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Database: UniProt
Entry: B9RDT1_RICCO
LinkDB: B9RDT1_RICCO
Original site: B9RDT1_RICCO 
ID   B9RDT1_RICCO            Unreviewed;       538 AA.
AC   B9RDT1;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   SubName: Full=Minor histocompatibility antigen H13, putative {ECO:0000313|EMBL:EEF50539.1};
GN   ORFNames=RCOM_1615650 {ECO:0000313|EMBL:EEF50539.1};
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN   [1] {ECO:0000313|Proteomes:UP000008311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX   PubMed=20729833; DOI=10.1038/nbt.1674;
RA   Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA   Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA   Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA   Rabinowicz P.D.;
RT   "Draft genome sequence of the oilseed species Ricinus communis.";
RL   Nat. Biotechnol. 28:951-956(2010).
CC   -!- FUNCTION: Intramembrane-cleaving aspartic protease (I-CLiP) that
CC       cleaves type II membrane signal peptides in the hydrophobic plane of
CC       the membrane. {ECO:0000256|ARBA:ARBA00003012}.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004337}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase A22B family.
CC       {ECO:0000256|ARBA:ARBA00006859}.
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DR   EMBL; EQ973775; EEF50539.1; -; Genomic_DNA.
DR   RefSeq; XP_002511870.1; XM_002511824.2.
DR   AlphaFoldDB; B9RDT1; -.
DR   STRING; 3988.B9RDT1; -.
DR   MEROPS; A22.A05; -.
DR   GeneID; 8261889; -.
DR   KEGG; rcu:8261889; -.
DR   eggNOG; KOG2442; Eukaryota.
DR   InParanoid; B9RDT1; -.
DR   OrthoDB; 51438at2759; -.
DR   Proteomes; UP000008311; Unassembled WGS sequence.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030660; C:Golgi-associated vesicle membrane; IBA:GO_Central.
DR   GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
DR   GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; IBA:GO_Central.
DR   GO; GO:0033619; P:membrane protein proteolysis; IBA:GO_Central.
DR   Gene3D; 3.50.30.30; -; 1.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR007369; Peptidase_A22B_SPP.
DR   InterPro; IPR006639; Preselin/SPP.
DR   PANTHER; PTHR12174; SIGNAL PEPTIDE PEPTIDASE; 1.
DR   PANTHER; PTHR12174:SF102; SIGNAL PEPTIDE PEPTIDASE-LIKE 4; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF04258; Peptidase_A22B; 1.
DR   SMART; SM00730; PSN; 1.
DR   SUPFAM; SSF52025; PA domain; 1.
PE   3: Inferred from homology;
KW   Endosome {ECO:0000256|ARBA:ARBA00022753};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..538
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002890737"
FT   TRANSMEM        193..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        243..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        278..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        315..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        345..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        372..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        427..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        461..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        488..507
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          83..166
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
SQ   SEQUENCE   538 AA;  59452 MW;  10804DA3FE7325C0 CRC64;
     MEIKLSIYLI VSVLALSPCY GSASDIVHHD DVAPKRPGCN NDFVLVKVAT WVDGIENIEY
     VGVGARFGPT LESKEKRANK TRLVLADPPD LCILPKNKLN RDVILVRRGN CSFTTKSNIA
     EEANASAILI INYRTELFKM VCEANEADVI IGIPAVMLPQ DAGASLEHYV KNSSTVSVQL
     YSPQRPLVDV AEVFLWLMAV GTILGASYWS AWSAREVAIE QDKLLKDGSD DFQQTEGVPS
     SGVVNINITS AVLFVVVASC FLVMLYKLMS LWFMDVLVVL FCIGGTEGLQ TCLVALLSCF
     RCFQHAGESF IKVPFFGAVS HLTLAVSPFC IAFAVVWAVY RRVSFAWIGQ DILGITLIIT
     VLQIVHVPNL KVGTVLLSCA FLYDIFWVFV SKLWFKESVM IVVARGDKSG EDGIPMLLKI
     PRMFDPWGGY SIIGFGDIIL PGLLVAFALR YDWLTKKNLR AGYFLWAMTA YGLGLLITYV
     ALNMMDGHGQ PALLYIVPFT LGTFLTLGKK RGELKALWTR GAPERPCPHI RFQPPQSQ
//
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