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Database: UniProt
Entry: A0A3Q0G5B8_ALLSI
LinkDB: A0A3Q0G5B8_ALLSI
Original site: A0A3Q0G5B8_ALLSI 
ID   A0A3Q0G5B8_ALLSI        Unreviewed;      1903 AA.
AC   A0A3Q0G5B8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=PTPRD {ECO:0000313|RefSeq:XP_025053308.1};
OS   Alligator sinensis (Chinese alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025053308.1};
RN   [1] {ECO:0000313|RefSeq:XP_025053308.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 2A subfamily. {ECO:0000256|ARBA:ARBA00010504}.
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DR   RefSeq; XP_025053308.1; XM_025197523.1.
DR   Proteomes; UP000189705; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd00063; FN3; 8.
DR   CDD; cd05738; IgI_2_RPTP_IIa_LAR_like; 1.
DR   CDD; cd05739; IgI_3_RPTP_IIa_LAR_like; 1.
DR   CDD; cd14628; R-PTP-D-2; 1.
DR   CDD; cd14624; R-PTPc-D-1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 11.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR045905; R-PTP-delta_cat.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR46957; CYTOKINE RECEPTOR; 1.
DR   PANTHER; PTHR46957:SF8; PROTEIN TYROSINE PHOSPHATASE RECEPTOR TYPE S; 1.
DR   Pfam; PF00041; fn3; 7.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00014; FNTYPEIII.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 8.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 3.
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; 5.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
DR   PROSITE; PS50853; FN3; 8.
DR   PROSITE; PS50835; IG_LIKE; 3.
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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Receptor {ECO:0000313|RefSeq:XP_025053308.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1903
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018248961"
FT   TRANSMEM        1258..1281
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          31..122
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          134..223
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          235..317
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          324..414
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          419..515
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          517..606
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          611..708
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          713..812
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          813..906
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          911..1006
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1011..1097
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1348..1603
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1523..1594
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1635..1894
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1812..1885
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          400..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1289..1309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..421
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1903 AA;  213603 MW;  B2084960667004B7 CRC64;
     MLVPSCRMMH VARPVVVLLC FLLYADAETP PKFTRTPVDQ TGVSGGVASF ICQATGDPRP
     KIVWNKKGKK VSNQRFEVVI EFDDGSGSVL RIQPLRTPRD EAIYECVASN SVGEISVSTR
     LTVLREDQIP RGFPTIDMGP QLKVVERTRT ATMLCAASGN PDPEITWFKD FLPVDTSNNN
     GRIKQLRSGA LQIELSEESD QGKYECVATN SAGTRYSAPA NLYVRELREV RRVPPRFSIP
     PTNHEIMPGG SVNITCVAVG SPMPYVKWML GAEDLTPEDD MPIGRNVLEL NDVRQSANYT
     CVAMSTLGVI EAIAQITVKA LPKPPGTPVV TESTATSITL TWDSGNPEPV SYYIIQHKPK
     NSEEPYKEID GVATTRYSVA GLSPYSEYEF RVVAVNNIGR GPPSEPVSTR TSEQAPSSAP
     RNVQARMLSS TTILVQWEEP EEPNGQIQGY RVYYTMDPTQ HVNSWMKHNV ADSHITTIGN
     LVPQKTYSVK VLAFTSVGDG PLSSEIQVIT QTGVPGQPLN FKAEPESETS ILLSWTPPRS
     DTIANYELVY KDGEHAEEQR VSIEPTTSYR LQGLRPNSLY YFRLAARSPQ GLGASTAEIS
     ARTMQSKPSA PPQDISCMSP SSTSILVSWK PPPVEKQNGI ITEYSIKYIG IDGEDDKPHE
     ILGISSDTTH YLLEQLEKWT EYRISVTAYT DVGPGPESLA VLIRTDEDVP SGPPRKVEVE
     AVNSTAVKVS WRSPVPNKQH GQIRGYQVHF VRMENGEPKG QPMLKDVMLA DAQEMFISGL
     QPETTYSLTV TAYTTKGDGA RSKPKLVSTT GAVPGKPRLV ISHTQMNTAL IQWHPPVDTF
     GPLQGFRLKF GRKDMDTFTT LEFSEKEDHF TATDIHKGAS YVFRLSAKNK VGFGEEMVKE
     IYVPEEVPSG FPQNLHSESS TSTSVQLTWQ PPILAERNGV ITKYTLLYRD INVAHHPVEF
     PIAPADTTMT LSGLKPDTTY DVKVRAHTSK GPGPYSPSVQ FRTLPVDQAV FAKNFHVKAV
     MKTSVLLSWE IPENYNSAMP FKILYDDGKM VVEVDGRATQ KLIINLKPET SYSFVLTNRG
     NSAGGLQHRV TAKTAPDVLR TKPVFIGKTN LDGMITVELP EVPANENIKG YYIVIVPLKK
     SRGKFIKPWE SPDEMELDEL LKEIARKRRS IRFGREVELK PYIAAHFEVL PTEFTLGDKK
     QYGGFENKQL QSGQEYVFFV LAVMEHSEST MYATSPYSDP VVSMDLDPQP ITDEEEGLIW
     VVGPVLAVVF IICIVIAILL YKRKRAESDS RKSSIPNNKE IPSHHPTDPV ELRRLNFQTP
     GMASHPPIPI LELADHIERL KANDNLKFSQ EYESIDPGQQ FTWEHSNLEV NKPKNRYANV
     IAYDHSRVLL SAIEGIPGSD YINANYIDGY RKQNAYIATQ GSLPETFGDF WRMMWEQRGA
     TVVMMTKLEE RSRVKCDQYW PSRGTETYGL IQVTLLDTVE LATYCVRTFA LYKNGSSEKR
     EVRQFQFTAW PDHGVPEHPT PFLAFLRRVK TCNPPDAGPM VVHCSAGVGR TGCFIVIDAM
     LERIKHEKTV DIYGHVTLMR AQRNYMVQTE DQYIFIHDAL LEAVTCGNTE VPARNLYAYI
     QKLTQIETGE NVTGMELEFK RLASSKAHTS RFISANLPCN KFKNRLVNIM PYESTRVCLQ
     PIRGVEGSDY INASFIDGYR QQKAYIATQG PLAETTEDFW RMLWEHNSTI VVMLTKLREM
     GREKCHQYWP AERSARYQYF VVDPMAEYNM PQYILREFKV TDARDGQSRT VRQFQFTDWP
     EQGVPKSGEG FIDFIGQVHK TKEQFGQDGP ISVHCSAGVG RTGVFITLSI VLERMRYEGV
     VDIFQTVKML RTQRPAMVQT EDQYQFCYRA ALEYLGSFDH YAT
//
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