PTPRN_MOUSE
ID PTPRN_MOUSE Reviewed; 979 AA.
AC Q60673; E9Q746; Q62129;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase-like N;
DE Short=R-PTP-N;
DE AltName: Full=PTP IA-2 {ECO:0000305};
DE Contains:
DE RecName: Full=ICA512-N-terminal fragment;
DE Short=ICA512-NTF;
DE Contains:
DE RecName: Full=ICA512-transmembrane fragment;
DE Short=ICA512-TMF;
DE Contains:
DE RecName: Full=ICA512-cleaved cytosolic fragment;
DE Short=ICA512-CCF;
DE Flags: Precursor;
GN Name=Ptprn; Synonyms=Ptp35;
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], LACK OF FUNCTION AS PROTEIN TYROSINE
RP PHOSPHATASE, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=7980563; DOI=10.1006/bbrc.1994.2549;
RA Lu J., Notkins A.L., Lan M.S.;
RT "Isolation, sequence and expression of a novel mouse brain cDNA, mIA-2, and
RT its relatedness to members of the protein tyrosine phosphatase family.";
RL Biochem. Biophys. Res. Commun. 204:930-936(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Swiss Webster; TISSUE=Fibroblast;
RX PubMed=8526904; DOI=10.1006/bbrc.1995.2758;
RA Magistrelli G., Covini N., Mosca M., Lippoli G., Isacchi A.;
RT "Expression of PTP35, the murine homologue of the protein tyrosine
RT phosphatase-related sequence IA-2, is regulated during cell growth and
RT stimulated by mitogens in 3T3 fibroblasts.";
RL Biochem. Biophys. Res. Commun. 217:154-161(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP LACK OF FUNCTION AS PROTEIN TYROSINE PHOSPHATASE, AND MUTAGENESIS OF
RP ALA-877 AND ASP-911.
RX PubMed=8878556; DOI=10.1006/bbrc.1996.1549;
RA Magistrelli G., Toma S., Isacchi A.;
RT "Substitution of two variant residues in the protein tyrosine phosphatase-
RT like PTP35/IA-2 sequence reconstitutes catalytic activity.";
RL Biochem. Biophys. Res. Commun. 227:581-588(1996).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12031972; DOI=10.2337/diabetes.51.6.1842;
RA Saeki K., Zhu M., Kubosaki A., Xie J., Lan M.S., Notkins A.L.;
RT "Targeted disruption of the protein tyrosine phosphatase-like molecule IA-2
RT results in alterations in glucose tolerance tests and insulin secretion.";
RL Diabetes 51:1842-1850(2002).
RN [6]
RP FUNCTION, SELF-ASSOCIATION, AND INTERACTION WITH PTPRN2; PTPRA AND PTPRE.
RX PubMed=12364328; DOI=10.1074/jbc.m208228200;
RA Gross S., Blanchetot C., Schepens J., Albet S., Lammers R., den Hertog J.,
RA Hendriks W.;
RT "Multimerization of the protein-tyrosine phosphatase (PTP)-like insulin-
RT dependent diabetes mellitus autoantigens IA-2 and IA-2beta with receptor
RT PTPs (RPTPs). Inhibition of RPTPalpha enzymatic activity.";
RL J. Biol. Chem. 277:48139-48145(2002).
RN [7]
RP FUNCTION.
RX PubMed=15939893; DOI=10.1073/pnas.0408887102;
RA Harashima S., Clark A., Christie M.R., Notkins A.L.;
RT "The dense core transmembrane vesicle protein IA-2 is a regulator of
RT vesicle number and insulin secretion.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:8704-8709(2005).
RN [8]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16269463; DOI=10.1210/en.2005-0638;
RA Kubosaki A., Nakamura S., Clark A., Morris J.F., Notkins A.L.;
RT "Disruption of the transmembrane dense core vesicle proteins IA-2 and IA-
RT 2beta causes female infertility.";
RL Endocrinology 147:811-815(2006).
RN [9]
RP FUNCTION.
RX PubMed=18178618; DOI=10.1073/pnas.0710931105;
RA Mziaut H., Kersting S., Knoch K.P., Fan W.H., Trajkovski M., Erdmann K.,
RA Bergert H., Ehehalt F., Saeger H.D., Solimena M.;
RT "ICA512 signaling enhances pancreatic beta-cell proliferation by regulating
RT cyclins D through STATs.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:674-679(2008).
RN [10]
RP FUNCTION.
RX PubMed=19019914; DOI=10.1152/ajprenal.90543.2008;
RA Kim S.M., Theilig F., Qin Y., Cai T., Mizel D., Faulhaber-Walter R.,
RA Hirai H., Bachmann S., Briggs J.P., Notkins A.L., Schnermann J.;
RT "Dense-core vesicle proteins IA-2 and IA-2{beta} affect renin synthesis and
RT secretion through the {beta}-adrenergic pathway.";
RL Am. J. Physiol. 296:F382-F389(2009).
RN [11]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=19361477; DOI=10.1016/j.neuroscience.2009.01.022;
RA Nishimura T., Kubosaki A., Ito Y., Notkins A.L.;
RT "Disturbances in the secretion of neurotransmitters in IA-2/IA-2beta null
RT mice: changes in behavior, learning and lifespan.";
RL Neuroscience 159:427-437(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307 AND SER-308, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [13]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=21732083; DOI=10.1007/s00125-011-2221-6;
RA Cai T., Hirai H., Zhang G., Zhang M., Takahashi N., Kasai H., Satin L.S.,
RA Leapman R.D., Notkins A.L.;
RT "Deletion of Ia-2 and/or Ia-2beta in mice decreases insulin secretion by
RT reducing the number of dense core vesicles.";
RL Diabetologia 54:2347-2357(2011).
CC -!- FUNCTION: Plays a role in vesicle-mediated secretory processes
CC (PubMed:21732083). Required for normal accumulation of secretory
CC vesicles in hippocampus, pituitary and pancreatic islets. Required for
CC the accumulation of normal levels of insulin-containing vesicles and
CC preventing their degradation (PubMed:15939893, PubMed:21732083). Plays
CC a role in insulin secretion in response to glucose stimuli
CC (PubMed:12031972, PubMed:21732083). Required for normal accumulation of
CC the neurotransmitters norepinephrine, dopamine and serotonin in the
CC brain (PubMed:16269463). In females, but not in males, required for
CC normal accumulation and secretion of pituitary hormones, such as
CC luteinizing hormone (LH) and follicle-stimulating hormone (FSH)
CC (PubMed:16269463). Seems to lack intrinsic enzyme activity
CC (PubMed:7980563, PubMed:8878556). Required to maintain normal levels of
CC renin expression and renin release (PubMed:19019914). May regulate
CC catalytic active protein-tyrosine phosphatases such as PTPRA through
CC dimerization (PubMed:12364328). {ECO:0000250|UniProtKB:Q16849,
CC ECO:0000269|PubMed:12031972, ECO:0000269|PubMed:12364328,
CC ECO:0000269|PubMed:15939893, ECO:0000269|PubMed:19019914,
CC ECO:0000269|PubMed:7980563, ECO:0000269|PubMed:8878556}.
CC -!- FUNCTION: [ICA512-transmembrane fragment]: ICA512-TMF regulates
CC dynamics and exocytosis of insulin secretory granules (SGs); binding of
CC ICA512-TMF to SNTB2/beta-2-syntrophin is proposed to restrain SGs
CC mobility and exocytosis by tethering them to the actin cytoskeleton
CC depending on UTRN; the function is inhibited by cytoplasmic ICA512-CFF
CC dimerizing with ICA512-TMF and displacing SNTB2 (By similarity).
CC {ECO:0000250|UniProtKB:Q16849}.
CC -!- FUNCTION: [ICA512-cleaved cytosolic fragment]: ICA512-CCF translocated
CC to the nucleus promotes expression of insulin and other granule-related
CC genes; the function implicates binding to and regulating activity of
CC STAT5B probably by preventing its dephosphorylation and potentially by
CC inducing its sumoylation by recruiting PIAS4 (By similarity). Enhances
CC pancreatic beta-cell proliferation by converging with signaling by
CC STAT5B and STAT3 (PubMed:18178618). ICA512-CCF located in the cytoplasm
CC regulates dynamics and exocytosis of insulin secretory granules (SGs)
CC by dimerizing with ICA512-TMF and displacing SNTB2 thus enhancing SGs
CC mobility and exocytosis (By similarity). {ECO:0000250|UniProtKB:Q16849,
CC ECO:0000269|PubMed:18178618}.
CC -!- SUBUNIT: Homodimer; shown for the unprocessed protein (proICA512) in
CC the endoplasmic reticulum and resolved during protein maturation as
CC ICA512-TMF seems to be predominantly monomeric in secretory granules;
CC however, ICA512-CCF interacts with ICA512-TMF disrupting the ICA512-
CC TMF:SNTB2 complex. The isolated lumenal RESP18 homology domain has been
CC shown to form disulfide-linked homooligomers. Interacts (via
CC cytoplasmic domain) with phosphorylated SNTB2; this protects PTPRN
CC against cleavage by CAPN1 to produce ICA512-CCF. Dephosphorylation of
CC SNTB2 upon insulin stimulation disrupts the interaction and results in
CC PTPRN cleavage. Interacts with SNX19. ICA512-CCF interacts with PIAS4;
CC in the nucleus. Interacts with STAT5B (phosphorylated); down-regulated
CC by ICA512-CCF sumoylation; ICA512-CCF prevents STAT5B
CC dephosphorylation; ICA512-CCF mediates interaction of STAT5B with
CC PIAS4. Interacts (via RESP18 homology domain) with insulin and
CC proinsulin (By similarity). Interacts with PTPRN2, PTPRA and PTPRE
CC (PubMed:12364328). {ECO:0000250|UniProtKB:Q16849,
CC ECO:0000269|PubMed:12364328}.
CC -!- INTERACTION:
CC Q60673; P18052: Ptpra; NbExp=3; IntAct=EBI-8328895, EBI-6597520;
CC Q60673; P80560: Ptprn2; NbExp=4; IntAct=EBI-8328895, EBI-8538944;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q63259}; Single-
CC pass type I membrane protein {ECO:0000250|UniProtKB:Q63259}.
CC Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000269|PubMed:19361477}; Single-pass type I membrane protein
CC {ECO:0000305}. Perikaryon {ECO:0000250|UniProtKB:Q63259}. Cell
CC projection, axon {ECO:0000250|UniProtKB:Q63259}. Synapse
CC {ECO:0000250|UniProtKB:Q63259}. Cell membrane
CC {ECO:0000250|UniProtKB:Q63259}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q63259}. Endosome
CC {ECO:0000250|UniProtKB:Q63259}. Note=Detected on neuronal secretory
CC vesicles, but not on synaptic vesicles. Colocalizes with insulin-
CC containing secretory granules. Primarily detected on secretory vesicle
CC membranes. Transiently found at the cell membrane, when secretory
CC vesicles fuse with the cell membrane to release their cargo. Is then
CC endocytosed and recycled to secretory vesicles via the Golgi apparatus
CC membranes. {ECO:0000250|UniProtKB:Q63259}.
CC -!- SUBCELLULAR LOCATION: [ICA512-transmembrane fragment]: Cytoplasmic
CC vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q63259}.
CC -!- SUBCELLULAR LOCATION: [ICA512-cleaved cytosolic fragment]: Nucleus
CC {ECO:0000250|UniProtKB:Q16849}.
CC -!- TISSUE SPECIFICITY: Detected in pituitary (PubMed:16269463). Detected
CC in brain (at protein level) (PubMed:12031972, PubMed:16269463,
CC PubMed:19361477). Detected in brain (PubMed:7980563, PubMed:12031972).
CC Weakly expressed in the colon, intestine, stomach and pancreas
CC (PubMed:7980563). {ECO:0000269|PubMed:12031972,
CC ECO:0000269|PubMed:16269463, ECO:0000269|PubMed:19361477,
CC ECO:0000269|PubMed:7980563}.
CC -!- DOMAIN: The RESP18 homology domain is sufficient for targeting
CC proICA512 to secretory granules. {ECO:0000250|UniProtKB:Q16849}.
CC -!- PTM: Subject to proteolytic cleavage at multiple sites. Subject to
CC cleavage on a pair of basic residues. On exocytosis of secretory
CC granules in pancreatic beta-cells ICA512-TMF is transiently inserted in
CC the plasma-membrane and cleaved by mu-type calpain CPN1 to yield
CC ICA512-CCF. {ECO:0000250|UniProtKB:P56722,
CC ECO:0000250|UniProtKB:Q16849, ECO:0000250|UniProtKB:Q63259}.
CC -!- PTM: O-glycosylated. {ECO:0000250|UniProtKB:Q16849}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q16849}.
CC -!- PTM: Sumoylated at two sites including Lys-754. Sumoylation decreases
CC interaction with STAT5. {ECO:0000250|UniProtKB:Q16849}.
CC -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate,
CC appear healthy and normal, but show impaired glucose tolerance and
CC impaired insulin secretion in response to glucose (PubMed:12031972).
CC Pancreatic islets from mice lacking both Ptprn and Ptprn2 contain
CC decreased numbers of insulin-containing vesicles and show a further
CC decrease in insulin secretion after glucose stimuli (PubMed:21732083).
CC Mice lacking both Ptprn and Ptprn2 appear normal, but have lower levels
CC of the neurotransmitters norepinephrine, dopamine and serotonin in the
CC brain. Likewise, they have decreased numbers of synaptic vesicles in
CC the hippocampus and show decreased neurotransmitter release after K(+)
CC stimulation; basal levels of neurotransmitter release are unaffected.
CC They show increased anxiety-like behavior with strongly decreased
CC exploratory activity and rearing. Besides, they show defects in
CC remembering conditioned learning. With increasing age, mutant mice
CC develop a tendency to suffer seizures and display a reduced life span;
CC roughly half of the mutant mice are dead after 40 weeks
CC (PubMed:19361477). The majority of female mice deficient in both Ptprn
CC and Ptprn2 are infertile or have small litters, due to abnormalities of
CC the estrous cycle and absence of corpora lutea. These defects are due
CC to decreased levels of luteinizing hormone and follicle-stimulating
CC hormone (FSH) in the pituitary and decreased levels of luteinizing
CC hormone (LH) in the blood plasma. In contrast, male mice lacking both
CC Ptprn and Ptprn2 display normal hormone levels and normal fertility
CC (PubMed:16269463). {ECO:0000269|PubMed:12031972,
CC ECO:0000269|PubMed:16269463}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 8 subfamily. {ECO:0000305}.
CC -!- CAUTION: Does not possess catalytic activity due to replacement of
CC highly conserved residues in tyrosine-protein phosphatase domain.
CC {ECO:0000305|PubMed:8878556}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA52453.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U11812; AAA52102.1; -; mRNA.
DR EMBL; X74438; CAA52453.1; ALT_INIT; mRNA.
DR EMBL; AC166150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; I48721; I48721.
DR PIR; JC2349; JC2349.
DR AlphaFoldDB; Q60673; -.
DR SMR; Q60673; -.
DR IntAct; Q60673; 4.
DR MINT; Q60673; -.
DR STRING; 10090.ENSMUSP00000027404; -.
DR GlyConnect; 2672; 1 N-Linked glycan (1 site).
DR GlyGen; Q60673; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q60673; -.
DR PhosphoSitePlus; Q60673; -.
DR MaxQB; Q60673; -.
DR PaxDb; Q60673; -.
DR PRIDE; Q60673; -.
DR ProteomicsDB; 301948; -.
DR UCSC; uc011wnn.1; mouse.
DR MGI; MGI:102765; Ptprn.
DR eggNOG; KOG0793; Eukaryota.
DR InParanoid; Q60673; -.
DR ChiTaRS; Ptprn; mouse.
DR PRO; PR:Q60673; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q60673; protein.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051020; F:GTPase binding; ISO:MGI.
DR GO; GO:0030507; F:spectrin binding; ISO:MGI.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; ISO:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:MGI.
DR GO; GO:1990502; P:dense core granule maturation; ISO:MGI.
DR GO; GO:0030073; P:insulin secretion; ISO:MGI.
DR GO; GO:0035773; P:insulin secretion involved in cellular response to glucose stimulus; IMP:UniProtKB.
DR GO; GO:0001553; P:luteinization; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:1904692; P:positive regulation of type B pancreatic cell proliferation; IMP:UniProtKB.
DR GO; GO:0051046; P:regulation of secretion; IBA:GO_Central.
DR GO; GO:0000302; P:response to reactive oxygen species; ISS:UniProtKB.
DR Gene3D; 3.30.70.2470; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR033522; IA-2/IA-2_beta.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR021613; Receptor_IA-2_dom.
DR InterPro; IPR038112; Receptor_IA-2_ectodomain_sf.
DR InterPro; IPR029403; RESP18_dom.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR46106; PTHR46106; 1.
DR Pfam; PF11548; Receptor_IA-2; 1.
DR Pfam; PF14948; RESP18; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
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 Cell membrane; Cell projection; Cytoplasmic vesicle; Disulfide bond;
KW Endosome; Glycoprotein; Isopeptide bond; Membrane; Nucleus; Phosphoprotein;
KW Receptor; Reference proteome; Signal; Synapse; Transcription;
KW Transcription regulation; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..37
FT /evidence="ECO:0000250"
FT CHAIN 38..979
FT /note="Receptor-type tyrosine-protein phosphatase-like N"
FT /id="PRO_0000025452"
FT CHAIN 38..448
FT /note="ICA512-N-terminal fragment"
FT /evidence="ECO:0000250|UniProtKB:P56722,
FT ECO:0000250|UniProtKB:Q16849"
FT /id="PRO_0000438082"
FT CHAIN 449..979
FT /note="ICA512-transmembrane fragment"
FT /evidence="ECO:0000250|UniProtKB:P56722,
FT ECO:0000250|UniProtKB:Q16849"
FT /id="PRO_0000438083"
FT CHAIN 659..979
FT /note="ICA512-cleaved cytosolic fragment"
FT /evidence="ECO:0000250|UniProtKB:Q16849"
FT /id="PRO_0000438084"
FT TOPO_DOM 38..575
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 576..600
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 601..979
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 709..969
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 38..134
FT /note="RESP18 homology domain"
FT /evidence="ECO:0000250|UniProtKB:Q16849"
FT REGION 113..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..575
FT /note="Sufficient for dimerization of proICA512"
FT /evidence="ECO:0000250|UniProtKB:Q16849"
FT REGION 601..732
FT /note="Sufficient for dimerization of proICA512"
FT /evidence="ECO:0000250|UniProtKB:P80560"
FT REGION 644..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 448..449
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P56722"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43
FT /note="Interchain (with C-43 or C-50); in multimeric form"
FT /evidence="ECO:0000250|UniProtKB:Q16849"
FT DISULFID 50
FT /note="Interchain (with C-43 or C-50); in multimeric form"
FT /evidence="ECO:0000250|UniProtKB:Q16849"
FT DISULFID 56..65
FT /evidence="ECO:0000250|UniProtKB:Q16849"
FT CROSSLNK 754
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:Q16849"
FT MUTAGEN 877
FT /note="A->D: No effect on dephosphorylating activity;
FT increased the dephosphorylating efficiency; when associated
FT with 911-A."
FT /evidence="ECO:0000269|PubMed:8878556"
FT MUTAGEN 911
FT /note="D->A: Confers dephosphorylating activity; increased
FT the dephosphorylating efficiency; when associated with 877-
FT D."
FT /evidence="ECO:0000269|PubMed:8878556"
FT CONFLICT 166..169
FT /note="RSWG -> GDGAGA (in Ref. 2; CAA52453)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="L -> M (in Ref. 1; AAA52102)"
FT /evidence="ECO:0000305"
FT CONFLICT 615
FT /note="L -> V (in Ref. 2; CAA52453)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="T -> S (in Ref. 1; AAA52102)"
FT /evidence="ECO:0000305"
FT CONFLICT 859
FT /note="L -> V (in Ref. 2; CAA52453)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 979 AA; 106083 MW; AA3A7E126A3C5F3D CRC64;
MRRPRRPGGS GGSGGSGGLR LLVCLLLLSG RPGGCSAISA HGCLFDRRLC SHLEVCIQDG
LFGQCQAGVG QARPLLQVTS PVLQRLQGVL RQLMSQGLSW HDDLTQHVIS QEMERIPRLR
PPEPHPRDRS GLVPRKPGPA GELLTQGNPT GSSPAAQGFP RPAGGRSWGG SPLSSLQAEL
LPPLLEHLLM PPQPPHPALT YEPALLQPYL FHQFGSRDGS RGSESSSGVV GVGHLSKAEG
PALFSRSASK AILGTHSGHS FGDLTGPSPA QLFQDSGLLY MAQELPVPGR ARAPRLPENG
GNRAEDSSEG HEEEVLGGRG EKSPPQAAQP ELSLQRLTAV LAGYGVELRQ LTPEQFSTLL
TLLQLLPKGT GRNLEGAVNV GGADVKKTIQ QMQRGDPAEA LPPTPSLPGY LTASPASSEV
QQVLSPGFPE PPHTPSPLGS SSVLLEKKSP LGQSQPTVVG RPSARPSAEE YGYIVTDQKP
LSLVAGVRLL EILAEHVHMS SGSFINISVV GPAVTFRIRH NEQNLSLADV TQQAGLVKSE
LEAQTGLQIL QTGVGQREEA AEVLPRQAHG ISPMRSVLLT LVALAGVAGL LVALAVALCM
RHHSRQRDKE RLAALGPEGA HGDTTFEYQD LCRQHMATKS LFNRAEGQPE PSRVSSVSSQ
FSDAAQASPS SHSSTPSWCE EPAQANMDIS TGHMILAYME DHLRNRDRLA KEWQALCAYQ
AEPNTCAAAQ DESNIKKNRH PDFLPYDHAR IKLKVESSPS RSDYINASPI IEHDPRMPAY
IATQGPLSHT IADFWQMVWE SGCTVIVMLT PLVEDGVKQC DRYWPDEGSS LYHVYEVNLV
SEHIWCEDFL VRSFYLKNLQ TQETRTLTQF HFLSWPAEGT PASTRPLLDF RRKVNKCYRG
RSCPIIVHCS DGAGRTGTYI LIDMVLNRMA KGVKEIDIAA TLEHVRDQRP GLVRSKDQFE
FALTAVAEEV NAILKALPQ
