SPP2B_CHICK
ID SPP2B_CHICK Reviewed; 596 AA.
AC Q5F383;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Signal peptide peptidase-like 2B {ECO:0000250|UniProtKB:Q8TCT7};
DE Short=SPP-like 2B {ECO:0000250|UniProtKB:Q8TCT7};
DE Short=SPPL2b {ECO:0000250|UniProtKB:Q8TCT7};
DE EC=3.4.23.-;
DE Flags: Precursor;
GN Name=SPPL2B {ECO:0000250|UniProtKB:Q8TCT7}; ORFNames=RCJMB04_29c5;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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:0000250|UniProtKB:Q8TCT7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q3TD49};
CC Multi-pass membrane protein {ECO:0000305}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8TCT7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8TCT7}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q8TCT7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8TCT7}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q8TCT7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8TCT7}. Membrane
CC {ECO:0000250|UniProtKB:Q8TCT7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8TCT7}; Lumenal side
CC {ECO:0000250|UniProtKB:Q8TCT7}.
CC -!- DOMAIN: The PAL motif is required for normal active site conformation.
CC The catalytic domains embedded in the membrane are in the opposite
CC orientation to that of the presenilin protein family; therefore, it is
CC predicted to cleave type II-oriented substrate peptides like the
CC prototypic protease SPP. {ECO:0000250|UniProtKB:P49768}.
CC -!- SIMILARITY: Belongs to the peptidase A22B family. {ECO:0000305}.
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DR EMBL; AJ851767; CAH65401.1; -; mRNA.
DR RefSeq; NP_001026104.1; NM_001030933.1.
DR AlphaFoldDB; Q5F383; -.
DR STRING; 9031.ENSGALP00000000586; -.
DR MEROPS; A22.004; -.
DR PaxDb; Q5F383; -.
DR PRIDE; Q5F383; -.
DR GeneID; 420056; -.
DR KEGG; gga:420056; -.
DR CTD; 162540; -.
DR VEuPathDB; HostDB:geneid_420056; -.
DR eggNOG; KOG2442; Eukaryota.
DR InParanoid; Q5F383; -.
DR OrthoDB; 535101at2759; -.
DR PhylomeDB; Q5F383; -.
DR PRO; PR:Q5F383; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030660; C:Golgi-associated vesicle membrane; ISS:UniProtKB.
DR GO; GO:0071458; C:integral component of cytoplasmic side of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISS:UniProtKB.
DR GO; GO:0031293; P:membrane protein intracellular domain proteolysis; ISS:UniProtKB.
DR GO; GO:0033619; P:membrane protein proteolysis; IBA:GO_Central.
DR GO; GO:0050776; P:regulation of immune response; ISS:UniProtKB.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007369; Peptidase_A22B_SPP.
DR InterPro; IPR006639; Preselin/SPP.
DR InterPro; IPR033149; SPPL2B.
DR PANTHER; PTHR12174; PTHR12174; 1.
DR PANTHER; PTHR12174:SF39; PTHR12174:SF39; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04258; Peptidase_A22B; 1.
DR SMART; SM00730; PSN; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Endosome; Glycoprotein; Golgi apparatus; Hydrolase;
KW Lysosome; Membrane; Protease; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000250|UniProtKB:Q8TCT7"
FT CHAIN 22..596
FT /note="Signal peptide peptidase-like 2B"
FT /id="PRO_0000236078"
FT TOPO_DOM 22..170
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q8TCT7"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..242
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..315
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..408
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q8TCT7"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..466
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..596
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8TCT7"
FT DOMAIN 53..147
FT /note="PA"
FT REGION 543..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 468..470
FT /note="PAL"
FT COMPBIAS 575..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 355
FT /evidence="ECO:0000250|UniProtKB:P49810"
FT ACT_SITE 417
FT /evidence="ECO:0000250|UniProtKB:P49810"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 596 AA; 66397 MW; C531CDB848532ADD CRC64;
MAARWAQFLL FSLLSLPQVY CEYGMVHVLS EKGSSKGKDY CILFNSQWAH LPHDLGKASL
LQLQDQTASV LCSPSDVPDG GFNNRIPMVM RGNCTFYEKV RLAQINGARG LLIVSRERLV
PPGGNRSQYE EIDIPVALLS YSDMLDIVKS FGRSVKGAMY APNEPVLDYN MVIIFVMAVG
TVAIGGYWAG SRDVKERYMK HKRDDGAEKH EDETVDVTPI MICVFVVMCC SMLVLLYFFY
DHLVYVIIGI FCLAASIGLY SCLSPFVRRF PLGKCRIPDN NLPYFHKRPQ VRILLLAVFC
ISVSVVWGVF RNEDQWAWVL QDALGIAFCL YMLKTIRLPT FKGCTLLLLV LFVYDVFFVF
ITPFLTKTGE SIMVEVAAGP SDSATHEKLP MVLKVPRLNS SPLALCDRPF SLLGFGDILV
PGLLVAYCHR FDIQVQSSRV YFVACTIAYG IGLLVTFVAL ALMQMGQPAL LYLVPCTLIT
SFSVALWRKE LAMFWTGSGF AKDLPQPPLV IASVNCPQLP KDSNVPASQQ ETEEMANPTL
HVKELHSPTL AAEEPADNDT KTEQSEVSIA QSEEAAGHNK DDLESKSLNL EQKQLE
