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Database: UniProt
Entry: A0A1J1HM94_9DIPT
LinkDB: A0A1J1HM94_9DIPT
Original site: A0A1J1HM94_9DIPT 
ID   A0A1J1HM94_9DIPT        Unreviewed;      1503 AA.
AC   A0A1J1HM94;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=phosphoinositide 5-phosphatase {ECO:0000256|ARBA:ARBA00013044};
DE            EC=3.1.3.36 {ECO:0000256|ARBA:ARBA00013044};
GN   Name=putative Synaptojanin-1 {ECO:0000313|EMBL:CRK88524.1};
GN   ORFNames=CLUMA_CG002220 {ECO:0000313|EMBL:CRK88524.1};
OS   Clunio marinus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC   Clunio.
OX   NCBI_TaxID=568069 {ECO:0000313|EMBL:CRK88524.1, ECO:0000313|Proteomes:UP000183832};
RN   [1] {ECO:0000313|EMBL:CRK88524.1, ECO:0000313|Proteomes:UP000183832}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the SLC29A/ENT transporter (TC 2.A.57) family.
CC       {ECO:0000256|ARBA:ARBA00007965}.
CC   -!- SIMILARITY: Belongs to the synaptojanin family.
CC       {ECO:0000256|ARBA:ARBA00008943}.
CC   -!- SIMILARITY: In the central section; belongs to the inositol 1,4,5-
CC       trisphosphate 5-phosphatase family. {ECO:0000256|ARBA:ARBA00009678}.
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DR   EMBL; CVRI01000008; CRK88524.1; -; Genomic_DNA.
DR   STRING; 568069.A0A1J1HM94; -.
DR   OrthoDB; 21647at2759; -.
DR   Proteomes; UP000183832; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005337; F:nucleoside transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR   CDD; cd06174; MFS; 1.
DR   Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR002259; Eqnu_transpt.
DR   InterPro; IPR046985; IP5.
DR   InterPro; IPR000300; IPPc.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR002013; SAC_dom.
DR   InterPro; IPR015047; SYNJ1/2_RRM.
DR   PANTHER; PTHR11200; INOSITOL 5-PHOSPHATASE; 1.
DR   PANTHER; PTHR11200:SF257; PHOSPHOINOSITIDE 5-PHOSPHATASE; 1.
DR   Pfam; PF08952; DUF1866; 1.
DR   Pfam; PF01733; Nucleoside_tran; 1.
DR   Pfam; PF02383; Syja_N; 1.
DR   PRINTS; PR01130; DERENTRNSPRT.
DR   SMART; SM01165; DUF1866; 1.
DR   SMART; SM00128; IPPc; 1.
DR   SUPFAM; SSF56219; DNase I-like; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS50275; SAC; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183832};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        1090..1110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1137..1157
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1169..1188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1194..1213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1234..1257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1263..1283
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1329..1346
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1366..1390
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1397..1414
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1434..1457
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1469..1493
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          120..453
FT                   /note="SAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50275"
FT   REGION          908..940
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          953..995
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1013..1054
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        980..995
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1013..1030
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1031..1050
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1503 AA;  169329 MW;  2D3422393A70F1C2 CRC64;
     MAMGKNYRIL EKNKPEQPHS IILEHRSRPE TLLFESQAVA NLSAQETEAV RKQYVKILDA
     YGCLGVLQLN AGETTILYLV LVTGCFSVGK IADSEIFRIT QTQFVSLQHQ QPNEDKISEV
     RKVLNSGTFY FSWNSSSEKP STSAQNFDIT LSAQRRRKTN ETDNRFFWNR MLHIHLLRFA
     VECEFWLLKA MCGSIEIRTV YAGSRQARAV IISRLSCERA GTRFNVRGCN DEGYVANFVE
     TEQAIYLDNE VTSYLQTRGS VPLFWEQPGV QVGSHKVKLS RGFEATAPAF DRHMTMMKSR
     YGRQAICNLL GTSLIGSKEG EAMLSNEFQK HHEMSVHKDV PHIVFDYHQE CRGNQTNLSK
     LKDRLEKCCG SFGLFFASSD DVNQEQYGTI RTNCLDCLDR TNCVQTFIGL EVLNEQIKII
     GLADKKQTLS RFEEVFRQMW ISNGNEVSKI YAGTGAIGSI GAGAGSKIID GARSAARTIQ
     NNLLDSSKQE AIDILLVGST LSSELADRAR ILLPTNMLHA PTPVLREMCR RYNEYVSPAE
     LRVAIGTYNV NGGKHFRSVI YKDLSLIDWL APKNDAIIDI EHSDSVYDKM ADIYAIGFQE
     IVDLNAGNIV AASSDNAKAW AEELQRVLSK DDEPYALLTS QQLVGVCLYV FVRPQLAKSI
     RDVATDSVKT GLGGATGNKG AAAIRFVLNG TSFCFVAAHF AAGQSQVIER NADYAEITRK
     IAFPMGRTLK GHDYVFWCGD FNYRIDMDKD EMKEILKTGD LKPVLENDQL RKQQEAGSVF
     NDFLEGEINF PPTYKYDLFS EDYDTSEKAR APAWTDRVLW RRRIRQLDAD DPNFNPGKLL
     FYDGQAALAA VKRKKNLQVC GINLSINLKT EDWVKQVERE IELCTTNCVQ LCEYIDVSSN
     SDYNSLGIPL AGGEQTKKKP PARPPALPKS PQVTPKHHPR HTAGVINVNN IIRPQQSQPQ
     PQLPERPCLP PRPKAMEQKS DQISPPSEQT TMEAETYQAP SAIYEEIQDD IKGRGNRKMA
     SSRREEQSLL GHSRSNGTSI VSSRNDSTEP VRLTPAWEAQ NLPNDDLNFK GMTMERARLE
     CEPPSDKFKL IFLILVLHGI GTLTPWNMFI TAKDYFVNYK LSANYTGQNN TVYIDNFLPY
     IGFASQIPNV LFNWLNIFVN LGGDLTKRVV WSLVVEIIVF LITVILAMVD SSDWPGTFFW
     VTIVSVVILN IAGGIFQNTA YGMAAKLPPK YTGAVVLGSN ISGPFASVIS ILSGSIWPSV
     RKAAIYYFIT AMFVILLCFD TYFAMPLNKF YRYHELMSEK KQEKARRAGI NIKAHPPYYK
     IFRQSFMQLF NVFFIFFVTL TVFPTVHSDI KQLGEGKFLG IVPRELFTSI TCFFTFNFFA
     MLGSLATSWV KWPSPRFLII PVLARVVFIP LFLFCNYHPL SMERVLPVYI TNDYVYWTIA
     IIMSFSSGYL SSLAMMYAPQ SQTNPQYQIT AGMMAAAMLI TGIFTGILFS YIFPSFVKVA
     VNF
//
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