ID A0A452J4U5_9SAUR Unreviewed; 1564 AA.
AC A0A452J4U5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000035497.1};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000035497.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000035497.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}.
CC -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC {ECO:0000256|ARBA:ARBA00007881}.
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DR Ensembl; ENSGAGT00000040201.1; ENSGAGP00000035497.1; ENSGAGG00000025231.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd01213; PTB_tensin; 1.
DR CDD; cd14562; PTP_tensin-2; 1.
DR CDD; cd09927; SH2_Tensin_like; 1.
DR Gene3D; 2.60.40.1110; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR013625; PTB.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR035012; Tensin-like_SH2.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR InterPro; IPR033929; Tensin_PTB.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR45734; TENSIN; 1.
DR PANTHER; PTHR45734:SF1; TENSIN-2; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF08416; PTB; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 9..57
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 100..272
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 184..244
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 277..403
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1292..1401
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 473..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..877
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1564 AA; 170503 MW; 66A3213E45757496 CRC64;
MKPEKVPEPH SFKEKAFKKK KKACVVCKES IEALGLVCQA CKIASHKKCE AKVVSSCQPL
PPPELRRNTA PARRIEHLGS TKSLHTSKQR STLPRSFSLD HVMERKYDFD LTYITERIIS
VFFPPALEEQ RYRGNLREVA QMLKSKHEDK YTLFNLSEKR HDISRLNPKV QDFGWPDLHA
PPLDKICSIC KAMETWLNSD PQHVVVLHCK GNKGKTGVIV AAYMHYSKIS ASADQALSTL
TMRKFCEDKV AASLQPSQKR YISYFSGLLS GTIKMNSNTL FLHHVLIPAI PNYEASGGYQ
PFLKIYQSMQ LVYTSGIYSV PGPSPQKLCV TLEPALLLKG DVMVKCYHKQ TCSSDRDVVF
RVQFHTCTIH GAQLWFGKDE LDEAWQDERF PFEASVEFVF SSGPEKMKGL ETLRNSPAIT
VDYNISDPMV RWDSYENFNL RHEDSLEDMA HTRGPIDGSL YAKIKKKRNL SGFSAGGGSP
ASADSTQPGS RFLSVSSDSG HSSMLAEPSP PAKLLPTPAE REELDRLLGG FGVKARPETP
KQQRGASPHQ ELGRCPHSNG ARDRETAILE DDLVEMSPFG PLPYPSRRPG LARHCSCRLG
YRSQSCPGTH SPERLPSGAY YRPEGTLERR RLVYSTNGVH LHPAEGYPCL PQEAGPGEKR
RVYRSLSEGL QPLAHPYVYE LPHSSSKRED LAYKPPSYRE VLLLEEEPGC GLELCPCQDC
QEKAHEEAGL PPTTAFYGLH LGSREPEEWA HESAKSPLSR AGHPGQPVPL LMPAAYSQRT
RGHHEVFDFE PAHAKMPTHF GHGYPAQPMP GTHQKGHQGM EQSLETFHYR YGPPYPTLLP
HGAYACGTPT QCPQPPFYGR SPARPCTSPP DMRPYTPGYH SPPSGSASPV SSAYPASRNQ
SYEPQSPETG QGYPHPGHQD QIPAEMQGRG EEAPWRDVPG SLHQPHREAH ATCPAPSELS
GPPTPLHTSS PVQSKDSPAM PKGGTPAASL QESSACSSPE EMAPPSAKRT PEMSSALPGA
APSPTQPPSP TQACGHGATS RAQANGPALR QPCPRAHSLA SPPQGTGLSR VNPGEAPSHL
NGPSCPAVSP DSPPRNGTPA HLLPPGMDRL AQRSPLGTPV HSQACTSCRA TATLRNPASY
NGHLPSDRAE LAPGTLARCP NGSPLQSPIA SYSPSDLQCS PTPAFPIATA YYPGRERSPP
PPGSPSQGHA RDSPQQPPLP EKRHTLVAGN WERSSPPGRG TGTGHHVTFA PDTARPDPAS
PSGSPGARSS LSDMQPESHS NVKFVQDTSK FWYKPNLSRD QAIAMLKDKE PGCFLIRDSN
SFQGAYGLAL KVATPPANCL TLPSKGDPME QLVRHFLIET GPKGVKIKGC QNEPYFGSLP
ALVSQHSITP ISLPCKLRIP SRDPMEETSD VAIPTNVSTA ADLLKQGAAC SVLYLSSVET
ESLTGPQAVA KAAASTLSCS PRPLACLVHF KVSAQGITLT DNQRKLFFRR HYPVNSITFC
STDPQDRRWT NPDGTTSKLF GFVAKKQGSP CENVCHLFAE LDPEQPALAI VNFITKVMLG
PHRK
//
