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 10-JUN-2026, entry version 173. 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 P67812; P61009: SPCS3; NbExp=7; IntAct=EBI-1042500, EBI-6166040; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_001271918.2. [P67812-2] DR RefSeq; NP_001258848.1; NM_001271919.1. DR RefSeq; NP_001258849.1; NM_001271920.2. [P67812-4] DR RefSeq; NP_001258850.1; NM_001271921.1. DR RefSeq; NP_001258851.1; NM_001271922.2. [P67812-3] DR RefSeq; NP_055115.1; NM_014300.4. [P67812-1] DR RefSeq; XP_054233621.1; XM_054377646.1. [P67812-1] DR RefSeq; XP_054233622.1; XM_054377647.1. [P67812-1] DR RefSeq; XP_054233623.1; XM_054377648.1. [P67812-1] DR PDB; 7P2P; EM; 4.90 A; A=1-179. DR PDBsum; 7P2P; -. DR AlphaFoldDB; P67812; -. DR EMDB; EMD-13171; -. DR SMR; P67812; -. DR BioGRID; 117037; 153. DR ComplexPortal; CPX-2847; Signal peptidase complex, SEC11A variant. DR DIP; DIP-50359N; -. DR FunCoup; P67812; 1391. DR IntAct; P67812; 83. DR MINT; P67812; -. DR NDEx; IQUERY-CP-SEC11A; 1 NDEx IQuery Curated Pathway. DR ChEMBL; CHEMBL5725033; -. 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 jPOST; P67812; -. DR MassIVE; P67812; -. DR PeptideAtlas; P67812; -. DR ProteomicsDB; 39571; -. DR ProteomicsDB; 39580; -. DR ProteomicsDB; 5197; -. DR ProteomicsDB; 57523; -. [P67812-1] DR Pumba; P67812; -. DR TopDownProteomics; P67812-1; -. [P67812-1] DR Antibodypedia; 43614; 185 antibodies from 24 providers. DR DNASU; 23478; -. DR Ensembl; ENST00000268220.12; ENSP00000268220.7; ENSG00000140612.15. [P67812-1] DR Ensembl; ENST00000455959.7; ENSP00000413121.3; ENSG00000140612.15. [P67812-2] DR Ensembl; ENST00000558134.5; ENSP00000452697.1; ENSG00000140612.15. [P67812-3] DR Ensembl; ENST00000560266.5; ENSP00000452684.1; ENSG00000140612.15. [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 AGR; HGNC:17718; -. DR ClinPGx; PA162402586; -. 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 OpenTargets; ENSG00000140612; -. DR VEuPathDB; HostDB:ENSG00000140612; -. DR eggNOG; KOG3342; Eukaryota. DR GeneTree; ENSGT00390000015600; -. DR HOGENOM; CLU_089996_0_0_1; -. DR InParanoid; P67812; -. DR OMA; ILMNEYP; -. DR OrthoDB; 10257561at2759; -. DR PAN-GO; P67812; 3 GO annotations based on evolutionary models. DR PhylomeDB; P67812; -. 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 Reactome; R-HSA-9768727; Regulation of CDH1 posttranslational processing and trafficking to plasma membrane. DR Reactome; R-HSA-9828806; Maturation of hRSV A proteins. DR Reactome; R-HSA-9918432; Maturation of DENV proteins. DR SignaLink; P67812; -. DR Agora; ENSG00000140612; -. DR BioGRID-ORCS; 23478; 26 hits in 1152 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 211 other cell types or tissues. DR ExpressionAtlas; P67812; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ComplexPortal. 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:0009003; F:signal peptidase activity; IEA:UniProtKB-EC. DR GO; GO:0009615; P:response to virus; TAS:Reactome. DR GO; GO:0006465; P:signal peptide processing; IDA:UniProtKB. DR CDD; cd06530; S26_SPase_I; 1. DR FunFam; 2.10.109.10:FF:000003; Signal peptidase complex catalytic subunit SEC11; 1. DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 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 NCBIfam; TIGR02228; sigpep_I_arch; 1. DR PANTHER; PTHR10806; SIGNAL PEPTIDASE COMPLEX CATALYTIC SUBUNIT SEC11; 1. DR PANTHER; PTHR10806:SF28; SIGNAL PEPTIDASE COMPLEX CATALYTIC SUBUNIT SEC11B-RELATED; 1. DR Pfam; PF00717; Peptidase_S24; 1. DR PRINTS; PR00728; SIGNALPTASE. DR SUPFAM; SSF51306; LexA/Signal peptidase; 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; Proteomics identification; Reference proteome; KW Signal-anchor; Transmembrane; 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 //