ID V4CS00_LOTGI Unreviewed; 635 AA.
AC V4CS00;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=P/Homo B domain-containing protein {ECO:0000259|PROSITE:PS51829};
DE Flags: Fragment;
GN ORFNames=LOTGIDRAFT_102960 {ECO:0000313|EMBL:ESP05305.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESP05305.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESP05305.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000256|ARBA:ARBA00005325}.
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DR EMBL; KB199650; ESP05305.1; -; Genomic_DNA.
DR RefSeq; XP_009043850.1; XM_009045602.1.
DR AlphaFoldDB; V4CS00; -.
DR STRING; 225164.V4CS00; -.
DR EnsemblMetazoa; LotgiT102960; LotgiP102960; LotgiG102960.
DR GeneID; 20229679; -.
DR KEGG; lgi:LOTGIDRAFT_102960; -.
DR CTD; 20229679; -.
DR HOGENOM; CLU_002976_4_4_1; -.
DR OMA; NEWVVEI; -.
DR OrthoDB; 5474719at2759; -.
DR Proteomes; UP000030746; Unassembled WGS sequence.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR008979; Galactose-bd-like_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:SF14; NEUROENDOCRINE CONVERTASE 1; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 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 SUPFAM; SSF49785; Galactose-binding domain-like; 1.
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 Calcium {ECO:0000256|ARBA:ARBA00022837};
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:UP000030746};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 422..556
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 142..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 128
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 169
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 342
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ESP05305.1"
SQ SEQUENCE 635 AA; 71135 MW; 157757BF8247D14F CRC64;
LFFQLRGFDD NYLLRHKDVP SRSRRSADHH TKRLIDDSRV EWADQQYTKI RVKRDFLDDD
LYDGDFTAKR EAENLIYSKT SFNDPLWEKQ WYLHDDREDL SESKKDLHVI PAWKKGYTGK
GITVSILDDG LERLHTDLAD NYSPEASYDY NGDDDDPTPR YDPTNENKHG TRCAGEVAMI
ANNGKCGVGI AFNAKIGGIR MLDGEVTDTL EGQALQHAID VVDIFSASWG PNDDGNTLEG
PGKLAHKAFE NGVTEGRKGK GVIYVWASGN GGRLYDNCDC DGYTGSIYTL SISSASQVFK
RPWYGELCAS TMGTTYSSGS AIDDRISTDL NDTCTKSHTG TSAAAPLAAG IIALLLESNP
DLTWRDVQHL VTWTSQAGPL IQQSKSGWTR NGAGFLVNTA FGFGILDTAG LIDAAEKKTW
KSVPKQMKCT INSTSKSNLP HNQRLEIQIY SSGCEGQENE INYIEHVQLH LTLDYTKRGA
ISVHITSPSN TTTMLLSERP YDKSTKGFQS WPLMSVHNWG EDPKGTWKVV LEDTTDDKNN
GILQDLRLVI YGTTEQPHHM RHGPRKYIGN YNHVQNKEQV GISQKKLPKQ QRQFSFIDIN
SQKSDPNNKT VFVCRLGLHY QQGTTRCKYG INFMV
//
