ID A0A2Y9DDP0_TRIMA Unreviewed; 841 AA.
AC A0A2Y9DDP0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Proprotein convertase subtilisin/kexin type 6 {ECO:0000313|RefSeq:XP_004372698.1};
GN Name=LOC101351134 {ECO:0000313|RefSeq:XP_004372698.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004372698.1};
RN [1] {ECO:0000313|RefSeq:XP_004372698.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR RefSeq; XP_004372698.1; XM_004372641.1.
DR AlphaFoldDB; A0A2Y9DDP0; -.
DR STRING; 127582.A0A2Y9DDP0; -.
DR GeneID; 101351134; -.
DR KEGG; tmu:101351134; -.
DR InParanoid; A0A2Y9DDP0; -.
DR OrthoDB; 5474719at2759; -.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00064; FU; 4.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR032778; GF_recep_IV.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR034182; Kexin/furin.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010909; PLAC.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR PANTHER; PTHR42884:SF8; PROPROTEIN CONVERTASE SUBTILISIN_KEXIN TYPE 6; 1.
DR Pfam; PF14843; GF_recep_IV; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00261; FU; 5.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 365..505
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT DOMAIN 803..841
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 510..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 75
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 116
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 290
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 841 AA; 93612 MW; B2EB0EDD134E882F CRC64;
MDPQVKWLQQ QEVKRRVKRQ ARSDPKTLYF NDPIWSSMWY MHCSDKNRRC RSEMNVQAAW
KRGYTGKNVV VTILDDGIER NHPDLAPNYD SYASYDVNGN DYDPSPRYDA SNENKHGTRC
AGEVAASANN SYCIVGIAYN AKIGGIRMLD GDVTDVVEAK SLGIRPNYID IYSASWGPDD
DGKTVDGPGR LAKQAFQYGI KKGRQGLGSI FIWASGNGGR EGDYCSCDGY TNSIYTISVS
STTENGYKPW YLEECASTLA TTYSSGAFFE RKIVTTDLRQ RCTDGHTGTS VSAPMVAGII
ALALEANNQL TWRDVQHLLV KTSRPAHLRA NDWKYNGAGH RVSHLYGFGL VDAEALVVEA
KKWKAVPSQH TCVTAVDKRP RSIPVAQTLR TTALTSACAD HSDQHVVYLE HVVAQISLSH
PRRGDLQIHL ISPAGTRSQL LAKRLLDHSN EGFTNWEFMT VHCWGEKAEG EWTLEIQDIP
SQVRNPEKQG KLKEWSLILY GTAQHPYNTF SSHQSRSRML ELSTPELELE PSKPAAFPAQ
SEVPEEEEDY TAPSTQGSPN ILQKSMCHPE CGNKGCDGPN ADQCLNCVHF SLGSSKTSRK
CVSTCPLGYF ADTAARRCRR CHKGCESCSG KAPTQCLSCR KGFYHHQEIS ACVTLCPVGF
YADESQKNCL KCHPSCKKCT DEPEKCTICK EGFSLVRDTC LPDCEPGTYF DSELIRCGEC
HPTCQTCVGP SREECIHCAK PFHFHDWKCV PTCGEGFYPE QMPGLPHKVC RRCDENCLSC
EGSSRNCSKC KPGFTHLGTL CITNHTCSNA DETFCEMVKS NRLCERKLFI QFCCRTCLLA
G
//
