PTPRQ_HUMAN
ID PTPRQ_HUMAN Reviewed; 2332 AA.
AC Q9UMZ3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Phosphatidylinositol phosphatase PTPRQ;
DE EC=3.1.3.-;
DE AltName: Full=Receptor-type tyrosine-protein phosphatase Q;
DE Short=PTP-RQ;
DE Short=R-PTP-Q;
DE EC=3.1.3.48;
DE Flags: Precursor;
GN Name=PTPRQ;
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=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2133-2266.
RA Dayton M.A., Blanchard K.L.;
RT "Differential expression of PTPase RNAs resulting from K562 differentiation
RT induced by PMA.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12837292; DOI=10.1016/s0014-4827(03)00121-6;
RA Seifert R.A., Coats S.A., Oganesian A., Wright M.B., Dishmon M.,
RA Booth C.J., Johnson R.J., Alpers C.E., Bowen-Pope D.F.;
RT "PTPRQ is a novel phosphatidylinositol phosphatase that can be expressed as
RT a cytoplasmic protein or as a subcellularly localized receptor-like
RT protein.";
RL Exp. Cell Res. 287:374-386(2003).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=19351528; DOI=10.1016/j.bbrc.2009.04.001;
RA Jung H., Kim W.K., Kim do H., Cho Y.S., Kim S.J., Park S.G., Park B.C.,
RA Lim H.M., Bae K.H., Lee S.C.;
RT "Involvement of PTP-RQ in differentiation during adipogenesis of human
RT mesenchymal stem cells.";
RL Biochem. Biophys. Res. Commun. 383:252-257(2009).
RN [5]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND VARIANT DFNB84A GLY-281.
RX PubMed=20346435; DOI=10.1016/j.ajhg.2010.02.015;
RA Schraders M., Oostrik J., Huygen P.L., Strom T.M., van Wijk E., Kunst H.P.,
RA Hoefsloot L.H., Cremers C.W., Admiraal R.J., Kremer H.;
RT "Mutations in PTPRQ are a cause of autosomal-recessive nonsyndromic hearing
RT impairment DFNB84 and associated with vestibular dysfunction.";
RL Am. J. Hum. Genet. 86:604-610(2010).
RN [6]
RP INVOLVEMENT IN DFNB84A, AND VARIANT GLU-471.
RX PubMed=20472657; DOI=10.1136/jmg.2009.075697;
RA Shahin H., Rahil M., Abu Rayan A., Avraham K.B., King M.C., Kanaan M.,
RA Walsh T.;
RT "Nonsense mutation of the stereociliar membrane protein gene PTPRQ in human
RT hearing loss DFNB84.";
RL J. Med. Genet. 47:643-645(2010).
RN [7]
RP INVOLVEMENT IN DFNA73, VARIANT DFNA73 2327-TRP--MET-2332 DEL, AND
RP CHARACTERIZATION OF VARIANT DFNA73 2327-TRP--MET-2332 DEL.
RX PubMed=29309402; DOI=10.1038/gim.2017.155;
RA Eisenberger T., Di Donato N., Decker C., Delle Vedove A., Neuhaus C.,
RA Nuernberg G., Toliat M., Nuernberg P., Muerbe D., Bolz H.J.;
RT "A C-terminal nonsense mutation links PTPRQ with autosomal-dominant hearing
RT loss, DFNA73.";
RL Genet. Med. 20:614-621(2018).
CC -!- FUNCTION: Phosphatidylinositol phosphatase required for auditory
CC function. May act by regulating the level of phosphatidylinositol 4,5-
CC bisphosphate (PIP2) level in the basal region of hair bundles. Can
CC dephosphorylate a broad range of phosphatidylinositol phosphates,
CC including phosphatidylinositol 3,4,5-trisphosphate and most
CC phosphatidylinositol monophosphates and diphosphates. Phosphate can be
CC hydrolyzed from the D3 and D5 positions in the inositol ring. Has low
CC tyrosine-protein phosphatase activity; however, the relevance of such
CC activity in vivo is unclear. Plays an important role in adipogenesis of
CC mesenchymal stem cells (MSCs). Regulates the phosphorylation state of
CC AKT1 by suppressing the phosphatidylinositol 3,4,5-trisphosphate (PIP3)
CC level in MSCs and preadipocyte cells. {ECO:0000269|PubMed:19351528}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12837292}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:12837292}.
CC -!- TISSUE SPECIFICITY: In developing kidney, it localizes to the basal
CC membrane of podocytes, beginning when podocyte progenitors can first be
CC identified in the embryonic kidney (at protein level). Expressed in
CC lung and kidney. {ECO:0000269|PubMed:12837292,
CC ECO:0000269|PubMed:20346435}.
CC -!- DEVELOPMENTAL STAGE: Expressed at highest levels in fetal kidney,
CC followed by fetal lung and fetal cochlea.
CC {ECO:0000269|PubMed:20346435}.
CC -!- INDUCTION: Down-regulated during adipogenesis of mesenchymal stem
CC cells. {ECO:0000269|PubMed:19351528}.
CC -!- DISEASE: Deafness, autosomal recessive, 84A (DFNB84A) [MIM:613391]: A
CC form of non-syndromic deafness characterized by progressive,
CC sensorineural hearing loss and vestibular dysfunction.
CC {ECO:0000269|PubMed:20346435, ECO:0000269|PubMed:20472657}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Deafness, autosomal dominant, 73 (DFNA73) [MIM:617663]: A form
CC of non-syndromic hearing loss characterized by mild to severe bilateral
CC symptoms with variable age of onset from early childhood to the third
CC decade. {ECO:0000269|PubMed:29309402}. Note=The disease may be caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2A subfamily. {ECO:0000305}.
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DR EMBL; AC083812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC074031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF169351; AAD50277.1; -; mRNA.
DR PDB; 4IKC; X-ray; 1.56 A; A=2015-2293.
DR PDBsum; 4IKC; -.
DR AlphaFoldDB; Q9UMZ3; -.
DR SMR; Q9UMZ3; -.
DR STRING; 9606.ENSP00000482885; -.
DR DEPOD; PTPRQ; -.
DR GlyGen; Q9UMZ3; 10 sites.
DR iPTMnet; Q9UMZ3; -.
DR PhosphoSitePlus; Q9UMZ3; -.
DR BioMuta; PTPRQ; -.
DR DMDM; 158563998; -.
DR EPD; Q9UMZ3; -.
DR jPOST; Q9UMZ3; -.
DR MassIVE; Q9UMZ3; -.
DR PeptideAtlas; Q9UMZ3; -.
DR PRIDE; Q9UMZ3; -.
DR ProteomicsDB; 85237; -.
DR GeneCards; PTPRQ; -.
DR HGNC; HGNC:9679; PTPRQ.
DR MalaCards; PTPRQ; -.
DR MIM; 603317; gene.
DR MIM; 613391; phenotype.
DR MIM; 617663; phenotype.
DR neXtProt; NX_Q9UMZ3; -.
DR Orphanet; 90635; Autosomal dominant non-syndromic sensorineural deafness type DFNA.
DR Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR eggNOG; KOG0791; Eukaryota.
DR eggNOG; KOG3510; Eukaryota.
DR eggNOG; KOG4228; Eukaryota.
DR InParanoid; Q9UMZ3; -.
DR PhylomeDB; Q9UMZ3; -.
DR TreeFam; TF351926; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; Q9UMZ3; -.
DR SignaLink; Q9UMZ3; -.
DR ChiTaRS; PTPRQ; human.
DR Pharos; Q9UMZ3; Tbio.
DR PRO; PR:Q9UMZ3; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q9UMZ3; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:1990264; P:peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity; IBA:GO_Central.
DR GO; GO:0045598; P:regulation of fat cell differentiation; IDA:UniProtKB.
DR CDD; cd00063; FN3; 17.
DR Gene3D; 2.60.40.10; -; 17.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00041; fn3; 13.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 17.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF49265; SSF49265; 9.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50853; FN3; 17.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Deafness; Disease variant; Glycoprotein; Hydrolase; Membrane;
KW Non-syndromic deafness; Protein phosphatase; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..2332
FT /note="Phosphatidylinositol phosphatase PTPRQ"
FT /id="PRO_0000302850"
FT TOPO_DOM 36..1947
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1948..1968
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1969..2332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..99
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 100..195
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 199..294
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 350..438
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 441..539
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 514..606
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 610..705
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 710..799
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 804..894
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 899..988
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 993..1093
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1098..1190
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1192..1282
FT /note="Fibronectin type-III 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1287..1380
FT /note="Fibronectin type-III 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1384..1470
FT /note="Fibronectin type-III 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1474..1578
FT /note="Fibronectin type-III 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1583..1681
FT /note="Fibronectin type-III 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1686..1787
FT /note="Fibronectin type-III 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2036..2292
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 2233
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 944
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1038
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1080
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1844
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 281
FT /note="R -> G (in DFNB84A)"
FT /evidence="ECO:0000269|PubMed:20346435"
FT /id="VAR_063526"
FT VARIANT 471
FT /note="Q -> E (in dbSNP:rs61729287)"
FT /evidence="ECO:0000269|PubMed:20472657"
FT /id="VAR_069041"
FT VARIANT 1040
FT /note="T -> I (in dbSNP:rs12316867)"
FT /id="VAR_034970"
FT VARIANT 1098
FT /note="F -> L (in dbSNP:rs6539524)"
FT /id="VAR_034971"
FT VARIANT 1120
FT /note="A -> P (in dbSNP:rs7975340)"
FT /id="VAR_034972"
FT VARIANT 1244
FT /note="N -> D (in dbSNP:rs17713202)"
FT /id="VAR_034973"
FT VARIANT 1734
FT /note="I -> T (in dbSNP:rs7963963)"
FT /id="VAR_034974"
FT VARIANT 2121
FT /note="R -> K (in dbSNP:rs1163042)"
FT /id="VAR_034975"
FT VARIANT 2327..2332
FT /note="Missing (in DFNA73; unknown pathological
FT significance; no effect on PTPRQ expression in patient
FT cells)"
FT /evidence="ECO:0000269|PubMed:29309402"
FT /id="VAR_080184"
FT TURN 2018..2020
FT /evidence="ECO:0007829|PDB:4IKC"
FT HELIX 2021..2042
FT /evidence="ECO:0007829|PDB:4IKC"
FT HELIX 2053..2056
FT /evidence="ECO:0007829|PDB:4IKC"
FT HELIX 2058..2063
FT /evidence="ECO:0007829|PDB:4IKC"
FT TURN 2073..2075
FT /evidence="ECO:0007829|PDB:4IKC"
FT TURN 2086..2089
FT /evidence="ECO:0007829|PDB:4IKC"
FT STRAND 2092..2096
FT /evidence="ECO:0007829|PDB:4IKC"
FT STRAND 2099..2101
FT /evidence="ECO:0007829|PDB:4IKC"
FT STRAND 2105..2109
FT /evidence="ECO:0007829|PDB:4IKC"
FT HELIX 2113..2115
FT /evidence="ECO:0007829|PDB:4IKC"
FT HELIX 2116..2126
FT /evidence="ECO:0007829|PDB:4IKC"
FT STRAND 2130..2133
FT /evidence="ECO:0007829|PDB:4IKC"
FT STRAND 2156..2159
FT /evidence="ECO:0007829|PDB:4IKC"
FT STRAND 2162..2171
FT /evidence="ECO:0007829|PDB:4IKC"
FT STRAND 2173..2184
FT /evidence="ECO:0007829|PDB:4IKC"
FT STRAND 2187..2196
FT /evidence="ECO:0007829|PDB:4IKC"
FT STRAND 2201..2204
FT /evidence="ECO:0007829|PDB:4IKC"
FT HELIX 2209..2221
FT /evidence="ECO:0007829|PDB:4IKC"
FT STRAND 2224..2226
FT /evidence="ECO:0007829|PDB:4IKC"
FT STRAND 2229..2238
FT /evidence="ECO:0007829|PDB:4IKC"
FT HELIX 2239..2255
FT /evidence="ECO:0007829|PDB:4IKC"
FT STRAND 2257..2259
FT /evidence="ECO:0007829|PDB:4IKC"
FT HELIX 2261..2271
FT /evidence="ECO:0007829|PDB:4IKC"
FT HELIX 2279..2292
FT /evidence="ECO:0007829|PDB:4IKC"
SQ SEQUENCE 2332 AA; 260924 MW; 999D87AA00BA04C2 CRC64;
MKKVPIKPEQ PEKLRAFNIS THSFSLHWSL PSGHVERYQV DLVPDSGFVT IRDLGGGEYQ
VDVSNVVPGT RYDITISSIS TTYTSPVTRI VTTNVTKPGP PVFLAGERVG SAGILLSWNT
PPNPNGRIIS YIVKYKEVCP WMQTVYTQVR SKPDSLEVLL TNLNPGTTYE IKVAAENSAG
IGVFSDPFLF QTAESAPGKV VNLTVEAYNA SAVKLIWYLP RQPNGKITSF KISVKHARSG
IVVKDVSIRV EDILTGKLPE CNENSESFLW STASPSPTLG RVTPPSRTTH SSSTLTQNEI
SSVWKEPISF VVTHLRPYTT YLFEVSAVTT EAGYIDSTIV RTPESVPEGP PQNCVTGNIT
GKSFSILWDP PTIVTGKFSY RVELYGPSGR ILDNSTKDLK FAFTNLTPFT MYDVYIAAET
SAGTGPKSNI SVFTPPDVPG AVFDLQLAEV ESTQVRITWK KPRQPNGIIN QYRVKVLVPE
TGIILENTLL TGNNEYINDP MAPEIVNIVE PMVGLYEGSA EMSSDLHSLA TFIYNSHPDK
NFPARNRAED QTSPVVTTRN QYITDIAAEQ LSYVIRRLVP FTEHMISVSA FTIMGEGPPT
VLSVRTRQQV PSSIKIINYK NISSSSILLY WDPPEYPNGK ITHYTIYAME LDTNRAFQIT
TIDNSFLITG LKKYTKYKMR VAASTHVGES SLSEENDIFV RTSEDEPESS PQDVEVIDVT
ADEIRLKWSP PEKPNGIIIA YEVLYKNIDT LYMKNTSTTD IILRNLRPHT LYNISVRSYT
RFGHGNQVSS LLSVRTSETV PDSAPENITY KNISSGEIEL SFLPPSSPNG IIKKYTIYLK
RSNGNEERTI NTTSLTQNIK VLKKYTQYII EVSASTLKGE GVRSAPISIL TEEDAPDSPP
QDFSVKQLSG VTVKLSWQPP LEPNGIILYY TVYVWNRSSL KTINVTETSL ELSDLDYNVE
YSAYVTASTR FGDGKTRSNI ISFQTPEGAP SDPPKDVYYA NLSSSSIILF WTPPSKPNGI
IQYYSVYYRN TSGTFMQNFT LHEVTNDFDN MTVSTIIDKL TIFSYYTFWL TASTSVGNGN
KSSDIIEVYT DQDIPEGFVG NLTYESISST AINVSWVPPA QPNGLVFYYV SLILQQTPRH
VRPPLVTYER SIYFDNLEKY TDYILKITPS TEKGFSDTYT AQLYIKTEED VPETSPIINT
FKNLSSTSVL LSWDPPVKPN GAIISYDLTL QGPNENYSFI TSDNYIILEE LSPFTLYSFF
AAARTRKGLG PSSILFFYTD ESVPLAPPQN LTLINCTSDF VWLKWSPSPL PGGIVKVYSF
KIHEHETDTI YYKNISGFKT EAKLVGLEPV STYSIRVSAF TKVGNGNQFS NVVKFTTQES
VPDVVQNMQC MATSWQSVLV KWDPPKKANG IITQYMVTVE RNSTKVSPQD HMYTFIKLLA
NTSYVFKVRA STSAGEGDES TCHVSTLPET VPSVPTNIAF SDVQSTSATL TWIRPDTILG
YFQNYKITTQ LRAQKCKEWE SEECVEYQKI QYLYEAHLTE ETVYGLKKFR WYRFQVAAST
NAGYGNASNW ISTKTLPGPP DGPPENVHVV ATSPFSISIS WSEPAVITGP TCYLIDVKSV
DNDEFNISFI KSNEENKTIE IKDLEIFTRY SVVITAFTGN ISAAYVEGKS SAEMIVTTLE
SAPKDPPNNM TFQKIPDEVT KFQLTFLPPS QPNGNIQVYQ ALVYREDDPT AVQIHNLSII
QKTNTFVIAM LEGLKGGHTY NISVYAVNSA GAGPKVPMRI TMDIKAPARP KTKPTPIYDA
TGKLLVTSTT ITIRMPICYY SDDHGPIKNV QVLVTETGAQ HDGNVTKWYD AYFNKARPYF
TNEGFPNPPC TEGKTKFSGN EEIYIIGADN ACMIPGNEDK ICNGPLKPKK QYLFKFRATN
IMGQFTDSDY SDPVKTLGEG LSERTVEIIL SVTLCILSII LLGTAIFAFA RIRQKQKEGG
TYSPQDAEII DTKLKLDQLI TVADLELKDE RLTRPISKKS FLQHVEELCT NNNLKFQEEF
SELPKFLQDL SSTDADLPWN RAKNRFPNIK PYNNNRVKLI ADASVPGSDY INASYISGYL
CPNEFIATQG PLPGTVGDFW RMVWETRAKT LVMLTQCFEK GRIRCHQYWP EDNKPVTVFG
DIVITKLMED VQIDWTIRDL KIERHGDCMT VRQCNFTAWP EHGVPENSAP LIHFVKLVRA
SRAHDTTPMI VHCSAGVGRT GVFIALDHLT QHINDHDFVD IYGLVAELRS ERMCMVQNLA
QYIFLHQCIL DLLSNKGSNQ PICFVNYSAL QKMDSLDAME GDVELEWEET TM
