ID A0A3Q3BDM2_KRYMA Unreviewed; 530 AA.
AC A0A3Q3BDM2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Signal peptide peptidase-like 2A {ECO:0000313|Ensembl:ENSKMAP00000022779.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000022779.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000022779.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004366}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004366}; Lumenal side
CC {ECO:0000256|ARBA:ARBA00004366}.
CC -!- SIMILARITY: Belongs to the peptidase A22B family.
CC {ECO:0000256|ARBA:ARBA00006859}.
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DR RefSeq; XP_017274254.1; XM_017418765.1.
DR AlphaFoldDB; A0A3Q3BDM2; -.
DR STRING; 37003.ENSKMAP00000022779; -.
DR Ensembl; ENSKMAT00000023069.1; ENSKMAP00000022779.1; ENSKMAG00000016902.1.
DR GeneID; 108237385; -.
DR KEGG; kmr:108237385; -.
DR GeneTree; ENSGT00940000157722; -.
DR OMA; QWGPCHF; -.
DR OrthoDB; 907832at2759; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProt.
DR GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; IEA:InterPro.
DR CDD; cd02129; PA_hSPPL_like; 1.
DR Gene3D; 3.50.30.30; -; 1.
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:SF34; SIGNAL PEPTIDE PEPTIDASE-LIKE 2A; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04258; Peptidase_A22B; 1.
DR SMART; SM00730; PSN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
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..530
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018745333"
FT TRANSMEM 169..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 287..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 422..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 455..478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 484..502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 59..142
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
SQ SEQUENCE 530 AA; 57501 MW; DD1060A7E22560F9 CRC64;
MDPKGAFGVA LLSVVFFTSE VKGQEAILRV SSGDSYREYC IVHNHSWTPL SPTLDAATQY
PLVNLTSTLL CNASGVNPEA VKGKAVVVMR GECDFSQKAL VAQNLSASAL LIASTNSLIT
PSANESEYPK VKIPLALMRY RDFLEAKQVF GDGMGVKLYA PPYSKIDPSI AVILLISVVT
ITLGGFWSGA CEREKLNSCA GGGGGGGGKG KASSGELSLY SPLKVFIFVA LMCGMLVLMY
YFYNILVYVI IVIFCLASAS ALFSCLDAVM DKLGCGTLSV SVRDKSISVR SVLLAAACIS
IVVVWGVYRN EDRWIWILQD LLGIAFCLNF MKTISLSNFK ICVILLSLLL VYDVFFVFIT
PFFTKNGVSI MVQVALGPDA AGEKTQGNVV EIPAEPQPPS EKLPVVMRVP RFSAWAQNLC
GMQFSILGYG DIIVPGLLVA YCSRFDVWVN SRKKIYFISC CIAYFLGMIL TFVVMLLSGM
GQPALLYLVP FTLITSAVVA GCRGEMRQFW SGTTYEVLDS PREPLLPGKN
//
