SC11A_HUMAN
ID SC11A_HUMAN Reviewed; 179 AA.
AC P67812; B2RAD7; B4DUL4; H0YK72; H0YK83; O75957; P21378; Q53FQ8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Signal peptidase complex catalytic subunit SEC11A;
DE EC=3.4.21.89 {ECO:0000269|PubMed:34388369};
DE AltName: Full=Endopeptidase SP18;
DE AltName: Full=Microsomal signal peptidase 18 kDa subunit;
DE Short=SPase 18 kDa subunit;
DE AltName: Full=SEC11 homolog A;
DE AltName: Full=SEC11-like protein 1;
DE AltName: Full=SPC18;
GN Name=SEC11A; Synonyms=SEC11L1, SPC18, SPCS4A;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Hepatoma;
RA Xie T.P., Wu M.C., Liu X.P., Wang H.J., Liang Y., Guo Y.J.;
RT "Human signal peptidase 18 kDa subunit, mRNA complete cds.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zhang J., Mao M., Liu T., Wu J., Zhang Q., Fu G., Shen Y., Zhou J., Yu Y.,
RA Wang Z., Chen S., Chen Z.;
RT "Human microsomal signal peptidase.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Neuroblastoma, and Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Gastric mucosa;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-179.
RC TISSUE=Hepatoma;
RA Xie T.P., Liu X.P., Wang H.J., Liang Y., Wang H., Qian W.Z., Wei L.X.,
RA Liu Y.J., He P., Guo Y.J.;
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14] {ECO:0007744|PDB:7P2P}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.9 ANGSTROMS), FUNCTION, CATALYTIC
RP ACTIVITY, IDENTIFICATION IN THE SIGNAL PEPTIDASE COMPLEX, DOMAIN, ACTIVE
RP SITE, AND MUTAGENESIS OF SER-56; ARG-97; ASP-116; ASP-121 AND ASP-122.
RX PubMed=34388369; DOI=10.1016/j.molcel.2021.07.031;
RA Liaci A.M., Steigenberger B., Telles de Souza P.C., Tamara S.,
RA Groellers-Mulderij M., Ogrissek P., Marrink S.J., Scheltema R.A.,
RA Foerster F.;
RT "Structure of the human signal peptidase complex reveals the determinants
RT for signal peptide cleavage.";
RL Mol. Cell 81:3934-3948.e11(2021).
CC -!- FUNCTION: Catalytic component of the signal peptidase complex (SPC)
CC which catalyzes the cleavage of N-terminal signal sequences from
CC nascent proteins as they are translocated into the lumen of the
CC endoplasmic reticulum (PubMed:34388369). Specifically cleaves N-
CC terminal signal peptides that contain a hydrophobic alpha-helix (h-
CC region) shorter than 18-20 amino acids (PubMed:34388369).
CC {ECO:0000269|PubMed:34388369}.
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 Evidence={ECO:0000269|PubMed:34388369};
CC -!- SUBUNIT: Component of the signal peptidase complex paralog A (SPC-A)
CC composed of a catalytic subunit SEC11A and three accessory subunits
CC SPCS1, SPCS2 and SPCS3 (PubMed:34388369). Within the complex, interacts
CC with SPCS2 and SPCS3 (PubMed:34388369). The complex induces a local
CC thinning of the ER membrane which is used to measure the length of the
CC signal peptide (SP) h-region of protein substrates (PubMed:34388369).
CC This ensures the selectivity of the complex towards h-regions shorter
CC than 18-20 amino acids (PubMed:34388369).
CC {ECO:0000269|PubMed:34388369}.
CC -!- INTERACTION:
CC P67812; Q08AM2: ADAM33; NbExp=3; IntAct=EBI-1042500, EBI-10225815;
CC P67812; P06276: BCHE; NbExp=3; IntAct=EBI-1042500, EBI-7936069;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P67811}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P67811}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P67812-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P67812-2; Sequence=VSP_055052;
CC Name=3;
CC IsoId=P67812-3; Sequence=VSP_055053;
CC Name=4;
CC IsoId=P67812-4; Sequence=VSP_055054, VSP_055055;
CC -!- DOMAIN: The C-terminal short (CTS) helix is essential for catalytic
CC activity (PubMed:34388369). It may be accommodated as a transmembrane
CC helix in the thinned membrane environment of the complex, similarly to
CC the signal peptide in the complex substrates (Probable).
CC {ECO:0000269|PubMed:34388369, ECO:0000305|PubMed:34388369}.
CC -!- SIMILARITY: Belongs to the peptidase S26B family. {ECO:0000305}.
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DR EMBL; AF108945; AAD19640.1; -; mRNA.
DR EMBL; AF061737; AAD17526.1; -; mRNA.
DR EMBL; AK300693; BAG62376.1; -; mRNA.
DR EMBL; AK314146; BAG36834.1; -; mRNA.
DR EMBL; AK223224; BAD96944.1; -; mRNA.
DR EMBL; AC087732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC115102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471101; EAX01952.1; -; Genomic_DNA.
DR EMBL; CH471101; EAX01954.1; -; Genomic_DNA.
DR EMBL; CH471101; EAX01956.1; -; Genomic_DNA.
DR EMBL; BC000359; AAH00359.3; -; mRNA.
DR EMBL; BC014508; AAH14508.1; -; mRNA.
DR EMBL; AF090315; AAC36354.1; -; mRNA.
DR CCDS; CCDS45340.1; -. [P67812-1]
DR CCDS; CCDS61742.1; -. [P67812-2]
DR CCDS; CCDS61743.1; -. [P67812-3]
DR CCDS; CCDS61744.1; -. [P67812-4]
DR RefSeq; NP_001258847.1; NM_001271918.1. [P67812-2]
DR RefSeq; NP_001258848.1; NM_001271919.1.
DR RefSeq; NP_001258849.1; NM_001271920.1. [P67812-4]
DR RefSeq; NP_001258850.1; NM_001271921.1.
DR RefSeq; NP_001258851.1; NM_001271922.1. [P67812-3]
DR RefSeq; NP_055115.1; NM_014300.3. [P67812-1]
DR PDB; 7P2P; EM; 4.90 A; A=1-179.
DR PDBsum; 7P2P; -.
DR AlphaFoldDB; P67812; -.
DR SMR; P67812; -.
DR BioGRID; 117037; 125.
DR ComplexPortal; CPX-2847; Signal peptidase complex, SEC11A variant.
DR DIP; DIP-50359N; -.
DR IntAct; P67812; 27.
DR MINT; P67812; -.
DR STRING; 9606.ENSP00000452697; -.
DR MEROPS; S26.009; -.
DR GlyGen; P67812; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P67812; -.
DR MetOSite; P67812; -.
DR PhosphoSitePlus; P67812; -.
DR SwissPalm; P67812; -.
DR BioMuta; SEC11A; -.
DR DMDM; 54039634; -.
DR EPD; P67812; -.
DR jPOST; P67812; -.
DR MassIVE; P67812; -.
DR MaxQB; P67812; -.
DR PaxDb; P67812; -.
DR PeptideAtlas; P67812; -.
DR PRIDE; P67812; -.
DR ProteomicsDB; 39571; -.
DR ProteomicsDB; 39580; -.
DR ProteomicsDB; 5197; -.
DR ProteomicsDB; 57523; -. [P67812-1]
DR TopDownProteomics; P67812-1; -. [P67812-1]
DR Antibodypedia; 43614; 196 antibodies from 24 providers.
DR DNASU; 23478; -.
DR Ensembl; ENST00000268220.12; ENSP00000268220.7; ENSG00000140612.14. [P67812-1]
DR Ensembl; ENST00000455959.7; ENSP00000413121.3; ENSG00000140612.14. [P67812-2]
DR Ensembl; ENST00000558134.5; ENSP00000452697.1; ENSG00000140612.14. [P67812-3]
DR Ensembl; ENST00000560266.5; ENSP00000452684.1; ENSG00000140612.14. [P67812-4]
DR GeneID; 23478; -.
DR KEGG; hsa:23478; -.
DR MANE-Select; ENST00000268220.12; ENSP00000268220.7; NM_014300.4; NP_055115.1.
DR UCSC; uc002blb.3; human. [P67812-1]
DR CTD; 23478; -.
DR DisGeNET; 23478; -.
DR GeneCards; SEC11A; -.
DR HGNC; HGNC:17718; SEC11A.
DR HPA; ENSG00000140612; Low tissue specificity.
DR MIM; 618258; gene.
DR neXtProt; NX_P67812; -.
DR OpenTargets; ENSG00000140612; -.
DR PharmGKB; PA162402586; -.
DR VEuPathDB; HostDB:ENSG00000140612; -.
DR eggNOG; KOG3342; Eukaryota.
DR GeneTree; ENSGT00390000015600; -.
DR HOGENOM; CLU_089996_0_0_1; -.
DR InParanoid; P67812; -.
DR OMA; YNVRGKD; -.
DR OrthoDB; 1486616at2759; -.
DR PhylomeDB; P67812; -.
DR TreeFam; TF313648; -.
DR PathwayCommons; P67812; -.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
DR Reactome; R-HSA-400511; Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
DR Reactome; R-HSA-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR SignaLink; P67812; -.
DR BioGRID-ORCS; 23478; 26 hits in 1074 CRISPR screens.
DR ChiTaRS; SEC11A; human.
DR GenomeRNAi; 23478; -.
DR Pharos; P67812; Tbio.
DR PRO; PR:P67812; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P67812; protein.
DR Bgee; ENSG00000140612; Expressed in germinal epithelium of ovary and 209 other tissues.
DR ExpressionAtlas; P67812; baseline and differential.
DR Genevisible; P67812; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005787; C:signal peptidase complex; IDA:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0006465; P:signal peptide processing; IDA:UniProtKB.
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; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR InterPro; IPR019533; Peptidase_S26.
DR InterPro; IPR001733; Peptidase_S26B.
DR InterPro; IPR037712; SEC11A.
DR PANTHER; PTHR10806; PTHR10806; 1.
DR PANTHER; PTHR10806:SF28; PTHR10806:SF28; 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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Endoplasmic reticulum; Hydrolase;
KW Membrane; Protease; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..179
FT /note="Signal peptidase complex catalytic subunit SEC11A"
FT /id="PRO_0000109543"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P67811"
FT TRANSMEM 17..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..179
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P67811"
FT REGION 165..176
FT /note="C-terminal short (CTS) helix"
FT /evidence="ECO:0000269|PubMed:34388369"
FT ACT_SITE 56
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:34388369"
FT ACT_SITE 96
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:34388369"
FT ACT_SITE 122
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:34388369"
FT VAR_SEQ 1..26
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055052"
FT VAR_SEQ 145..179
FT /note="FVPYIGIVTILMNDYPKFKYAVLFLLGLFVLVHRE -> MQFSFCWVYSCWF
FT IVSKKPALLFLGRCHSFRYWMFGVDTGL (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_055053"
FT VAR_SEQ 146..164
FT /note="VPYIGIVTILMNDYPKFKY -> YQENSSVEDRNYLFLILEL (in
FT isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_055054"
FT VAR_SEQ 165..179
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_055055"
FT MUTAGEN 56
FT /note="S->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:34388369"
FT MUTAGEN 97
FT /note="R->D: Slight reduction in catalytic activity; when
FT associated with R-116."
FT /evidence="ECO:0000269|PubMed:34388369"
FT MUTAGEN 116
FT /note="D->N: Moderate reduction in catalytic activity.
FT Reduces protein stability."
FT /evidence="ECO:0000269|PubMed:34388369"
FT MUTAGEN 116
FT /note="D->R: Slight reduction in catalytic activity; when
FT associated with D-97."
FT /evidence="ECO:0000269|PubMed:34388369"
FT MUTAGEN 121
FT /note="D->N: No effect on catalytic activity or protein
FT stability."
FT /evidence="ECO:0000269|PubMed:34388369"
FT MUTAGEN 122
FT /note="D->N: Loss of catalytic activity. Slight reduction
FT in protein stability."
FT /evidence="ECO:0000269|PubMed:34388369"
FT CONFLICT 19
FT /note="Y -> C (in Ref. 1; AAD19640 and 7; AAC36354)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="I -> T (in Ref. 4; BAD96944)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="K -> R (in Ref. 1; AAD19640 and 7; AAC36354)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 179 AA; 20625 MW; DFD245A17BA3B47F CRC64;
MLSLDFLDDV RRMNKRQLYY QVLNFGMIVS SALMIWKGLM VITGSESPIV VVLSGSMEPA
FHRGDLLFLT NRVEDPIRVG EIVVFRIEGR EIPIVHRVLK IHEKQNGHIK FLTKGDNNAV
DDRGLYKQGQ HWLEKKDVVG RARGFVPYIG IVTILMNDYP KFKYAVLFLL GLFVLVHRE
