ATG4B_MOUSE
ID ATG4B_MOUSE Reviewed; 393 AA.
AC Q8BGE6; Q6ZQ22; Q8R098;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Cysteine protease ATG4B {ECO:0000305};
DE EC=3.4.22.- {ECO:0000269|PubMed:14530254, ECO:0000269|PubMed:29458288};
DE AltName: Full=AUT-like 1 cysteine endopeptidase;
DE AltName: Full=Autophagy-related cysteine endopeptidase 1 {ECO:0000303|PubMed:12446702};
DE Short=Autophagin-1 {ECO:0000303|PubMed:12446702};
DE AltName: Full=Autophagy-related protein 4 homolog B {ECO:0000303|PubMed:14530254};
DE Short=MmAPG4B {ECO:0000303|PubMed:29458288};
GN Name=Atg4b {ECO:0000303|PubMed:20577052, ECO:0000312|MGI:MGI:1913865};
GN Synonyms=Apg4b {ECO:0000303|PubMed:14530254}, Autl1,
GN Kiaa0943 {ECO:0000303|PubMed:14621295};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RETRACTED PAPER.
RC STRAIN=BALB/cJ;
RX PubMed=12446702; DOI=10.1074/jbc.m208247200;
RA Marino G., Uria J.A., Puente X.S., Quesada V., Bordallo J., Lopez-Otin C.;
RT "Human autophagins, a family of cysteine proteinases potentially implicated
RT in cell degradation by autophagy.";
RL J. Biol. Chem. 278:3671-3678(2003).
RN [2]
RP RETRACTION NOTICE OF PUBMED:12446702.
RX PubMed=30808002; DOI=10.1074/jbc.w118.007325;
RA Marino G., Uria J.A., Puente X.S., Quesada V., Bordallo J., Lopez-Otin C.;
RL J. Biol. Chem. 294:1431-1431(2019).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas, Skin, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 128-393.
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14530254; DOI=10.1074/jbc.m308762200;
RA Hemelaar J., Lelyveld V.S., Kessler B.M., Ploegh H.L.;
RT "A single protease, Apg4B, is specific for the autophagy-related ubiquitin-
RT like proteins GATE-16, MAP1-LC3, GABARAP, and Apg8L.";
RL J. Biol. Chem. 278:51841-51850(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20577052; DOI=10.1172/jci42601;
RA Marino G., Fernandez A.F., Cabrera S., Lundberg Y.W., Cabanillas R.,
RA Rodriguez F., Salvador-Montoliu N., Vega J.A., Germana A., Fueyo A.,
RA Freije J.M., Lopez-Otin C.;
RT "Autophagy is essential for mouse sense of balance.";
RL J. Clin. Invest. 120:2331-2344(2010).
RN [9]
RP INTERACTION WITH GBP7.
RX PubMed=21551061; DOI=10.1126/science.1201711;
RA Kim B.H., Shenoy A.R., Kumar P., Das R., Tiwari S., MacMicking J.D.;
RT "A family of IFN-gamma-inducible 65-kD GTPases protects against bacterial
RT infection.";
RL Science 332:717-721(2011).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=20634410; DOI=10.1177/0300985810375810;
RA Read R., Savelieva K., Baker K., Hansen G., Vogel P.;
RT "Histopathological and neurological features of Atg4b knockout mice.";
RL Vet. Pathol. 48:486-494(2011).
RN [11]
RP UBIQUITINATION.
RX PubMed=23093945; DOI=10.1371/journal.pgen.1003007;
RA Kuang E., Okumura C.Y., Sheffy-Levin S., Varsano T., Shu V.C., Qi J.,
RA Niesman I.R., Yang H.J., Lopez-Otin C., Yang W.Y., Reed J.C., Broday L.,
RA Nizet V., Ronai Z.A.;
RT "Regulation of ATG4B stability by RNF5 limits basal levels of autophagy and
RT influences susceptibility to bacterial infection.";
RL PLoS Genet. 8:e1003007-e1003007(2012).
RN [12]
RP FUNCTION.
RX PubMed=29458288; DOI=10.1080/15548627.2018.1437341;
RA Kauffman K.J., Yu S., Jin J., Mugo B., Nguyen N., O'Brien A., Nag S.,
RA Lystad A.H., Melia T.J.;
RT "Delipidation of mammalian Atg8-family proteins by each of the four ATG4
RT proteases.";
RL Autophagy 14:992-1010(2018).
CC -!- FUNCTION: Cysteine protease that plays a key role in autophagy by
CC mediating both proteolytic activation and delipidation of ATG8 family
CC proteins (PubMed:14530254, PubMed:20577052, PubMed:29458288). Required
CC for canonical autophagy (macroautophagy), non-canonical autophagy as
CC well as for mitophagy (By similarity). The protease activity is
CC required for proteolytic activation of ATG8 family proteins: cleaves
CC the C-terminal amino acid of ATG8 proteins MAP1LC3A, MAP1LC3B,
CC MAP1LC3C, GABARAPL1, GABARAPL2 and GABARAP, to reveal a C-terminal
CC glycine (PubMed:14530254, PubMed:29458288). Exposure of the glycine at
CC the C-terminus is essential for ATG8 proteins conjugation to
CC phosphatidylethanolamine (PE) and insertion to membranes, which is
CC necessary for autophagy (PubMed:14530254, PubMed:29458288). Protease
CC activity is also required to counteract formation of high-molecular
CC weight conjugates of ATG8 proteins (ATG8ylation): acts as a
CC deubiquitinating-like enzyme that removes ATG8 conjugated to other
CC proteins, such as ATG3 (By similarity). In addition to the protease
CC activity, also mediates delipidation of ATG8 family proteins
CC (PubMed:29458288). Catalyzes delipidation of PE-conjugated forms of
CC ATG8 proteins during macroautophagy (By similarity). Also involved in
CC non-canonical autophagy, a parallel pathway involving conjugation of
CC ATG8 proteins to single membranes at endolysosomal compartments, by
CC catalyzing delipidation of ATG8 proteins conjugated to
CC phosphatidylserine (PS) (By similarity). Compared to other members of
CC the family (ATG4A, ATG4C or ATG4C), constitutes the major protein for
CC proteolytic activation of ATG8 proteins, while it displays weaker
CC delipidation activity than other ATG4 paralogs (PubMed:29458288).
CC Involved in phagophore growth during mitophagy independently of its
CC protease activity and of ATG8 proteins: acts by regulating ATG9A
CC trafficking to mitochondria and promoting phagophore-endoplasmic
CC reticulum contacts during the lipid transfer phase of mitophagy (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y4P1,
CC ECO:0000269|PubMed:14530254, ECO:0000269|PubMed:20577052,
CC ECO:0000269|PubMed:29458288}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-C-terminal L-amino acid-glycyl-
CC phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-
CC glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:67548, Rhea:RHEA-COMP:17323, Rhea:RHEA-COMP:17324,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:64612, ChEBI:CHEBI:172940,
CC ChEBI:CHEBI:172941; Evidence={ECO:0000250|UniProtKB:Q9Y4P1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67549;
CC Evidence={ECO:0000250|UniProtKB:Q9Y4P1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-C-terminal L-amino acid-glycyl-phosphatidylserine +
CC H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-
CC glycero-3-phospho-L-serine; Xref=Rhea:RHEA:67576, Rhea:RHEA-
CC COMP:17324, Rhea:RHEA-COMP:17326, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57262, ChEBI:CHEBI:172940, ChEBI:CHEBI:172942;
CC Evidence={ECO:0000250|UniProtKB:Q9Y4P1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67577;
CC Evidence={ECO:0000250|UniProtKB:Q9Y4P1};
CC -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide. Redox-regulated
CC during autophagy since reducing conditions activate ATG4A whereas an
CC oxidizing environment such as the presence of H(2)O(2) inhibits its
CC activity. The cysteine protease activity compounds is inhibited by
CC styrylquinoline compounds 4-28 and LV-320.
CC {ECO:0000250|UniProtKB:Q9Y4P1}.
CC -!- SUBUNIT: Interacts with PFKP; promoting phosphorylation of ATG4B at
CC Ser-34 (By similarity). Interacts with GBP7 (PubMed:21551061).
CC {ECO:0000250|UniProtKB:Q9Y4P1, ECO:0000269|PubMed:21551061}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14530254}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y4P1}. Cytoplasmic vesicle,
CC autophagosome {ECO:0000250|UniProtKB:Q9Y4P1}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9Y4P1}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9Y4P1}. Note=Mainly localizes to the cytoplasm,
CC including cytosol. A samll potion localizes to mitochondria;
CC phosphorylation at Ser-34 promotes localization to mitochondria.
CC {ECO:0000250|UniProtKB:Q9Y4P1}.
CC -!- DOMAIN: The LIR motif (LC3-interacting region) is required for the
CC interaction with ATG8 family proteins MAP1LC3A, MAP1LC3B, MAP1LC3C and
CC GABARAPL1. Required for proteolytic activation and delipidation of ATG8
CC proteins. {ECO:0000250|UniProtKB:Q9Y4P1}.
CC -!- PTM: Phosphorylation at Ser-383 and Ser-392 promotes autophagy by
CC increasing protein delipidation activity without affecting proteolytic
CC activation of ATG8 proteins. Phosphorylation at Ser-316 by ULK1
CC inhibits autophagy by decreasing both proteolytic activation and
CC delipidation activities. Phosphorylation at Ser-316 is dephosphorylated
CC by protein phosphatase 2A (PP2A). Phosphorylation at Ser-34 by AKT2
CC promotes its hydrolase activity, leading to increased proteolytic
CC activation and delipidation of ATG8 family proteins. Phosphorylation at
CC Ser-34 by AKT1 promotes mitochondrial localization and inhibition of
CC the F1F0-ATP synthase activity, leading to elevation of mitochondrial
CC reactive oxygen species (ROS). {ECO:0000250|UniProtKB:Q9Y4P1}.
CC -!- PTM: Ubiquitinated by RNF5, leading to its degradation by the
CC proteasome. {ECO:0000269|PubMed:23093945}.
CC -!- PTM: S-nitrosylation at Cys-189 and Cys-292 in response to high glucose
CC decreases both proteolytic activation and delipidation activities.
CC {ECO:0000250|UniProtKB:Q9Y4P1}.
CC -!- PTM: O-glycosylated by OGT, leading to increase protease activity,
CC thereby promoting the proteolytic activation of ATG8 family proteins.
CC {ECO:0000250|UniProtKB:Q9Y4P1}.
CC -!- PTM: Forms reversible intrachain disulfide bonds in response to
CC oxidative stress. Forms interchain disulfide bonds, leading to
CC formation of homooligomers in response to oxidation.
CC {ECO:0000250|UniProtKB:Q9Y4P1}.
CC -!- DISRUPTION PHENOTYPE: Mice develop normally but are born at a slightly
CC lower ratio than the expected Mendelian rate (PubMed:20577052,
CC PubMed:20634410). Cells display systemic reduction of autophagic
CC activity, characterized by defective proteolytic processing of ATG8
CC family proteins, compromising the rate of autophagosome maturation
CC (PubMed:20577052). Mice show severe balance disorders, which are caused
CC by defects in the development of otoconia (PubMed:20577052). The
CC central nervous system (CNS) of mutant mice also displays amorphous
CC globular bodies in the neuropil of the deep cerebellar nuclei and
CC adjacent vestibular nuclei (PubMed:20634410). The spheroid-like bodies
CC in the deep cerebellar and vestibular nuclei show heterogeneous
CC composition, characteristics of proteinaceous material
CC (PubMed:20634410). {ECO:0000269|PubMed:20577052,
CC ECO:0000269|PubMed:20634410}.
CC -!- SIMILARITY: Belongs to the peptidase C54 family. {ECO:0000305}.
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DR EMBL; AJ504653; CAD43220.1; -; mRNA.
DR EMBL; AK028712; BAC26079.1; -; mRNA.
DR EMBL; AK031570; BAC27455.1; -; mRNA.
DR EMBL; AK075796; BAC35965.1; -; mRNA.
DR EMBL; AK088811; BAC40587.1; -; mRNA.
DR EMBL; BC027184; AAH27184.1; -; mRNA.
DR EMBL; AK129242; BAC98052.1; -; mRNA.
DR CCDS; CCDS15195.1; -.
DR RefSeq; NP_777363.1; NM_174874.3.
DR AlphaFoldDB; Q8BGE6; -.
DR SMR; Q8BGE6; -.
DR BioGRID; 211597; 21.
DR STRING; 10090.ENSMUSP00000027502; -.
DR MEROPS; C54.003; -.
DR iPTMnet; Q8BGE6; -.
DR PhosphoSitePlus; Q8BGE6; -.
DR EPD; Q8BGE6; -.
DR jPOST; Q8BGE6; -.
DR MaxQB; Q8BGE6; -.
DR PaxDb; Q8BGE6; -.
DR PeptideAtlas; Q8BGE6; -.
DR PRIDE; Q8BGE6; -.
DR ProteomicsDB; 265147; -.
DR DNASU; 66615; -.
DR GeneID; 66615; -.
DR KEGG; mmu:66615; -.
DR UCSC; uc007cej.1; mouse.
DR CTD; 23192; -.
DR MGI; MGI:1913865; Atg4b.
DR eggNOG; KOG2674; Eukaryota.
DR InParanoid; Q8BGE6; -.
DR OrthoDB; 431748at2759; -.
DR PhylomeDB; Q8BGE6; -.
DR TreeFam; TF314847; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR BioGRID-ORCS; 66615; 7 hits in 77 CRISPR screens.
DR ChiTaRS; Atg4b; mouse.
DR PRO; PR:Q8BGE6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BGE6; protein.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0019786; F:Atg8-specific peptidase activity; ISO:MGI.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0000045; P:autophagosome assembly; IMP:ParkinsonsUK-UCL.
DR GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; IMP:ParkinsonsUK-UCL.
DR GO; GO:0016237; P:lysosomal microautophagy; ISS:UniProtKB.
DR GO; GO:0000423; P:mitophagy; ISS:UniProtKB.
DR GO; GO:0031173; P:otolith mineralization completed early in development; IMP:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0051697; P:protein delipidation; IDA:UniProtKB.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR InterPro; IPR032916; ATG4B_met.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR005078; Peptidase_C54.
DR PANTHER; PTHR22624; PTHR22624; 1.
DR PANTHER; PTHR22624:SF39; PTHR22624:SF39; 1.
DR Pfam; PF03416; Peptidase_C54; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 1: Evidence at protein level;
KW Acetylation; Autophagy; Cytoplasm; Cytoplasmic vesicle; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Isopeptide bond;
KW Mitochondrion; Phosphoprotein; Protease; Protein transport;
KW Reference proteome; S-nitrosylation; Thiol protease; Transport;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..393
FT /note="Cysteine protease ATG4B"
FT /id="PRO_0000215845"
FT MOTIF 388..391
FT /note="LIR"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT ACT_SITE 74
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT ACT_SITE 278
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT ACT_SITE 280
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT MOD_RES 189
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT MOD_RES 292
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT MOD_RES 301
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT DISULFID 292..361
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT DISULFID 292
FT /note="Interchain (with C-361)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT DISULFID 361
FT /note="Interchain (with C-292)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT CONFLICT 128..153
FT /note="IAQMGVGEGKSIGQWYGPNTVAQVLK -> NCLNCHCCGVMLMLYKAHGSVL
FT AFCR (in Ref. 4; AAH27184)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="A -> V (in Ref. 1; CAD43220 and 3; BAC26079/
FT BAC27455/BAC35965)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="T -> K (in Ref. 3; BAC40587, 4 and 5)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 44375 MW; EB9BF54B06F79135 CRC64;
MDAATLTYDT LRFAEFEDFP ETSEPVWILG RKYSIFTEKD EILSDVASRL WFTYRRNFPA
IGGTGPTSDT GWGCMLRCGQ MIFAQALVCR HLGRDWRWTQ RKRQPDSYFN VLNAFLDRKD
SYYSIHQIAQ MGVGEGKSIG QWYGPNTVAQ VLKKLAVFDT WSSLAVHIAM DNTVVMEEIR
RLCRANLPCA GAAALPTDSE RHCNGFPAGA EVTNRPSAWR PLVLLIPLRL GLTDINEAYV
ETLKHCFMMP QSLGVIGGKP NSAHYFIGYV GEELIYLDPH TTQPAVELTD SCFIPDESFH
CQHPPSRMGI GELDPSIAVG FFCKTEEDFN DWCQQVKKLS QLGGALPMFE LVEQQPSHLA
CQDVLNLSLD SSDVERLERF FDSEDEDFEI LSL
