SC11B_HUMAN
ID SC11B_HUMAN Reviewed; 166 AA.
AC P0C7V7;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Putative signal peptidase complex catalytic subunit SEC11B;
DE EC=3.4.21.89;
DE AltName: Full=SEC11 homolog B;
DE AltName: Full=SEC11-like protein 2;
GN Name=SEC11B; Synonyms=SEC11L2, SPCS4B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
CC -!- FUNCTION: Putative component of some signal peptidase complex which
CC removes signal peptides from nascent proteins as they are translocated
CC into the lumen of the endoplasmic reticulum. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences
CC from secreted and periplasmic proteins.; EC=3.4.21.89;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S26B family. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR EMBL; AC091076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0C7V7; -.
DR SMR; P0C7V7; -.
DR MEROPS; S26.022; -.
DR iPTMnet; P0C7V7; -.
DR PhosphoSitePlus; P0C7V7; -.
DR BioMuta; HGNC:31884; -.
DR DMDM; 206557848; -.
DR EPD; P0C7V7; -.
DR jPOST; P0C7V7; -.
DR MassIVE; P0C7V7; -.
DR MaxQB; P0C7V7; -.
DR PeptideAtlas; P0C7V7; -.
DR PRIDE; P0C7V7; -.
DR ProteomicsDB; 52377; -.
DR GeneCards; SEC11B; -.
DR HGNC; HGNC:31884; SEC11B.
DR neXtProt; NX_P0C7V7; -.
DR InParanoid; P0C7V7; -.
DR SignaLink; P0C7V7; -.
DR ChiTaRS; SEC11B; human.
DR Pharos; P0C7V7; Tdark.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; P0C7V7; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005787; C:signal peptidase complex; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
DR CDD; cd06530; S26_SPase_I; 1.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR InterPro; IPR019533; Peptidase_S26.
DR InterPro; IPR001733; Peptidase_S26B.
DR PANTHER; PTHR10806; PTHR10806; 1.
DR Pfam; PF00717; Peptidase_S24; 1.
DR PRINTS; PR00728; SIGNALPTASE.
DR SUPFAM; SSF51306; SSF51306; 1.
DR TIGRFAMs; TIGR02228; sigpep_I_arch; 1.
DR PROSITE; PS00501; SPASE_I_1; 1.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 5: Uncertain;
KW Hydrolase; Membrane; Protease; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..166
FT /note="Putative signal peptidase complex catalytic subunit
FT SEC11B"
FT /id="PRO_0000344461"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..166
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 43
FT /evidence="ECO:0000250"
SQ SEQUENCE 166 AA; 19160 MW; 64C26E8B71A2BF00 CRC64;
MNKWRLYYQV LNFGMIVSSA LMIWKGLMVI TGSESPIVLL SGSMEPAFHR GYLLFLTNRV
EDPIRVGEIA VLRIEGRKIP IVHRVLKIHE KQNGHIKFLT KGDNNAVDDR GLYKQDQHWL
EKKDVVGRAR GFVPYIGIGT SLMNDYPKHK YEVLFLLGLF VLVHRE
