ID L5LN35_MYODS Unreviewed; 2754 AA.
AC L5LN35;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN ORFNames=MDA_GLEAN10007368 {ECO:0000313|EMBL:ELK26903.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK26903.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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;
CC Evidence={ECO:0000256|ARBA:ARBA00001490};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 3 subfamily. {ECO:0000256|ARBA:ARBA00025789}.
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DR EMBL; KB110664; ELK26903.1; -; Genomic_DNA.
DR eggNOG; KOG0791; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd00063; FN3; 13.
DR CDD; cd14617; R-PTPc-B; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 15.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 3.
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; IPR041201; PTPRJ_TM.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR008356; Tyr_Pase_KIM-con.
DR PANTHER; PTHR46957; CYTOKINE RECEPTOR; 1.
DR PANTHER; PTHR46957:SF3; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR Pfam; PF00041; fn3; 15.
DR Pfam; PF18861; PTP_tm; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR01778; KIMPTPASE.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 17.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 16.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50853; FN3; 10.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Receptor {ECO:0000313|EMBL:ELK26903.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2340..2366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 232..426
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 364..426
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 837..929
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1015..1102
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1103..1192
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1193..1282
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1366..1453
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1454..1544
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1630..1720
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1721..1811
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1984..2080
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2081..2172
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2421..2681
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 2596..2672
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 642..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 390
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR608356-50"
SQ SEQUENCE 2754 AA; 306620 MW; 4032C554AD317D1B CRC64;
MDVNKLNITL LRIFRQGVAA ALGLLPQQVH INRLIGKKNS VELFVSPINR KGGISDALPS
EEVLRSLNTN VLHQSLSQFG ITEVSPEILY RLKEKFQLSL RQDKEKNQEI HLSPLALQPA
QSEAKTANSM VQPEQAPKVL SVVVDPQGRH APEIKATTSV CPSPFKMKPI GLQERRGSNV
SLTLDMSSLG NVEPFVAVPT PREKVAMEYL QSASRILTRS QLRDVVASSH LLQSEFMEIP
MNFVDPKEID IPRHGTKNRY KTILPNPLSR VCLRPKNVTD SLSTYINANY IRGYSGREKA
FIATQGPMIN TVNDFWQMVW QEDSPVIVMI TKLKEKNEQG SHTQHVKHYW YTSWPDHKTP
DSAQPLLQLM LDVEEDRLAS AGRGPVVVHC SAGIGRTGCF IATSIGCRQL KEEGVVDPLS
IVCQLRVDSP PSSPCLPSVL STLAPVESGG FTSGSGTYLH PEEGPSSEKG FQIVHVQKQQ
CLFENKIVSM GSCNGTEKNQ QWMWTEDAKL LHLKSALCLG ISNSSGGPSR SAIFVHCSQA
PRWTCYEKTG FLEVKNASLF LKKQGTKAVV KKGRKYLHSW MKRDVNKEGK PVNESLCLKK
AGLGAEFSVR SIRNTSPPQI PTAFNAAPYS PDQLISNTTE AFTRTTPENS SRNSSQGQPP
SLQVTGSTET SSVPWTPRPF STTTEETGLG EPARCNFTVT ESGVSSRAAS LQWRTLGSPC
NFSFIYINDT SGFTKCHPRR IDNTTYECNP KDLQAGTVYN FRIVALDGEE RTVVLQTGAQ
CTNSCTLKGT VGREAAVGTG AGLGPFSVPL PSPFCHSPQS PVYQRPCSHV IVTDPLPPAR
FEISKEKTTS TSLHVGWTPS SGRVTWYEVQ LLDGHQKMQE AQIQESTSWN EYAFSNLTAG
SKYNIAITAV SGNKRSPTIH INGSTVPSPV KDIGISAKTN SLLISWSHGS GNVERYQLIL
MDKGILVHNV VVDKYATSYT FHGLTSGHLY NLTIVTEASG LQNRKWKLAR TTPTEVSNLK
VTNDGTLTSL KVKWQRPPGN VDSYNITLSH QGTITDSRTL APQVTETQFK GLTPGRLYQV
TISCVSGELS AQKMAVGRTV PEKVGNLEAN SNGSVRSLVV SWSPPAGDWE QYRILLFKDS
LVLLNITVGK EETHYVIDDI GLIPGRQYEV EVTVESGNLK NSKRCQGRTV PMAVLQLRVK
HANETSLGIM WQTPAAEWEK YIISLADRNL LLIHKSLPKE AKEFTFTDLV PGRKYIATVT
SISGDLKNSS STKGRTVPAQ VTGLHVANQG TTSSLFTNWT QAAGDIEFYQ VLLIHENVVI
KNESVSSETS TYSFHSLKSG SLYSVVVTTV SGGISSRQAV VEGRTVPSSV SGVTVNNSGR
NDYLSISWLP APGDVDNYVV TLSHDGKVVQ SLIIAKSVSE CSFSSLTPGR LYDVTITTRS
GKYENHSFSQ DRTVPDKVQG VSISNSARSD YLKVSWVHAT GDLDHYEVTI KNKNNFIQTK
SIPKSENECV FVKLVPGRLY SVTVSTKSGQ YEASEQGNGR TIPEPVKDLT LRNRSTNDLL
VTWSRADGDV DQYEIQLLFN DMKLLPSFHL GNTATEYRFT SLIPGRRYKI LVLTISGDVQ
QSAFIEGFTV PSTVKNIHVS PNGATDSLTV NWTPGEGDVD SYTVSAFRQN QKVESQTIPK
HISEHTFHRL EAGEQYQIVV ASVSGSLRNQ IDALGRTVPA SVQGIIADNV YSSHSLIVSW
QKAVGMAERY DILLLNENGI LLSNTSKPAT TKQHKFEDLT PGKKYKIQIL TVSGGLFSKE
AQTEGRTVPA AVTNLRITEN STRHLSFTWT TSEGELNWYN IFLYNPDRTL QDRAQVDPQV
QSFSFQNLLQ GRMYKMVIVT HSGELSNESS IFGRTVPASV SNLKGSNRNM TDSLWFSWSP
APGDFDFYEL ILYNPNGTKK ENWKEKDLTE WRFHGLVPGR KYTLCVVTHS GELSNKVTGQ
SRTAPSPPSL MSFADVANTS LAITWKGPPD WTDYDDFEVQ WLPRDAITVF NPYSNRKSEG
RIVYGLRPGR SYQFSVKTVS GDSWKTYSRP VSGSVRTKPD KIQNLHCRPQ NSTAIACSWI
PPDSDFDGYS IECRKMDTQE VEFSRKLEKE KSLLSIMMLV PHKRYLVSIK VQSAGVTSEV
VEDSTITMID RPPPPPPHIR VNKKDVLISK SSINFTFNCS WFSDTNGAVK YFTVVVREAD
GSDELKPEQQ HPLPSYLEYR HNASIRVYQT NYFASKCAES PDSNSKSFNI KLGAEMESLG
GKCDPNQLKF CDGPLKPRTA YRISIRAFTQ LFDEDLKEFT KPLYSDTFFS LPITTESEPF
FGVIEGVSAG LFLIGMLVAV VALFICRRRT SHGRERPSAQ LSIRRDRPLS VHLNLGQKGP
IKVNQFEGHF MKLQADSNYL LSKEYEDLKD VGRNQPCDIA LLPENRGKNR YNNILPYDAS
RVKLSNVDDD PCSDYINASY IPGNNFRREY IATQGPLPGT KDDFWKMAWE QNVHNIVMVT
QCVEKGRVKC DHYWPADQDS LYYGDLILQM LSESVLPEWT IREFRICSEE QLDTHRLIRH
FHYTVWPDHG VPETTQSLIQ FVRTVRDYIN RTPGAGPTVV HCSAGVGRTG TFIALDRILQ
QLDSKDSVDI YGAVHDLRLH RVHMVQTECQ YVYLHQCVRD VLRARKLRSE QENPLFPIYE
NVNPEYHREA QAKVVSSGAA VQGRAAVWRA VVEKGVKRSD EFLHQEECHL DPCL
//
