ID H3D124_TETNG Unreviewed; 1862 AA.
AC H3D124;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Proprotein convertase subtilisin/kexin type 5b {ECO:0000313|Ensembl:ENSTNIP00000014210.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000014210.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000014210.1}
RP IDENTIFICATION.
RG Ensembl;
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 STRING; 99883.ENSTNIP00000014210; -.
DR Ensembl; ENSTNIT00000014407.1; ENSTNIP00000014210.1; ENSTNIG00000015816.1.
DR GeneTree; ENSGT00940000155770; -.
DR InParanoid; H3D124; -.
DR OMA; TWYNDTW; -.
DR TreeFam; TF314277; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00064; FU; 17.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.30.70.850; Peptidase S8, pro-domain; 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; IPR032815; S8_pro-domain.
DR InterPro; IPR038466; S8_pro-domain_sf.
DR PANTHER; PTHR42884:SF13; NEUROENDOCRINE CONVERTASE 2; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF14843; GF_recep_IV; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF16470; S8_pro-domain; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00181; EGF; 14.
DR SMART; SM00261; FU; 22.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 7.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51829; P_HOMO_B; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1862
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003581862"
FT TRANSMEM 1764..1785
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 471..610
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 1800..1820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 180
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 221
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 396
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1862 AA; 204827 MW; 9F4385BD8269C3DF CRC64;
MVRNAAWRRS LLCVLALSLG LASAPCQARI YTNHWAVRIG GGPDVADRIA EKYGYRNMGQ
IGDLKDHYHF FHSRTIKRST LSSRGRHSFI SMEPKVEWIQ QQVVKRRIKR DYKTAPPRSL
SGPAHSSAAP GSVFYNDAKW SSMWYIHCND DVHNCQSDMN IMGAWKRGFT GKNVVVTILD
DGIERNHPDL LHNYDPQASY DVNSNDVDPM PRYDASNENK HGTRCAGEVA ASANNSYCIV
GIAYNARIGG VRMLDGDVTD MVEAKSLSLH PQHIDIYSAS WGPDDDGKTV DGPASLARQA
FENGMPPEGR KGRGSIFVWA SGNGGRSRDH CSCDGYTNSI YTISISSTAE SGRKPWYLEE
CSSTLTTTYS SGENYDRKII TTDLRHRCTD SHTGTSASAP MAAAIIALAL EANPLLTWRD
VQHIIVKTSK AGHLSAPDWK TNAAGYNVSH LYGFGLMDAE AMVKEAERWK QVPAQHVCVE
SADRQMRTIR PEHVVRSVYK ATGCTDNYNH VIYLEHVVVR ITITHPRRGD LSINLTSPSG
TKSQLLANRL FDHSMEGFKN WEFMTTHCWG EKAAGDWVLE IYDSPSQLRS QKVPGKLKEW
SLVLYGTSVH PYILRSEKPR SAEIRAHTNE EFAEDYNVAG PCDPECNERG CEGPGPHHCI
NCLHYFLKFK NNTRTCVSEC PSGFFRDDKK RCKKCSSACE TCVGSRSDQC TSCRPGYHLS
EGTNMCVSSC FESYYLDHDS NTCRRCPENC KRCNTSSICT ECEPGLSIQG NGCQLTCDLG
SYYNGHRKTC EACHPACATC AGVGVEGCTK CAQGYFLEDR NCVSTCSNGY YLPEKTSDSG
QVQRSCRKCD HSCYQCSGPG ERNCSSCMSG YNLEDGACVV STICKDGEYL SLRGECHLCD
VTCLQCTGPE REDCTSCSTS WFFNDGRCAH RCPRGRFAEG NQCSFCHHTC QECTDEGPEN
CTSCDTDKFG VARYLFQGQC RDVCPEGFFH SGRKRCEPCA ASCLACVAAD RCLSCGPGHK
LRDGQCGPLV CSTGEVADAR NLDCLPCDDG CKQCRQKFRE TICLKCEDDY YQFGTDCHRS
CPERTYSVDT NITCAPCEDA KCLTCDPSQC YWCEDGLYVL DGVCVADCGE GFFVDQESRD
CEPCHAACRA CGGPRYDDCD SCREGSKLKD GECLEARQFI VCPEKNFANI QGDCEQCHAS
CKTCFAPFKE NCTSCDPDLF LTAQQTCAAR CPLATFANKT SGRCAECSRG CDVCQTDQRC
QRCRSSLYLD NGVCVKACQR GFPEGGMCKP CSPECASCQG DPSYCLSCEQ QYLLQNHSCT
SQCLQGYYPA DRKCHRCPTY CRTCTQDGLC TECEKFYFLH TGQCVDDCPV GYFASQQQEC
VRCHADCASC DGPSSDDCEA CANPKAVRSN GECLPQCRSN TYHDKTTNEC RDCDRSCLTC
SGHGPSSCLS CGAKRRKDAS GHCVWVNQCD LTSYMDQNGQ CHQCHGACHR CSGPAENQCL
SCNQPAFLLN STCVPSCPVG YYSEDRDERV CERCHFSCRS CAGRHSLQCT ACKAGFFKQG
SSCVEHCSDS HYGNASTMVC DRCDPSCNQC LGGGNRNCLS CRQDFVLVKK WAQCLQSCPT
GFYLAEKSKT CYKCHPTCKT CSDEGALFCQ SCYDGFIYSR GICNSPCLTG YYPVPQGPEP
QALEPTCAAC HPSCVDCRGP GAWNCTVCPA LLILSDDGRC LSCCGGDGPH GDGAIPRECC
DCSASAVECV LGVLEAQGGA ARSFAAVCVL LILCAGFGSF VFLGLRARWL GAAPKPTAAG
YEKVDSSGQT APKPVASPSG EYSDRDIVYM SNDGTVYRKF KYGLLRDEEE MELDYDDETY
TY
//
