FRSFDLASCD
ERGSDLVTVY NTLSPMEPHA LVQLCGTYPP SYNLTFLSSQ NVLLITLITN TERRHPGFEA
TFFQLPKMSR CGGHLRKAQG TFNSPYYPGH YPPNVDCTWN IEVPNNQHVK VRFKFFYLLE
PGVPTGTCPK DYVEINGEKY CGERSQFVVT SNSNKITVRF HSDQSYTDTG FLAEYLSYDS
SDPCPGQFTC RTGRCIRKEM RCDGWADCTD YSDELNCSCD ATHQFTCKNK FCKPLFWVCD
SVNDCGDYSD EQGCSCPAQT FRCSNGKCLS KSQQCDGKDD CGDGSDEASC PKVNVVTCTK
HTYRCLNGLC LSKGNPECDG KKDCSDGSDE KDCDCGLRSF TRQARVVGGT DADEGEWPWQ
VSLHALGQGH VCGASLISPN WLVSAAHCYI DDRGFRYSDP TQWTAFLGLH DQSQRSAPEV
QERRLKRIIS HPSFNDFTFD YDIALLELEK PVEYSSVVRP ICLPDASHVF PAGKAIWVTG
WGHTQYGEFC ESNDPWGAPR MTLPPKQPGS QPCPALSPGT GALILQKGEG GALSEEDGRK
CGFVFGGEVV M
//
