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Database: UniProt
Entry: A0A3B5QGN0_XIPMA
LinkDB: A0A3B5QGN0_XIPMA
Original site: A0A3B5QGN0_XIPMA 
ID   A0A3B5QGN0_XIPMA        Unreviewed;       920 AA.
AC   A0A3B5QGN0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Proprotein convertase subtilisin/kexin type 5 {ECO:0000313|Ensembl:ENSXMAP00000030121.1};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000030121.1, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000030121.1}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000030121.1};
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   AlphaFoldDB; A0A3B5QGN0; -.
DR   Ensembl; ENSXMAT00000028442.1; ENSXMAP00000030121.1; ENSXMAG00000017401.2.
DR   GeneTree; ENSGT00940000155770; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
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; 5.
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; IPR010909; PLAC.
DR   InterPro; IPR032815; S8_pro-domain.
DR   InterPro; IPR038466; S8_pro-domain_sf.
DR   PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR   PANTHER; PTHR42884:SF7; PROPROTEIN CONVERTASE SUBTILISIN_KEXIN TYPE 5; 1.
DR   Pfam; PF14843; GF_recep_IV; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF08686; PLAC; 1.
DR   Pfam; PF16470; S8_pro-domain; 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; SSF54897; Protease propeptides/inhibitors; 1.
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:UP000002852};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..920
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017392799"
FT   DOMAIN          471..610
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   DOMAIN          876..920
FT                   /note="PLAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50900"
FT   REGION          187..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..204
FT                   /note="Polar residues"
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        395
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   920 AA;  102798 MW;  8976FBA3DC8B5905 CRC64;
     MVHNAAWRRS FLCVLAIYLG FASPPCKARL FTNHWAVRIA GGPEVADRIA EKYGYRNMGQ
     IGDLKDHYHF FHSRTIKRST LSSRGRHSFI SMEPKVEWIE QQVVKRRIKR DYKPVPPFSQ
     TSPAQNSVAQ NNIFYNDAKW SSMWYIHCSD DVHNCQSDMN IMGAWKRGYT GKDVVVTILD
     DGIERTHPDL SQNYDPQASY DVNSNDLDPM PRYDATNENK HGTRCAGEVA AAANNSHCIV
     GIAYNARIGG VRMLDGDVTD MVEARSLSLN PQHIDIYSAS WGPDDDGKTV DGPASLARQA
     FENGIRMGRK GRGSIFVWAS GNGGRSRDHC SCDGYTNSIY TISISSTAES GRKPWYLEEC
     SSTLTTTYSS GENYDRKIIT TDLRHRCTDS HTGTSASAPM AAAIIALALE ANTFLTWRDV
     QHIIVKTSRA GHLSAPDWKT NAAGYNVSHL YGFGLMDAEA MVKEAEQWKH VPAQQVCVET
     ADRQIRTIRP EHLVRSVYKA TGCSDNPNLK VIYLEHVVVR ITITHPRRGD LSINLTSPSG
     TKSQLLANRL FDHSMEGFKN WEFMTTHCWG EKAAGDWILE IYDSPSQLRS QKVPGKLKEW
     SLVLYGTSVH PYSTQQKDRF TDSLQPEEEF TEEYNGPCDA ECNENGCEGP GPHHCINCLH
     YFLKFKNNTR MCVSECPSGF FRDDRKRCKK CSSMCETCVG SRSDQCISCR TGYHLIEGSN
     TCAANCADGF YLDSDSNICR RCQENCKRCS ASNICTECKP GMSLQGHKCQ MTCNPGTYFN
     GHRRTCELCH RACATCAGTG IEACTKCADD YLLEDWRCVL TCSPGYYLSE QTSDNGQVQR
     FCKKCDNSCF ECLGPGELNC SSCNSGYNLE AGTCVVSTVC KDANEESWAE GGFCVLVKKN
     NLCQRRVLQQ LCCRTCSQKG
//
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