ID M4ASR1_XIPMA Unreviewed; 1879 AA.
AC M4ASR1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Proprotein convertase subtilisin/kexin type 5 {ECO:0000313|Ensembl:ENSXMAP00000017506.1};
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:ENSXMAP00000017506.1, 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:ENSXMAP00000017506.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000017506.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 8083.ENSXMAP00000017506; -.
DR Ensembl; ENSXMAT00000017531.2; ENSXMAP00000017506.1; ENSXMAG00000017401.2.
DR eggNOG; KOG3525; Eukaryota.
DR GeneTree; ENSGT00940000155770; -.
DR HOGENOM; CLU_003159_0_0_1; -.
DR InParanoid; M4ASR1; -.
DR OMA; TWYNDTW; -.
DR Proteomes; UP000002852; 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; 14.
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:SF3; FURIN-LIKE PROTEASE 1, ISOFORMS 1_1-X_2; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF14843; GF_recep_IV; 2.
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; 16.
DR SMART; SM01411; Ephrin_rec_like; 8.
DR SMART; SM00261; FU; 22.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 8.
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:UP000002852};
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..1879
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004048123"
FT TRANSMEM 1767..1789
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 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 1879 AA; 209836 MW; 60EFC41E0011D38A 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 KDGEYLSKQG TCHLCDVSCL
QCTGPESEAC TVCPDTRFFE DGRCVIRCQE RRYVQGKQCL PCHNTCKACT AEGPDSCTSC
DTDRLGEPRY LFQNQCREAC PEGFFHSATM CCEPCPAECV VCTAADRCVQ CSSGYRLRNG
HCVQLECSTD EASDDDQQDC LPCDEGCKKC RLNDSGDQKQ KTACLQCEDG YYLFEADCHQ
SCPDWTYEVK ETMMCSSCDD PVCRVCDQSQ CYWCEDGFYV SEGECVDHCQ EGYFMDKESQ
ECEPCHRECR SCGGPGSDSC DSCEDGFTLK NGECLDGKQL ATCPEGQFKN SQGKCELCHS
SCKNCFAARK ESCSSCNSNH FLTLNHTCVS RCPSGTFGNK TSGQCDPCLS GCVVCQEAQA
CQRCLTGLYL QNGTCVVECQ RGFPQGEECH QCAPECGSCK ERSSNCLSCE RRFLLLDNSC
LSSCPKGYYD NSKECLRCPQ HCSECSQDGL CKKCADYYFL YDADCVDECP KGYFDNDQEC
MQCHADCASC DGPDQNDCDV CRNPKAVRYY GECLARCPSN TYHDENTNEC KACDKSCLTC
SGHEPTDCLS CDTNRRVDES RHCVWNSQCS MDSYMDLNGD CQRCHTQCHR CDGPGRDHCL
GCNEPHLLLN TTCVKKCPVG YYIEDKVDRV CERCHPSCES CFGHHSQHCK TCKPGFFKQA
SSCVETCSES HFGNKTTMLC ERCDPSCSQC AGSGNTHCLN CREGYVYMRP WGQCLKSCPP
GYYKDIWSTD CHKCHHTCKT CNDEGALSCL SCYDGFTFEG GFCDNPCFIG SYPASKDLKR
DDPNCRHCDQ SCEGCWGPSM WQCTLCHPSH ILADDGRCLS CCGKKTPLDD TPIPRECCDC
EASYVRCILG VNFVMRSAED LESSARFNVM ACVMSIVVLG GGIFVLLSAR SKWFAMKSKT
KEGGYQKLNT NDVSPPQPTT SSFGEYSDRI TECENDEEYD EEDIVYMSKD GTVYRKFKYG
LLDDDDVELE YDDESYSYR
//
