CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001364
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphatidylinositol phosphatase PTPRQ 
Protein Synonyms/Alias
 Protein-tyrosine phosphatase receptor-type expressed by glomerular mesangial cells protein 1; rPTP-GMC1; Receptor-type tyrosine-protein phosphatase Q; PTP-RQ; R-PTP-Q 
Gene Name
 Ptprq 
Gene Synonyms/Alias
 Ptpgmc1 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
1984LSYRKSIKPISKKSFacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
 Phosphatidylinositol phosphatase required for auditory function. May act by regulating the level of phosphatidylinositol 4,5-bisphosphate (PIP2) level in the basal region of hair bundles. Can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates. Phosphate can be hydrolyzed from the D3 and D5 positions in the inositol ring. Has low tyrosine-protein phosphatase activity; however, the relevance of such activity in vivo is unclear. Plays an important role in adipogenesis of mesenchymal stem cells (MSCs). Regulates the phosphorylation state of AKT1 by suppressing the phosphatidylinositol 3,4,5-trisphosphate (PIP3) level in MSCs and preadipocyte cells (By similarity). 
Sequence Annotation
 DOMAIN 58 152 Fibronectin type-III 1.
 DOMAIN 157 251 Fibronectin type-III 2.
 DOMAIN 307 394 Fibronectin type-III 3.
 DOMAIN 399 490 Fibronectin type-III 4.
 DOMAIN 474 566 Fibronectin type-III 5.
 DOMAIN 567 660 Fibronectin type-III 6.
 DOMAIN 667 756 Fibronectin type-III 7.
 DOMAIN 761 851 Fibronectin type-III 8.
 DOMAIN 856 945 Fibronectin type-III 9.
 DOMAIN 950 1048 Fibronectin type-III 10.
 DOMAIN 1055 1148 Fibronectin type-III 11.
 DOMAIN 1153 1240 Fibronectin type-III 12.
 DOMAIN 1245 1338 Fibronectin type-III 13.
 DOMAIN 1343 1427 Fibronectin type-III 14.
 DOMAIN 1433 1536 Fibronectin type-III 15.
 DOMAIN 1541 1639 Fibronectin type-III 16.
 DOMAIN 1644 1743 Fibronectin type-III 17.
 DOMAIN 2006 2262 Tyrosine-protein phosphatase.
 ACT_SITE 2203 2203 Phosphocysteine intermediate (By
 CARBOHYD 54 54 N-linked (GlcNAc...) (Potential).
 CARBOHYD 162 162 N-linked (GlcNAc...) (Potential).
 CARBOHYD 169 169 N-linked (GlcNAc...) (Potential).
 CARBOHYD 318 318 N-linked (GlcNAc...) (Potential).
 CARBOHYD 354 354 N-linked (GlcNAc...) (Potential).
 CARBOHYD 389 389 N-linked (GlcNAc...) (Potential).
 CARBOHYD 733 733 N-linked (GlcNAc...) (Potential).
 CARBOHYD 746 746 N-linked (GlcNAc...) (Potential).
 CARBOHYD 904 904 N-linked (GlcNAc...) (Potential).
 CARBOHYD 998 998 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1010 1010 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1040 1040 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1251 1251 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1256 1256 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1805 1805 N-linked (GlcNAc...) (Potential).  
Keyword
 Alternative splicing; Cell membrane; Complete proteome; Glycoprotein; Hydrolase; Membrane; Protein phosphatase; Receptor; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2302 AA 
Protein Sequence
MMDFHFSFLF LLIGTSESQV DVSSSFDGTG YDITLSSVSA TTYSSPVSRT LATNVTKPGP 60
PVFLAGERVG SAGILLSWNT PPNPNGRIIS YVVKYKEVCP WMQTAYTRAR AKPDSLEVLL 120
TNLNPGTTYE IKVAAENNAG IGVFSDPFLF QTAESAPGKV VNLTVEALNY SAVNLIWYLP 180
RQPNGKITSF KISVKHARSG IVVKDVSLRV EDILSGKLPE CNENSESFLW STTSPSPTLG 240
RVTPTVRTTQ SSSTAARSKI SSVWKEPISF VVTHLRPYTT YLFEVSAVTT EAGYIDSTIV 300
RTPESVPEGP PQNCIMGNVT GKAFSISWDP PTIVTGKFSY RVELYGPSGR ILDNSTKDLR 360
FAFTHLTPFT MYDVYVAAET SAGVGPKSNL SVFTPPDVPG AVFDLQIAEV EATEIRITWR 420
KPRQPNGIIS QYRVKVSVLE TGVVLENTLL TGQDESISNP MSPEIMNLVD PMIGFYEGSG 480
EMSSDLHSPA SFIYNSHPHN DFPASTRAEE QSSPVVTTRN QYMTDITAEQ LSYVVRRLVP 540
FTEHTISVSA FTIMGEGPPT VLTVRTREQV PSSIQIINYK NISSSSILLY WDPPEYPNGK 600
ITHYTIYATE LDTNRAFQMT TVDNSFLITG LKKYTRYKMR VAASTHVGES SLSEENDIFV 660
RTPEDEPESS PQDVQVTGVS PSELRLKWSP PEKPNGIIIA YEVLYQNADT LFVKNTSTTD 720
IIISDLKPYT LYNISIRSYT RLGHGNQSSS LLSVRTSETV PDSAPENITY KNISSGEIEI 780
SFLPPRSPNG IIQKYTIYLK RSNSHEARTI NTTSLTQTIG GLKKYTHYVI EVSASTLKGE 840
GIRSRPISIL TEEDAPDSPP QNFSVKQLSG VTVMLSWQPP LEPNGIILYY TVYVWDKSSL 900
RAINATEASL VLSDLDYNVD YGACVTASTR FGDGNARSSI INFRTPEGEP SDPPNDVHYV 960
NLSSSSIILF WTPPVKPNGI IQYYSVYYQN TSGTFVQNFT LLQVTKESDN VTVSARIYRL 1020
AIFSYYTFWL TASTSVGNGN KSSDIIHVYT DQDIPEGPVG NLTFESISST AIHVSWEPPS 1080
QPNGLVFYYL SLNLQQSPPR HMIPPLVTYE NSIDFDDLEK YTDYIFKITP STEKGFSETY 1140
TTQLHIKTEE DVPDTPPIIN TFKNLSSTSI LLSWDPPLKP NGAILGYHLT LQGPHANHTF 1200
VTSGNHIVLE ELSPFTLYSF FAAARTMKGL GPSSILFFYT DESAPLAPPQ NLTLINYTSD 1260
FVWLTWSPSP LPGGIVKVYS FKIHEHETDT VFYKNISGLQ TDAKLEGLEP VSTYSVSVSA 1320
FTKVGNGNQY SNVVEFTTQE SVPEAVRNIE CVARDWQSVS VRWDPPRKTN GIIIHYMITV 1380
GGNSTKVSPR DPTYTFTKLL PNTSYVFEVR ASTSAGEGNE SRCDISTLPE TVPSAPTNVA 1440
FSNVQSTSAT LTWTKPDTIF GYFQNYKITT QLRAQKCREW EPEECIEHQK DQYLYEANQT 1500
EETVHGLKKF RWYRFQVAAS TNVGYSNASE WISTQTLPGP PDGPPENVHV VATSPFGINI 1560
SWSEPAVITG PTFYLIDVKS VDDDDFNISF LKSNEENKTT EINNLEVFTR YSVVITAFVG 1620
NVSRAYTDGK SSAEVIITTL ESVPKDPPNN MTFQKIPDEV TKFQLTFLPP SQPNGNIRVY 1680
QALVYREDDP TAVQIHNFSI IQKTDTSIIA MLEGLKGGHT YNISVYAINS AGAGPKVQMR 1740
ITMDIKAPAR PKSKPIPIRD ATGKLLVTST TITIRMPICY YNDDHGPIRN VQVLVAETGA 1800
QQDGNVTKWY DAYFNKARPY FTNEGFPNPP CIEGKTKFSG NEEIYVIGAD NACMIPGNEE 1860
KICNGPLKPK KQYLFKFRAT NVMGQFTDSE YSDPIKTLGE GLSERTVEII LSVTLCILSI 1920
ILLGTAIFAF VRIRQKQKEG GTYSPRDAEI IDTKFKLDQL ITVADLELKD ERLTRLLSYR 1980
KSIKPISKKS FLQHVEELCT NSNLKFQEEF SELPKFLQDL SSTDADLPWN RAKNRFPNIK 2040
PYNNNRVKLI ADVSLPGSDY INASYVSGYL CPNEFIATQG PLPGTVGDFW RMVWETRTKT 2100
LVMLTQCFEK GRIRCHQYWP EDNKPVTVFG DIVITKLMED IQIDWTIRDL KIERHGDCMT 2160
VRQCNFTGWP EHGVPENTTP LIHFVKLVRT SRAHDTTPMV VHCSAGVGRT GVFIALDHLT 2220
QHINNHDFVD IYGLVAELRS ERMCMVQNLA QYIFLHQCIL DLLSNKGGHQ PVCFVNYSTL 2280
QKMDSLDAME GDVELEWEET TM 2302 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
 GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC.
 GO:0045598; P:regulation of fat cell differentiation; ISS:UniProtKB. 
Interpro
 IPR003961; Fibronectin_type3.
 IPR013783; Ig-like_fold.
 IPR000387; Tyr/Dual-sp_Pase.
 IPR016130; Tyr_Pase_AS.
 IPR000242; Tyr_Pase_rcpt/non-rcpt. 
Pfam
 PF00041; fn3
 PF00102; Y_phosphatase 
SMART
 SM00060; FN3
 SM00194; PTPc 
PROSITE
 PS50853; FN3
 PS00383; TYR_PHOSPHATASE_1
 PS50056; TYR_PHOSPHATASE_2
 PS50055; TYR_PHOSPHATASE_PTP 
PRINTS
 PR00700; PRTYPHPHTASE.