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Database: UniProt
Entry: A0A2R2MIK7_LINUN
LinkDB: A0A2R2MIK7_LINUN
Original site: A0A2R2MIK7_LINUN 
ID   A0A2R2MIK7_LINUN        Unreviewed;      2093 AA.
AC   A0A2R2MIK7;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Myotubularin-related protein 13 isoform X1 {ECO:0000313|RefSeq:XP_023930024.1};
GN   Name=LOC106168468 {ECO:0000313|RefSeq:XP_023930024.1};
OS   Lingula unguis.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC   Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX   NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_023930024.1};
RN   [1] {ECO:0000313|RefSeq:XP_023930024.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_023930024.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
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DR   RefSeq; XP_013402966.1; XM_013547512.1.
DR   RefSeq; XP_023930024.1; XM_024074256.1.
DR   STRING; 7574.A0A2R2MIK7; -.
DR   EnsemblMetazoa; XM_024074256.1; XP_023930024.1; LOC106168468.
DR   KEGG; lak:106168468; -.
DR   InParanoid; A0A2R2MIK7; -.
DR   OrthoDB; 3195274at2759; -.
DR   Proteomes; UP000085678; Unplaced.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd20827; C1_Sbf-like; 1.
DR   CDD; cd13208; PH-GRAM_MTMR5_MTMR13; 1.
DR   CDD; cd01235; PH_Sbf1_hMTMR5; 1.
DR   CDD; cd14534; PTP-MTMR5-like; 1.
DR   Gene3D; 3.30.450.200; -; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 3.40.50.11500; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR001194; cDENN_dom.
DR   InterPro; IPR005112; dDENN_dom.
DR   InterPro; IPR043153; DENN_C.
DR   InterPro; IPR004182; GRAM.
DR   InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR   InterPro; IPR030564; Myotubularin_fam.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR022096; SBF1/SBF2.
DR   InterPro; IPR037516; Tripartite_DENN.
DR   InterPro; IPR005113; uDENN_dom.
DR   PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR   PANTHER; PTHR10807:SF109; SET DOMAIN BINDING FACTOR, ISOFORM A; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF02141; DENN; 1.
DR   Pfam; PF02893; GRAM; 1.
DR   Pfam; PF06602; Myotub-related; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF12335; SBF2; 1.
DR   Pfam; PF03456; uDENN; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00801; dDENN; 1.
DR   SMART; SM00799; DENN; 1.
DR   SMART; SM00568; GRAM; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00800; uDENN; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF50729; PH domain-like; 2.
DR   PROSITE; PS50211; DENN; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          6..425
FT                   /note="UDENN"
FT                   /evidence="ECO:0000259|PROSITE:PS50211"
FT   DOMAIN          1172..1756
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51339"
FT   DOMAIN          1890..1942
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          1989..2093
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          692..728
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1101..1151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        698..720
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1107..1140
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2093 AA;  235593 MW;  7318AC57635A9BC4 CRC64;
     MSRLADYFVV VGYDQEKERS GTSQGKIIQR FPEKDWPGSP FTLGIELFCQ PTGWSLSTQR
     HPPTFFVSVL TDIDADRHYC ACLTFHETVS MTSTKPDDED GDDGTPIRQS LMYAPKCLVL
     VSKFPEFETF RNCLGLIYTV YLENMQFQIE TLVGNILGCV QVPPPGGPQI RFSIGAGDRQ
     ALQPPVSSTI PTSGTSVAML FRQMGITNTI MLFCAAATDL KVLFHSQSYT RLTAASQALM
     ALMYPLKYSY VYIPLLPSHL LEVLNTPTPF IAGVHSSLKD EVSDLLDVII ADLDGGSVHV
     PECVTVPVLP NIVLSRTTEA LTMILNPELF TSDYAFPPNP AKLSSLTMQD KEIRAVFLRL
     FAELFTGYRS CLTLIRIHPE PFITFHKASF LGHRAMVSED FLTRVLDGMS YSTFVSERGP
     PFRVIDIFDE VYATLSDMIK HENGSQEKMM QSIKDLAQQL YINEHPNPQP YTQKIPKPPE
     GAYSRIHQPQ FPILDWIMVQ EIIDDGLAKS GIKSKLSQIR PPQPRIVPMG PHITTVAEKM
     QMLNNNARRL EVLRNCVSCI FENKISDARK VFPAVLRALK SKVSRLALCQ ELAYHVQSNR
     AMLEHQQFDL VVRLLNCALQ NESSMDENGV AAAMLPLVTS FCRKLCTGVI QFAYTCVQEH
     AVWANHQFWE ATFYQDVQRQ IRQLYAPQYE QEHSADKLSP PASPTTEGAE LSSSWGATGS
     WKGSPMDPRR RSITNMKYLK PKEVNALEIA AEQMAKCYDP QLRKWPNLSE SEKEEMINNE
     ESTVYSQAIH YANRMVYMRV PLDVTRGANL HFGADWESAS NSNITNSHVQ RKDHFYSSSI
     AESDSVDAES GFDEQEISEV GANVVKFVSR FVDKVCTESG VTADHIRSLH QMIPGVVAMH
     IETLEAVARE SKRLPPIQKP KILTPTLLPG EEIVMEGLRV YLLPDGREEA TGGSTGGPAL
     IPAEGAIFLT TYRIIFKGTP CDPLACEQIV VRYFPVSTLT KEKKLSSQYL SYVDQYLQEI
     IQMRANTFQL MKVGFDEEVS SEDVETFRKL TSKIRSPISV FSTFAFSGYQ FAQPAQLIKH
     KEKHASLKGF AKKTLMKTAR KAGLAKPKSA STSQRKQKYI LPTPPPSRRS TASLDSMDSD
     SRPASGVFDD ESLMDENEPV MSWTPDPKNL ERLGERAGYK DYQRLGLGSL NFNSAKSKTE
     PFRITTVNAT YSVCRSYPAM LVVPQTVSDD SIRKFARSHR QYRFPVVSWY HPKTKALLLR
     ASGFHSKGMM GMFKSHHNAP SGTSGEITST SVEQEKYFHA IVQCTPMGNL QHQQQSHNKS
     LSDSLTSIDS LMLSTDTLAL PDTPSLSRKN PIARAVNSLR SSGGKVKLTD NCMANNSRES
     ALAAGVAYSI STPTMSRRSP LLRRTIHGSL RANAGKGGKS LGRLGSVRDR RAVTSSGSLE
     VGMRLAMKSN GSIDHSAELE SQTQGLNKAA LYVLGEKAQV KNIKVDSFPK CEFVPVDFYE
     VRQVKTSFKK LLRACVPSAL LTDAEHSFYK LVQESEWLQQ LQSLMQLSGA VVDLIDLQGS
     SVMVCLEDGW DITTQVVSLA QVCLDPYYRT IKGFQALVEK EWLSFGHRFT HRSNQTAANQ
     ASGFAPVFLQ FLDAVHQVHR QFPLSFEYND FFLKFLAYHT VSNRFRTFML DNESERMEAG
     WLLEEKPKTS KIDGAATGED GFTLRQTMGT SVWDYIDKHH RRSPVFYNFS YVSMDGTNVL
     RPYSGIASLE LWDYYLTEDL SHGPPYDFET MYMDKKQNEE IEAIDGPLAP SSRRIVNGCY
     DTIWHLEPEC FSLAFQDIHK TQTKLDHLPM KWKAVWEKLD HPQSETLQRQ MSLKTRLTRS
     HGRTLHKRST LEILVRGKMA GDAIKSFGQP HRFEKFDFTT ASYCDHCGHL LWGLTQVKQG
     MRCADCGYNC HEKCVSSVPK NCAKLIRTPS EQPDSSVNLA EAQPHAPGDV TIQASRDMYR
     QFSARAQEHR THEGYLLKQG ALLKQWKQRW FVLDSMKHQL RWYDAMEDSH CKGYLDLSEV
     TSVGTSKNFQ GAPKRAEDNS FFEMKTVKRS YVFCAPNVQA SQEWIDKLNS CIQ
//
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