ID A0A2B4SM85_STYPI Unreviewed; 2801 AA.
AC A0A2B4SM85;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 08-OCT-2025, entry version 34.
DE RecName: Full=Telomere length regulation protein TEL2 homolog {ECO:0000256|ARBA:ARBA00018231};
GN Name=SBF1 {ECO:0000313|EMBL:PFX31011.1};
GN ORFNames=AWC38_SpisGene4215 {ECO:0000313|EMBL:PFX31011.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX31011.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the TEL2 family.
CC {ECO:0000256|ARBA:ARBA00006133}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFX31011.1}.
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DR EMBL; LSMT01000042; PFX31011.1; -; Genomic_DNA.
DR STRING; 50429.A0A2B4SM85; -.
DR OrthoDB; 5951637at2759; -.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:TreeGrafter.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042162; F:telomeric DNA binding; IEA:TreeGrafter.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; IEA:TreeGrafter.
DR CDD; cd20828; C1_MTMR-like; 1.
DR CDD; cd13208; PH-GRAM_MTMR5_MTMR13; 1.
DR CDD; cd14534; PTP-MTMR5-like; 1.
DR FunFam; 3.40.50.11500:FF:000006; SET binding factor 2; 1.
DR FunFam; 1.25.40.720:FF:000001; Telomere length regulation protein TEL2; 1.
DR FunFam; 1.25.40.720:FF:000003; Telomere length regulation protein TEL2 homolog; 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 Gene3D; 1.25.40.720; Telomere length regulation protein 2, C-terminal domain; 2.
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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR002219; PKC_DAG/PE.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR022096; SBF1/SBF2.
DR InterPro; IPR038528; TEL2_C_sf.
DR InterPro; IPR051970; TEL2_Regulation.
DR InterPro; IPR057348; TELO2_ARM.
DR InterPro; IPR019337; Telomere_length_regulation_dom.
DR InterPro; IPR037516; Tripartite_DENN.
DR InterPro; IPR005113; uDENN_dom.
DR PANTHER; PTHR15830; TELOMERE LENGTH REGULATION PROTEIN TEL2 FAMILY MEMBER; 1.
DR PANTHER; PTHR15830:SF10; TELOMERE LENGTH REGULATION PROTEIN TEL2 HOMOLOG; 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; PF25320; TELO2_ARM; 1.
DR Pfam; PF10193; Telomere_reg-2; 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; 1.
DR PROSITE; PS50211; DENN; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 853..1300
FT /note="UDENN"
FT /evidence="ECO:0000259|PROSITE:PS50211"
FT DOMAIN 2039..2483
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 2616..2666
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 2696..2801
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1558..1618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1986..2011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1558..1572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1594..1611
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2801 AA; 315492 MW; A4A179704370F867 CRC64;
MEQHLDRDLA SEVRRFVRER QNKLANASNS GEVIETLNDV VELFLRGTLL PFQVSLDKRP
VLKGEFVSNH FVRFSEFILS SKVIEFYSNL NEQQRKDGFE VFFLRGPSHD CLLVLGDVLS
KPATNLKNAK VIVSLLEKFF GEERLVDILV EQCRLSRPSK NGSLNSSVTG FESKLWGQLV
TLIVSLPQRV ANKLRFKCSP QFYPESYFNL VSCEIIKALE KLHDNLTMSQ DCSFKFLEEL
IGRICLVGQA ERMFAILLPA LEKWLKKSPL WNRICARLVT GIPDGCMEHV TEGLLKMADD
PSLISKLFGD SVLTNTKLKY LLTSKFLLMR SYTNMNVLYN IMGYLSGYKH RHLLVETLHT
LFDIWGDRSA IKHTTYDQHF YITCATVLSF GHLNIEERKS EKHVLLNKLL VGVQSHLESP
LEKVQRLGMV VAECLTCSLE PNGEKLVFGY MEDSDTKQLK SLAKGPQERM NLRSVGKRNE
PDVEIKGKDK LVTEESSSMK VSAEKNSPQI CEGDDDLVPY DLGEEDDSDL KSKAPKYLRD
CIEGLLASED SSKMEASLKN VEKLVGAEMD DLDDVCEELV KVLLHLQDQF STDMFGELRH
SAIVAVLIRC PEQIACYLTE EFFAPNYHLQ QRMDILSVLA DAAQQLSTPV EITKTKEVPR
RFPLPQAESN KCLQAIPEWQ KIVQERIDGK TKRFTKGPSH PQPKPVANKF ASVAGYFFFP
LMKNFDSKVN TLDLLGEDTL VLGRLVYTLG IIMYSARETP TARNMGKALL EFTWALKYHS
ESFVRQALIF AQAMVAVSVP SSILMNDAPG ELSELHDWLK TIVQNDTDAD SERVDGYGRL
HDIPSQEMSR LADYFVVAGI DRDSKNGEVK GKVIQRFPSK DRKDATFPEG LELFCQPGGW
YYSNYYKPPT FFVAVLTDME GDHRYCACFT FYEKCSPAKS KSKAVKSFNK EVLKDGSQSD
SSLSDKRFSD GVPGISINSE ELSMTEMYAP KCLCLVSRAS YFDILKSCLT TIYWSYLSGS
SKSLEGLVGC VLGFVQVPPP GGPKMTFSMG AGDRQTLSPP ASETLPVTGK SLSILFNQLG
IHNMLSLFCA ALTENKILFY SSSYAQLTNA TQAMLALMYP LKFGYVFIPI LPSALLEFLS
APTPFIMGVH ESYKDNLGSD LTDVILVDID GGHVSIPDSI NLPYLAEPFL SRARHELTMV
LYPQLVTADC AFQPPTSPSL PLLQDKELRA VFIRLFAQMF SGYRSCLTLI RIHPKPVITF
NKVSFLENRG LVGDAFLSKV LESISFLSFV ASRGPPYRPC DLFDQLCVEI DGILNSEGGL
DPEVQANIQQ LAQKLYDNEP SCESAENNVQ PVIPVEEIER CSQKVFPQLS EDAISRHINQ
QENLSLDYTV KSMEPCVVPA NPMSSRQQHY IPSRKLEVLK DCVAYIFDNK ISEARKSLPS
VVRGLKSKGA QLALCHELSL RARQNRSLLE HDQFDLVVKL MNSALQDDAS MSNTSVAAAL
LPLTSTFCRK LNAGVIQFAY TCVQEHPVWE RQQFWEEAFY TDVESQIKQL YVDEEAPKAN
AEDTLERKEQ RTSRSSLTPL AKHRSFTKSR DNLSSTPKDS GSSSDLDQSS QVEQKPVPSA
LSIAAKQLKK WPYYSKGEQD ALINSEEGIV YSQAIHYANR MVYMRIPLDA SEKMPPLTPA
TGMQVDEEGS VGGTHTGSIA NGVAGGSSEV GSCITDSWGR ESYMDDEDGG TVADKVTRFV
SRFVDRVGTE AGISQEHLKS LYTMIPGVVT MHIESLEPVY REYKNLAPIQ KAKIMRPTLL
LGEEMMSDGL RAYLIPDGRE LGRGGEDQGG ACLLPAEGAV FLTNYRVIFK GTPVDPFASE
MIVTRSFPVG SLIKEKKIGV QYLKHLGQWL HECIQLRSST FQMMKLIFDD EVEQEAIETF
RKKLQRRRSP NTVIGTFAFC GKGVPRTPTF VIEKHMGRQG TILKTKTKLV SASRTKASSI
VNIRSSLRKK RRQRNASDPQ SLDHRSLSGS LTTDDDDSVL DINDISLKGE PIVVQGAERL
SKLSYCGDYS RLKLGNIAKE SSEGPWRICM VNVTYTACRS YPSVVIVPQS ISDDSIVRIA
KNYRQGRFPV AVWRHQRNKA TLLRAGSIER STIGSIMRQT KTVAPGSVAS HTISSSASAE
QEKYFAAVVA ATPQSKNKNI SRATSLHHGV LLKDGYFADE VDSGQLVDRT IMRKGWEPAA
LYVFGDKTLL RHVKQEAYPK CDFVPIELPD IRAVRASFKK FQRATCPSTE TNSSFIQQVE
ESEWLQQLSA IMTVANCFVD LIDIQGSSVL VCFEDGWDAT PQVLSLAELM LDPYYRTIDG
FKLLIEKEWL SFGHKFTHRG NQIASTQGGF TPVFLQFLDC VHQIMLQFPL SFEFNDHFLC
TIAYHHASMR FRTFLLDSEH ERVESGWMAE EDHKPRGKSL WDYMDLQKTK SPLYNNFLYS
PNQTKVLRPF CKVPNLKVWK YYTTENLSTG PTYDFEMIND VTTTVENEGS PDGKQETYGS
CMTGCYGDVT QFALDECSWL LQELYRLEEE ADQKPKKWEQ HWHKLSYPTA KKMVFSYNTR
WFNHQRLNLH KRSTMEVILK GKLQVEERGA QGFSQPHNFE PHLFVPPSNC EHCLQLIIGI
LNKGVKCTEC GYNCHEKCQP QVPWQCKKRD LPEQPGSGMT KSTMSLPSEA DAAHPKKLHC
GYLLKRGHLL RQWKSRWFVL DTQRNELRYY DEEHDDHLQG AVDLGDMIAV QSLSNIPQGG
PKGSIKGAFF DLRTTKRVYN LMCNSSEEAK VWVEKLQSMN V
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