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Database: UniProt
Entry: A0A3Q7TCP4_VULVU
LinkDB: A0A3Q7TCP4_VULVU
Original site: A0A3Q7TCP4_VULVU 
ID   A0A3Q7TCP4_VULVU        Unreviewed;       558 AA.
AC   A0A3Q7TCP4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Signal peptide peptidase-like 2B isoform X1 {ECO:0000313|RefSeq:XP_025875004.1};
GN   Name=SPPL2B {ECO:0000313|RefSeq:XP_025875004.1};
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025875004.1};
RN   [1]
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_025875004.1}
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025875004.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025875004.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004337}. Lysosome membrane
CC       {ECO:0000256|ARBA:ARBA00004155}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004155}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004366}; Multi-pass membrane protein
CC       {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_025875004.1; XM_026019219.1.
DR   AlphaFoldDB; A0A3Q7TCP4; -.
DR   STRING; 9627.ENSVVUP00000003434; -.
DR   KEGG; vvp:112935485; -.
DR   OrthoDB; 907832at2759; -.
DR   Proteomes; UP000286640; Unplaced.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
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; 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:SF39; SIGNAL PEPTIDE PEPTIDASE-LIKE 2B; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        145..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        193..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        221..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        267..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        292..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        321..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        386..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        416..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        445..463
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          48..122
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   REGION          482..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..501
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   558 AA;  61308 MW;  E58F2785E688E7CF CRC64;
     MVHVVSETGG PRGKDYCILY NPQWAHLPHD LGKASLLQLR DWTASVLCSP PDLPTKGFSN
     QIPLVARGNC TFYEKVRLAQ GGGARGLLIV SKETLVPPGG NKTQYEEIGI PVALLSYRDM
     LDIFKNFGRA VRAALYAPNE PMLDYNMVII FVMAVGTVAL GGYWAGSRDV KKRYMKHKRD
     DGPEKQEDEA VDVTPVMICV FVVMCCSMLV LLYYFYDQLV YVIIGIFCLS SSTGLYSCLA
     PLVQRLPFGR CRVPDNSLPY FHKRPRVSML LLALLCLAVS VVWGIFRNED QWAWVLQDAL
     GVAFCLYMLK TIRLPTFKAC TLLLLVLFVY DVFFVFITPF LTKSGNSIMV EVATGPSDSA
     THEKLPMVLK VPRLNASPLA LCDRPFSLLG FGDILVPGLL VAYCHRFDIQ VQSSRVYFVA
     CTVAYGIGLL VTFMALALMQ RGQPALLYLV PCTLITSCAL ALWRRELGMF WTGSGFVKDL
     PQSPWAPSSA DSPQPRKDSD TGLSQPPPGE ELAKCPLPHG QPPELSVPEE TGAGASPQEP
     VSPEGHAPEP VSVVGTSA
//
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