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Receptor-type tyrosine-protein phosphatase eta (Protein-tyrosine phosphatase eta) (R-PTP-eta) (EC 3.1.3.48) (HPTP beta-like tyrosine phosphatase) (Protein-tyrosine phosphatase receptor type J) (R-PTP-J) (Susceptibility to colon cancer 1) (CD antigen CD148)

 PTPRJ_MOUSE             Reviewed;        1238 AA.
Q64455; Q3UH64; Q3UHL5; Q541R5; Q8CIW9; Q8K3Q2;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
15-DEC-2009, sequence version 2.
25-OCT-2017, entry version 152.
RecName: Full=Receptor-type tyrosine-protein phosphatase eta;
Short=Protein-tyrosine phosphatase eta;
Short=R-PTP-eta;
EC=3.1.3.48;
AltName: Full=HPTP beta-like tyrosine phosphatase;
AltName: Full=Protein-tyrosine phosphatase receptor type J;
Short=R-PTP-J;
AltName: Full=Susceptibility to colon cancer 1;
AltName: CD_antigen=CD148;
Flags: Precursor;
Name=Ptprj; Synonyms=Byp, Scc1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=MRL-LPR/LPR; TISSUE=Lymph node;
PubMed=8549806; DOI=10.1016/0014-5793(95)01415-2;
Kuramochi S., Matsuda S., Matsuda Y., Saitoh T., Ohsugi M.,
Yamamoto T.;
"Molecular cloning and characterization of Byp, a murine receptor-type
tyrosine phosphatase similar to human DEP-1.";
FEBS Lett. 378:7-14(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=129/SvSl, and BALB/cJ;
PubMed=12089527; DOI=10.1038/ng903;
Ruivenkamp C.A.L., van Wezel T., Zanon C., Stassen A.P.M., Vlcek C.,
Csikos T., Klous A.M., Tripodis N., Perrakis A., Boerrigter L.,
Groot P.C., Lindeman J., Mooi W.J., Meijjer G.A., Scholten G.,
Dauwerse H., Paces V., van Zandwijk N., van Ommen G.J.B., Demant P.;
"Ptprj is a candidate for the mouse colon-cancer susceptibility locus
Scc1 and is frequently deleted in human cancers.";
Nat. Genet. 31:295-300(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=129P2;
Csikos T., Snoek M., de Boer T., Drenth T., Krimpenfort P.,
van Amerongen R., Zevenhoven J., van der Valk M., Hellberg C.,
Ostman A., Demant P., Berns A.;
"Phenotypic consequences of the germ-line loss of the putative tumor
suppressor Ptprj (Scc1).";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
TISSUE SPECIFICITY.
PubMed=8483328;
Honda H., Shibuya M., Chiba S., Yazaki Y., Hirai H.;
"Identification of novel protein-tyrosine phosphatases in a human
leukemia cell line, F-36P.";
Leukemia 7:742-746(1993).
[6]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=9823776;
Osborne J.M., den Elzen N., Lichanska A.M., Costelloe E.O., Yamada T.,
Cassady A.I., Hume D.A.;
"Murine DEP-1, a receptor protein tyrosine phosphatase, is expressed
in macrophages and is regulated by CSF-1 and LPS.";
J. Leukoc. Biol. 64:692-701(1998).
[7]
FUNCTION, AND MUTAGENESIS OF ASP-1106 AND CYS-1140.
PubMed=12771128; DOI=10.1083/jcb.200209019;
Grazia Lampugnani M., Zanetti A., Corada M., Takahashi T., Balconi G.,
Breviario F., Orsenigo F., Cattelino A., Kemler R., Daniel T.O.,
Dejana E.;
"Contact inhibition of VEGF-induced proliferation requires vascular
endothelial cadherin, beta-catenin, and the phosphatase DEP-1/CD148.";
J. Cell Biol. 161:793-804(2003).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12913111; DOI=10.1083/jcb.200303040;
Lin J., Weiss A.;
"The tyrosine phosphatase CD148 is excluded from the immunologic
synapse and down-regulates prolonged T cell signaling.";
J. Cell Biol. 162:673-682(2003).
[9]
FUNCTION.
PubMed=12588999; DOI=10.1128/MCB.23.5.1817-1831.2003;
Takahashi T., Takahashi K., St John P.L., Fleming P.A., Tomemori T.,
Watanabe T., Abrahamson D.R., Drake C.J., Shirasawa T., Daniel T.O.;
"A mutant receptor tyrosine phosphatase, CD148, causes defects in
vascular development.";
Mol. Cell. Biol. 23:1817-1831(2003).
[10]
FUNCTION, AND MUTAGENESIS OF CYS-1140.
PubMed=12833140; DOI=10.1038/sj.onc.1206652;
Jandt E., Denner K., Kovalenko M., Ostman A., Bohmer F.D.;
"The protein-tyrosine phosphatase DEP-1 modulates growth factor-
stimulated cell migration and cell-matrix adhesion.";
Oncogene 22:4175-4185(2003).
[11]
FUNCTION.
PubMed=18249142; DOI=10.1016/j.immuni.2007.11.024;
Zhu J.W., Brdicka T., Katsumoto T.R., Lin J., Weiss A.;
"Structurally distinct phosphatases CD45 and CD148 both regulate B
cell and macrophage immunoreceptor signaling.";
Immunity 28:183-196(2008).
[12]
FUNCTION.
PubMed=19246339; DOI=10.1182/blood-2008-08-174318;
Senis Y.A., Tomlinson M.G., Ellison S., Mazharian A., Lim J., Zhao Y.,
Kornerup K.N., Auger J.M., Thomas S.G., Dhanjal T., Kalia N.,
Zhu J.W., Weiss A., Watson S.P.;
"The tyrosine phosphatase CD148 is an essential positive regulator of
platelet activation and thrombosis.";
Blood 113:4942-4954(2009).
[13]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19268662; DOI=10.1016/j.yexcr.2009.02.023;
Dave R.K., Hume D.A., Elsegood C., Kellie S.;
"CD148/DEP-1 association with areas of cytoskeletal organisation in
macrophages.";
Exp. Cell Res. 315:1734-1744(2009).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145; ASN-313; ASN-317 AND
ASN-538.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Tyrosine phosphatase which dephosphorylates or
contributes to the dephosphorylation of CTNND1, FLT3, PDGFRB, MET,
RET, KDR, LYN, SRC, MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and
PIK3R2. Plays a role in cell adhesion, migration, proliferation
and differentiation. Involved in vascular development. May be
involved in the mechanism of contact inhibition of cell growth.
Regulator of macrophage adhesion and spreading. Positively affects
cell-matrix adhesion. Positive regulator of platelet activation
and thrombosis. Negative regulator of cell proliferation. Negative
regulator of PDGF-stimulated cell migration; through
dephosphorylation of PDGFR. Positive regulator of endothelial cell
survival, as well as of VEGF-induced SRC and AKT activation;
through KDR dephosphorylation. Negative regulator of EGFR
signaling pathway; through EGFR dephosphorylation. Enhances the
barrier function of epithelial junctions during reassembly.
Negatively regulates T-cell receptor (TCR) signaling. Upon T-cell
TCR activation, it is up-regulated and excluded from the
immunological synapses, while upon T-cell-antigen presenting cells
(APC) disengagement, it is no longer excluded and can
dephosphorylate PLCG1 and LAT to down-regulate prolongation of
signaling. {ECO:0000269|PubMed:12588999,
ECO:0000269|PubMed:12771128, ECO:0000269|PubMed:12833140,
ECO:0000269|PubMed:12913111, ECO:0000269|PubMed:18249142,
ECO:0000269|PubMed:19246339, ECO:0000269|PubMed:19268662}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
-!- SUBUNIT: Monomer. Interacts with CTNNB1 (phosphorylated) and JUP
(phosphorylated). Interacts with FLT3 (phosphorylated). Interacts
with GAB1 and GRB2 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Cell projection, ruffle membrane. Cell junction.
Note=After T-cell stimulation, it is temporarily excluded from
immunological synapses. Found at cell borders.
-!- TISSUE SPECIFICITY: Expressed at high levels in brain, kidney,
spleen and intestine, and at lower levels in liver, lung, thymus
and heart. Expressed at a high level in the myeloid cell line FDC-
P2, and at a lower level in the pre-B lymphoid cell line WEHI-231
and the T hybridoma cell line HB21.7.31. Not expressed in the
fibroblast cell line NIH3T3 or the erythroid cell line F5-5.
Expressed in macrophages. {ECO:0000269|PubMed:8483328,
ECO:0000269|PubMed:8549806, ECO:0000269|PubMed:9823776}.
-!- DEVELOPMENTAL STAGE: Expressed at 11.5 dpc in presumptive
macrophages concentrated in the liver and scattered throughout the
embryonic mesenchyme. Expressed at 11.5 and 12.5 dpc in the
developing eye and in the ganglia and processes of cranial and
spinal nerves constituting the PNS. {ECO:0000269|PubMed:9823776}.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Receptor class 3 subfamily. {ECO:0000305}.
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EMBL; D45212; BAA08146.1; -; mRNA.
EMBL; AY038877; AAN11409.1; -; Genomic_DNA.
EMBL; AY038861; AAN11409.1; JOINED; Genomic_DNA.
EMBL; AY038891; AAK96030.1; -; mRNA.
EMBL; AY039232; AAK98640.1; -; mRNA.
EMBL; DQ133576; ABA07808.1; -; mRNA.
EMBL; AK147318; BAE27842.1; -; mRNA.
EMBL; AK147556; BAE27993.1; -; mRNA.
PIR; S68700; S68700.
RefSeq; NP_033008.3; NM_008982.5.
UniGene; Mm.330393; -.
ProteinModelPortal; Q64455; -.
SMR; Q64455; -.
IntAct; Q64455; 1.
STRING; 10090.ENSMUSP00000129592; -.
iPTMnet; Q64455; -.
PhosphoSitePlus; Q64455; -.
EPD; Q64455; -.
MaxQB; Q64455; -.
PaxDb; Q64455; -.
PRIDE; Q64455; -.
DNASU; 19271; -.
GeneID; 19271; -.
KEGG; mmu:19271; -.
CTD; 5795; -.
MGI; MGI:104574; Ptprj.
eggNOG; KOG0791; Eukaryota.
eggNOG; COG5599; LUCA.
HOGENOM; HOG000232054; -.
HOVERGEN; HBG053761; -.
InParanoid; Q64455; -.
KO; K05698; -.
ChiTaRS; Ptprj; mouse.
PRO; PR:Q64455; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_PTPRJ; -.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0001772; C:immunological synapse; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
GO; GO:0070097; F:delta-catenin binding; ISO:MGI.
GO; GO:0045295; F:gamma-catenin binding; ISO:MGI.
GO; GO:0051019; F:mitogen-activated protein kinase binding; ISO:MGI.
GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IMP:UniProtKB.
GO; GO:0007596; P:blood coagulation; IMP:UniProtKB.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
GO; GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:UniProtKB.
GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; IDA:UniProtKB.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISS:UniProtKB.
GO; GO:2000272; P:negative regulation of receptor activity; IMP:UniProtKB.
GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IDA:UniProtKB.
GO; GO:0043116; P:negative regulation of vascular permeability; ISO:MGI.
GO; GO:0048709; P:oligodendrocyte differentiation; IMP:MGI.
GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISO:MGI.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0050918; P:positive chemotaxis; ISO:MGI.
GO; GO:0045785; P:positive regulation of cell adhesion; ISO:MGI.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IDA:UniProtKB.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IDA:UniProtKB.
GO; GO:0010572; P:positive regulation of platelet activation; IMP:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
GO; GO:0030155; P:regulation of cell adhesion; ISO:MGI.
GO; GO:0001570; P:vasculogenesis; IMP:MGI.
CDD; cd00063; FN3; 5.
Gene3D; 1.20.5.100; -; 1.
Gene3D; 2.60.40.10; -; 7.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR021157; Cyt_c1_TM_anchor_C.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR000242; PTPase_domain.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
Pfam; PF00041; fn3; 3.
Pfam; PF00102; Y_phosphatase; 1.
PRINTS; PR00700; PRTYPHPHTASE.
SMART; SM00060; FN3; 8.
SMART; SM00194; PTPc; 1.
SMART; SM00404; PTPc_motif; 1.
SUPFAM; SSF49265; SSF49265; 5.
SUPFAM; SSF52799; SSF52799; 1.
PROSITE; PS50853; FN3; 6.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
1: Evidence at protein level;
Cell junction; Cell membrane; Cell projection; Complete proteome;
Glycoprotein; Hydrolase; Membrane; Phosphoprotein;
Protein phosphatase; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 1238 Receptor-type tyrosine-protein
phosphatase eta.
/FTId=PRO_0000025445.
TOPO_DOM 29 876 Extracellular. {ECO:0000255}.
TRANSMEM 877 897 Helical. {ECO:0000255}.
TOPO_DOM 898 1238 Cytoplasmic. {ECO:0000255}.
DOMAIN 39 122 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 170 266 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 270 358 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 359 443 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 444 527 Fibronectin type-III 5.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 528 621 Fibronectin type-III 6.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 622 718 Fibronectin type-III 7.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 717 803 Fibronectin type-III 8.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 942 1199 Tyrosine-protein phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
REGION 1140 1146 Substrate binding. {ECO:0000250}.
ACT_SITE 1140 1140 Phosphocysteine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00160,
ECO:0000255|PROSITE-ProRule:PRU10044}.
BINDING 1106 1106 Substrate. {ECO:0000250}.
BINDING 1184 1184 Substrate. {ECO:0000250}.
MOD_RES 910 910 Phosphoserine.
{ECO:0000250|UniProtKB:Q12913}.
CARBOHYD 62 62 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 78 78 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 85 85 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 90 90 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 114 114 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 145 145 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 164 164 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 173 173 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 182 182 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 198 198 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 207 207 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 244 244 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 253 253 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 267 267 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 278 278 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 313 313 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 317 317 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 333 333 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 366 366 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 379 379 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 398 398 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 403 403 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 437 437 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 452 452 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 488 488 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 506 506 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 538 538 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 572 572 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 576 576 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 662 662 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 668 668 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 685 685 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 691 691 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 725 725 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 811 811 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 838 838 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 1106 1106 D->A: Substrate trapping with much higher
affinity for substrate.
{ECO:0000269|PubMed:12771128}.
MUTAGEN 1140 1140 C->S: Catalytically inactive and
substrate trapping with higher affinity
for substrate.
{ECO:0000269|PubMed:12771128,
ECO:0000269|PubMed:12833140}.
CONFLICT 175 175 S -> T (in Ref. 1; BAA08146 and 2;
AAK96030/AAK98640). {ECO:0000305}.
CONFLICT 211 211 L -> P (in Ref. 2; AAK98640).
{ECO:0000305}.
CONFLICT 217 217 V -> A (in Ref. 2; AAK98640).
{ECO:0000305}.
CONFLICT 463 463 Q -> H (in Ref. 4; BAE27842).
{ECO:0000305}.
CONFLICT 553 553 A -> T (in Ref. 2; AAK98640).
{ECO:0000305}.
CONFLICT 622 622 P -> S (in Ref. 2; AAK98640).
{ECO:0000305}.
CONFLICT 1061 1061 D -> E (in Ref. 2; AAK98640).
{ECO:0000305}.
CONFLICT 1126 1126 Y -> D (in Ref. 2; AAN11409).
{ECO:0000305}.
CONFLICT 1133 1133 E -> K (in Ref. 2; AAN11409).
{ECO:0000305}.
SEQUENCE 1238 AA; 136769 MW; E525D346A2C60335 CRC64;
MKPAARETRT PPRSPGLRWA LLPLLLLLRQ GQVLCAGAAP NPIFDIEAVV SPTSVLLTWK
HNDSGASECR IENKMESNLT FPVKNQTSCN ITGLSPGTSY TFSIISVTTN ETLNKTITTE
PWPVSDLHVT SVGVTQARLT WSNANGTASY RMLIEELTTH SSVNISGLKP GTNNSFAFPE
SNETQADFAV AEEVPDANGT KRIPVTNLSQ LHKNSLVSVD PPSGQDPSLT EILLTDLKPD
TQYNATIYSQ AANGTEGQPR NKVFKTNSTQ VSDVRAMNIS ASSMTLTWKS NYDGSRTSIV
YKIHVAGGTH SVNQTVNKTE AIILGLSSST LYNITVHPFL GQTEGTPGFL QVYTSPDQVS
DFRVTNVSTR AIGLAWRSND SKSFEIFIKQ DGGEKHRNAS TGNQSYMVED LKPGTSYHFE
IIPRGPDGTE GLSSTVNGST DPSAVTDIRV VNISTTEMQL EWQNTDDASG YTYHLVLESK
SGSIIRTNSS QKWITVGSLT PGTLYNVTIF PEVDQIQGIS NSITQYTRPS SVSHIEVNTT
TTTAAIRWKN EDAASASYAY SVLILKTGDG SNVTSNFTKD PSILIPELIP GVSYTVKILT
QVGDGTTSLV PGWNLFCTEP EPVTSFHCEV VPKEPALVLK WACPFGMYTG FELGVRSDSW
DNMTRLENCT SDDDTECRTE VAYLNFSTSY NISIATLSCG KMALPAQNIC TTGITDPPTP
DGSPNITSVS HNSVKVKFSG FEASHGPIKA YAVILTTGEA AQPSADVLKY TYEDFKRGAS
DTYVTYLIRI EEKGQSQGLS EVLNYEIDVG NQSTTLGYYN GRLEPLGSYR ACVAGFTNIT
YNLQNDGLIN GDESYVSFSP YSEAVFLPQD PGVICGAVFG CIFGALAITA VGGFIFWRKK
RTDAKNNEVS FSQIKPKKSK LIRVENFEAY FKKQQADSNC GFAEEYEDLK LIGISLPKYT
AEIAENRGKN RYNNVLPYDI SRVKLSVQTH STDDYINANY MPGYHSKKDF IATQGPLPNT
LKDFWRMVWE KNVYAIVMLT KCVEQGRTKC EEYWPSKQAQ DYGDITVAMT SEVVLPEWTI
RDFVVKNMQN SESHPLRQFH FTSWPDHGVP DTTDLLINFR YLVRDYMKQI PPESPILVHC
SAGVGRTGTF IAIDRLIYQI ENENTVDVYG IVYDLRMHRP LMVQTEDQYV FLNQCVLDII
RAQKDSKVDL IYQNTTAMTI YENLEPVSMF GKTNGYIA


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