ID A0A2K6DQX2_MACNE Unreviewed; 428 AA.
AC A0A2K6DQX2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Transmembrane serine protease 13 {ECO:0000313|Ensembl:ENSMNEP00000038328.1};
GN Name=TMPRSS13 {ECO:0000313|Ensembl:ENSMNEP00000038328.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000038328.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000038328.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR AlphaFoldDB; A0A2K6DQX2; -.
DR Ensembl; ENSMNET00000062806.1; ENSMNEP00000038328.1; ENSMNEG00000042137.1.
DR GeneTree; ENSGT00940000159197; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000042137; Expressed in lymph node.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF11; TRANSMEMBRANE SERINE PROTEASE 2; 1.
DR Pfam; PF15494; SRCR_2; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00202; SR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF56487; SRCR-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50287; SRCR_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 126..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 155..276
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 286..396
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 210..274
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 428 AA; 46598 MW; 4679032C1BB8B485 CRC64;
QASPAGTPPG RASPAQASPA GTPPGRASPA QASPARASPA QASASPARAS PARSSPSRSS
SGRSSSARSA SVTTSPTRVY LVRATPVGAV PIRSSPARSA PAARATRESP GTSLPKFTWR
EGQKRLPLIG CVLLLIALVV SLIILFQFWR GHTGIRYKEQ RESCPKHAVR CDGVVDCKLK
SDELGCVRFD WDKSLLKIYS GSSHQWLPIC SSNWNDSYSE KTCQQLGFES AYRTTEVAHR
DFANSFSISR YNSTIQESLH RSECPSQRYI SLQCSHCGLR AMTGRIVGGA LASESKWPWQ
VSLHFGTTHI CGGTLIDAQW VLTAAHCFFV TREKVLEGWK VYAGTSNLHQ LPEAVSIAEI
IINSNYTDEE DDYDIALMRL SKPLTLSGDI CQLISGLQSF CMAEVKTLKD PYMEHFCCII
RETEAQGL
//
