ID HACD2_HUMAN Reviewed; 254 AA. AC Q6Y1H2; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 159. DE RecName: Full=Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 2 {ECO:0000305}; DE EC=4.2.1.134 {ECO:0000269|PubMed:18554506}; DE AltName: Full=3-hydroxyacyl-CoA dehydratase 2 {ECO:0000303|PubMed:18554506}; DE Short=HACD2 {ECO:0000303|PubMed:18554506}; DE AltName: Full=Protein-tyrosine phosphatase-like member B {ECO:0000312|HGNC:HGNC:9640}; GN Name=HACD2 {ECO:0000303|PubMed:18554506, ECO:0000312|HGNC:HGNC:9640}; GN Synonyms=PTPLB {ECO:0000305}; 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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP INTERACTION WITH BCAP31, MUTAGENESIS OF PRO-101, AND CAUTION. RX PubMed=15024066; DOI=10.1128/mcb.24.7.2767-2778.2004; RA Wang B., Pelletier J., Massaad M.J., Herscovics A., Shore G.C.; RT "The yeast split-ubiquitin membrane protein two-hybrid screen identifies RT BAP31 as a regulator of the turnover of endoplasmic reticulum-associated RT protein tyrosine phosphatase-like B."; RL Mol. Cell. Biol. 24:2767-2778(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Testis; 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 FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, PATHWAY, RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RX PubMed=18554506; DOI=10.1016/j.febslet.2008.06.007; RA Ikeda M., Kanao Y., Yamanaka M., Sakuraba H., Mizutani Y., Igarashi Y., RA Kihara A.; RT "Characterization of four mammalian 3-hydroxyacyl-CoA dehydratases involved RT in very long-chain fatty acid synthesis."; RL FEBS Lett. 582:2435-2440(2008). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [7] 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 [8] 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 [9] 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 [10] RP ACETYLATION AT ALA-2. RX PubMed=25732826; DOI=10.1016/j.celrep.2015.01.053; RA Aksnes H., Van Damme P., Goris M., Starheim K.K., Marie M., Stoeve S.I., RA Hoel C., Kalvik T.V., Hole K., Glomnes N., Furnes C., Ljostveit S., RA Ziegler M., Niere M., Gevaert K., Arnesen T.; RT "An organellar nalpha-acetyltransferase, naa60, acetylates cytosolic N RT termini of transmembrane proteins and maintains Golgi integrity."; RL Cell Rep. 10:1362-1374(2015). CC -!- FUNCTION: Catalyzes the third of the very long-chain fatty acids CC (VLCFA) elongation four-step cycle (condensation, reduction, CC dehydration, and reduction). This endoplasmic reticulum-elongation CC process is characterized by the addition of two carbons to the lipid CC chain through each cycle. This enzyme catalyzes the dehydration of the CC 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each CC cycle of elongation. Therefore, it participates in the production of CC various VLCFAs involved in multiple biological processes as precursors CC of membrane lipids and lipid mediators. {ECO:0000269|PubMed:18554506}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain CC (2E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:45812, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:83728, ChEBI:CHEBI:85440; EC=4.2.1.134; CC Evidence={ECO:0000269|PubMed:18554506}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45813; CC Evidence={ECO:0000305|PubMed:18554506}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(3R)-hydroxyhexadecanoyl-CoA = (2E)-hexadecenoyl-CoA + H2O; CC Xref=Rhea:RHEA:39159, ChEBI:CHEBI:15377, ChEBI:CHEBI:61526, CC ChEBI:CHEBI:74278; Evidence={ECO:0000269|PubMed:18554506}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39160; CC Evidence={ECO:0000305|PubMed:18554506}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(3R)-hydroxyoctadecanoyl-CoA = (2E)-octadecenoyl-CoA + H2O; CC Xref=Rhea:RHEA:39155, ChEBI:CHEBI:15377, ChEBI:CHEBI:71412, CC ChEBI:CHEBI:76374; Evidence={ECO:0000269|PubMed:18554506}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39156; CC Evidence={ECO:0000305|PubMed:18554506}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(3R)-hydroxyeicosanoyl-CoA = (2E)-eicosenoyl-CoA + H2O; CC Xref=Rhea:RHEA:39175, ChEBI:CHEBI:15377, ChEBI:CHEBI:74691, CC ChEBI:CHEBI:76373; Evidence={ECO:0000269|PubMed:18554506}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39176; CC Evidence={ECO:0000305|PubMed:18554506}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(3R)-hydroxydocosanoyl-CoA = (2E)-docosenoyl-CoA + H2O; CC Xref=Rhea:RHEA:39187, ChEBI:CHEBI:15377, ChEBI:CHEBI:74692, CC ChEBI:CHEBI:76375; Evidence={ECO:0000269|PubMed:18554506}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39188; CC Evidence={ECO:0000305|PubMed:18554506}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(3R)-hydroxytetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + H2O; CC Xref=Rhea:RHEA:39199, ChEBI:CHEBI:15377, ChEBI:CHEBI:74693, CC ChEBI:CHEBI:76377; Evidence={ECO:0000269|PubMed:18554506}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39200; CC Evidence={ECO:0000305|PubMed:18554506}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(3R)-hydroxyhexacosanoyl-CoA = (2E)-hexacosenoyl-CoA + H2O; CC Xref=Rhea:RHEA:39211, ChEBI:CHEBI:15377, ChEBI:CHEBI:74281, CC ChEBI:CHEBI:76378; Evidence={ECO:0000269|PubMed:18554506}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39212; CC Evidence={ECO:0000305|PubMed:18554506}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=121.7 uM for 3-hydroxypalmitoyl-CoA (at 37 degrees Celsius) CC {ECO:0000269|PubMed:18554506}; CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC {ECO:0000269|PubMed:18554506}. CC -!- SUBUNIT: May interact with enzymes of the ELO family (including CC ELOVL1); with those enzymes that mediate condensation, the first of the CC four steps of the reaction cycle responsible for fatty acids CC elongation, may be part of a larger fatty acids elongase complex CC (PubMed:18554506). Interacts with BCAP31 (PubMed:15024066). CC {ECO:0000269|PubMed:15024066, ECO:0000269|PubMed:18554506}. CC -!- INTERACTION: CC Q6Y1H2; P51572: BCAP31; NbExp=4; IntAct=EBI-530257, EBI-77683; CC Q6Y1H2; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-530257, EBI-6942903; CC Q6Y1H2; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-530257, EBI-18304435; CC Q6Y1H2; Q13651: IL10RA; NbExp=3; IntAct=EBI-530257, EBI-1031656; CC Q6Y1H2; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-530257, EBI-12188413; CC Q6Y1H2; Q9NZ01: TECR; NbExp=7; IntAct=EBI-530257, EBI-2877718; CC Q6Y1H2; Q9Y320: TMX2; NbExp=3; IntAct=EBI-530257, EBI-6447886; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:15024066, ECO:0000269|PubMed:18554506}; Multi-pass CC membrane protein {ECO:0000269|PubMed:15024066, CC ECO:0000269|PubMed:18554506}. CC -!- TISSUE SPECIFICITY: Highly expressed in testis, spleen, prostate, colon CC and heart, followed by moderate expression in thymus, ovary, small CC intestine, peripheral blood leukocytes, liver, skeletal muscle and CC pancreas. Weakly detected in kidney, placenta, brain and lung. CC {ECO:0000269|PubMed:15024066}. CC -!- MISCELLANEOUS: Turns over rapidly through degradation by the proteasome CC system. {ECO:0000269|PubMed:15024066}. CC -!- SIMILARITY: Belongs to the very long-chain fatty acids dehydratase HACD CC family. {ECO:0000305}. CC -!- CAUTION: Shares some similarity with tyrosine phosphatase proteins but CC it has probably no phosphatase activity. {ECO:0000269|PubMed:15024066}. 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; AY191814; AAP20101.1; -; mRNA. DR EMBL; AK289983; BAF82672.1; -; mRNA. DR EMBL; AC020631; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC023165; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC025571; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC084039; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC049369; AAH49369.1; -; mRNA. DR EMBL; BC060839; AAH60839.1; -; mRNA. DR CCDS; CCDS46895.1; -. DR RefSeq; NP_940684.1; NM_198402.4. DR AlphaFoldDB; Q6Y1H2; -. DR BioGRID; 128393; 97. DR IntAct; Q6Y1H2; 35. DR STRING; 9606.ENSP00000373153; -. DR SwissLipids; SLP:000000438; -. DR GlyCosmos; Q6Y1H2; 1 site, No reported glycans. DR GlyGen; Q6Y1H2; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q6Y1H2; -. DR PhosphoSitePlus; Q6Y1H2; -. DR SwissPalm; Q6Y1H2; -. DR BioMuta; HACD2; -. DR DMDM; 74738322; -. DR EPD; Q6Y1H2; -. DR jPOST; Q6Y1H2; -. DR MassIVE; Q6Y1H2; -. DR MaxQB; Q6Y1H2; -. DR PaxDb; 9606-ENSP00000373153; -. DR PeptideAtlas; Q6Y1H2; -. DR ProteomicsDB; 67831; -. DR Pumba; Q6Y1H2; -. DR TopDownProteomics; Q6Y1H2; -. DR Antibodypedia; 32955; 104 antibodies from 16 providers. DR DNASU; 201562; -. DR Ensembl; ENST00000383657.10; ENSP00000373153.5; ENSG00000206527.10. DR GeneID; 201562; -. DR KEGG; hsa:201562; -. DR MANE-Select; ENST00000383657.10; ENSP00000373153.5; NM_198402.5; NP_940684.1. DR UCSC; uc003egj.3; human. DR AGR; HGNC:9640; -. DR CTD; 201562; -. DR DisGeNET; 201562; -. DR GeneCards; HACD2; -. DR HGNC; HGNC:9640; HACD2. DR HPA; ENSG00000206527; Low tissue specificity. DR MIM; 615939; gene. DR neXtProt; NX_Q6Y1H2; -. DR OpenTargets; ENSG00000206527; -. DR PharmGKB; PA33983; -. DR VEuPathDB; HostDB:ENSG00000206527; -. DR eggNOG; KOG3187; Eukaryota. DR GeneTree; ENSGT00530000062962; -. DR HOGENOM; CLU_034302_2_0_1; -. DR InParanoid; Q6Y1H2; -. DR OMA; SEWWLMY; -. DR OrthoDB; 276005at2759; -. DR PhylomeDB; Q6Y1H2; -. DR TreeFam; TF313326; -. DR PathwayCommons; Q6Y1H2; -. DR Reactome; R-HSA-75876; Synthesis of very long-chain fatty acyl-CoAs. DR SABIO-RK; Q6Y1H2; -. DR SignaLink; Q6Y1H2; -. DR SIGNOR; Q6Y1H2; -. DR UniPathway; UPA00094; -. DR BioGRID-ORCS; 201562; 34 hits in 1156 CRISPR screens. DR ChiTaRS; HACD2; human. DR GenomeRNAi; 201562; -. DR Pharos; Q6Y1H2; Tbio. DR PRO; PR:Q6Y1H2; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q6Y1H2; Protein. DR Bgee; ENSG00000206527; Expressed in gingival epithelium and 208 other cell types or tissues. DR ExpressionAtlas; Q6Y1H2; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0018812; F:3-hydroxyacyl-CoA dehydratase activity; EXP:Reactome. DR GO; GO:0019899; F:enzyme binding; IDA:UniProtKB. DR GO; GO:0102158; F:very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase activity; IDA:UniProtKB. DR GO; GO:0030497; P:fatty acid elongation; IDA:UniProtKB. DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; TAS:Reactome. DR GO; GO:0030148; P:sphingolipid biosynthetic process; IGI:UniProtKB. DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IDA:UniProtKB. DR InterPro; IPR007482; Tyr_Pase-like_PTPLA. DR PANTHER; PTHR11035; VERY-LONG-CHAIN (3R)-3-HYDROXYACYL-COA DEHYDRATASE; 1. DR PANTHER; PTHR11035:SF17; VERY-LONG-CHAIN (3R)-3-HYDROXYACYL-COA DEHYDRATASE 2; 1. DR Pfam; PF04387; PTPLA; 1. DR Genevisible; Q6Y1H2; HS. PE 1: Evidence at protein level; KW Acetylation; Endoplasmic reticulum; Fatty acid biosynthesis; KW Fatty acid metabolism; Glycoprotein; Lipid biosynthesis; Lipid metabolism; KW Lyase; Membrane; Reference proteome; Transmembrane; Transmembrane helix. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..254 FT /note="Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase FT 2" FT /id="PRO_0000349319" FT TOPO_DOM 2..41 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 42..60 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 61..79 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 80..97 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 98..107 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 108..125 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 126..130 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 131..146 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 147..169 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 170..187 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 188..217 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 218..235 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 236..254 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 11..33 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 176 FT /evidence="ECO:0000250|UniProtKB:P40857" FT ACT_SITE 183 FT /evidence="ECO:0000250|UniProtKB:P40857" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|PubMed:25732826, FT ECO:0007744|PubMed:19413330" FT CARBOHYD 209 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT MUTAGEN 101 FT /note="P->R: Does not restore any protein tyrosine FT phosphatase activity." FT /evidence="ECO:0000269|PubMed:15024066" SQ SEQUENCE 254 AA; 28368 MW; 6B301176C696899E CRC64; MAAVAATAAA KGNGGGGGRA GAGDASGTRK KKGPGPLATA YLVIYNVVMT AGWLVIAVGL VRAYLAKGSY HSLYYSIEKP LKFFQTGALL EILHCAIGIV PSSVVLTSFQ VMSRVFLIWA VTHSVKEVQS EDSVLLFVIA WTITEIIRYS FYTFSLLNHL PYLIKWARYT LFIVLYPMGV SGELLTIYAA LPFVRQAGLY SISLPNKYNF SFDYYAFLIL IMISYIPIFP QLYFHMIHQR RKILSHTEEH KKFE //