ID A0A1I8J2N2_9PLAT Unreviewed; 1802 AA.
AC A0A1I8J2N2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=PLAT domain-containing protein {ECO:0000313|WBParaSite:maker-uti_cns_0045612-snap-gene-0.15-mRNA-1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0045612-snap-gene-0.15-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0045612-snap-gene-0.15-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the polycystin family.
CC {ECO:0000256|ARBA:ARBA00007200}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
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DR WBParaSite; maker-uti_cns_0045612-snap-gene-0.15-mRNA-1; maker-uti_cns_0045612-snap-gene-0.15-mRNA-1; maker-uti_cns_0045612-snap-gene-0.15.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd01752; PLAT_polycystin; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR InterPro; IPR013122; PKD1_2_channel.
DR InterPro; IPR003915; PKD_2.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR042060; PLAT_polycystin1.
DR InterPro; IPR046791; Polycystin_dom.
DR PANTHER; PTHR10877:SF183; AT14535P-RELATED; 1.
DR PANTHER; PTHR10877; POLYCYSTIN FAMILY MEMBER; 1.
DR Pfam; PF08016; PKD_channel; 1.
DR Pfam; PF01477; PLAT; 1.
DR Pfam; PF20519; Polycystin_dom; 1.
DR PRINTS; PR01433; POLYCYSTIN2.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR PROSITE; PS50095; PLAT; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 750..769
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 957..978
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 998..1020
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1229..1248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1488..1507
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1527..1549
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1569..1596
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1616..1638
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1677..1699
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 794..911
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT REGION 220..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1055
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1098
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1340..1353
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-2"
SQ SEQUENCE 1802 AA; 201408 MW; DE946E711C5D795A CRC64;
CAADSPTCEV EAKLPAGQEA NNYTLTICVS VFDGAYSEAF HAQTRVRVTP RAMKSEEFQS
NSPFFTDIIG AGKSGSVVSM AQIALPLLSA INQVSKDASG AANDTDPVAA EKRRKERSAA
KALVVDAARN AIESFNPNAS ETEQLQTLQL SGEMLKGANS VPNEISESSK ENTVAAGDLI
SKRLVDLSSS EDVTYDQIKE TSSLVLASSL NMLDEIVRSQ QSTMSNNSDS NSGGGGGGVD
TSTLSSEERL RRSDVSLRAL ENFRTTGLAL GNKQVAGETP TTIDLGNIKM NVEKQSTNSI
VGKKFGKGSG KDSGCSIGTG QSANGSIFVE PSQYDPNELK PSQAVVAQVI ENGANIFTMA
GNGSRMSSPV LSVGIYNDRQ YQFPVKDLND DSLVEVWVSN HPDAVAAIKP EVNATRPKSE
RMLITKVSVK QFDGLFAQVK HYTAEPIQSE NDNSMNESTT FRTETTTEAA TTLESTTTNG
PANDEMIEYL VFISAGKAPT EQNYDHFCQL PLLETRTCSR STARQAATEY TVGSLDGSGP
DAATAAKSAA PTTVATDYQV ESCNCSGTDG SGPCSKLGAS ATSTDVTGAW LLTKCVCNST
GCARTSGEDS SVPESVYEAD RWTCFFSPVN LGTNDTTKEF FIGIRAVRTL ASNRTDRNPN
RLPSLDLKVP ETDYVVTNYS ATTFTSGCFY VDMKTFKLSS DGVYLSQCST INSTLCYSSH
LTSFMSSFVV PPIQIDPNDS AWLKLDSNPI ALALVLSIVC FYFIILIWVR RKDEKDFERV
GITPLMDNHP ADVFRYELTF WTGARRQAGT TANVSFILYG EDDESAPRLV QDPKRPVLTR
NSVDSFLMTT PYYLGKLTHL RMWHDNSGSS PKWYLNRLLI QDLQTKEKYF FICNRWFAFD
EDDGMVDRIL TVSGREEVRK FDVVFWSKAQ KNLNDGHIWL SVVTRPPRSK FTRVQRATAC
LVLLLSTMMV NLMFYGQTAK VESPQLIEFG PVKFTAHSIY LATVSTLIIL PVNVLVVVLF
KNRRSKPPPG VKKMDAQPRQ PDDDQDDRDD EKPGSANPRS AVTPRAVRLS DVTEPAPADS
RLDMRQKSSN AGGTASNQNN DDDEDDEEKD KKPSFGGVLG EEKTAEWLAA MFVTLFQSII
LVQPVKILVL AIVYALLVKK IEEDEDEVTR DLVMAGAAKM HQRMTMRDLS DPAKMKAFLR
SRRVPPPPDL ETLRALREQR IKEQAMNDIL GDIMFYIIFL IILTMAAYTN QDYRSFIQNH
LVKGTITGVD ADGPNLDSVQ RIEDLFTYVG EFAAPRLYSN VCYNGEVCDM AGPGWSWDPH
LFLVRKPQLR QLRIKRPGTC KIEKYFKDSI YECRPEYSML NDDEASYLPM WQPFNSSYPE
QTEWSYTGAI KLFGIPYSGY LSTYAGGGYV ASLGKSAVEA KQMTEYLRNN SWIDKHTRAV
FFEFLIYNPN TNLFTFSEIL FEAFNGGGFV KYPQVYTLRL NRYVGANGAF FMAVDILSLI
FIVFFVYREC KELHKLGCLY FRDVFNVMDF LLLIFSCIEV VLFIIKITAQ QGVSYFMKKY
PERFINFQWL ILWAQMNQLF LGLVVFVFTI RFLRLLSFNR KMMMLGYVLK TAAKPLGYFL
VVFFIMFFAF VQLGYFMFNV KVESFKSLIN CIETLGVMTL NKFDFTTFVV GGGQLGMVFF
FVYMVFVSFV LINFFITIIN VSFSQVKQSW GETRNNYDIV DYVVKSIKSV FGINPQKRLN
HIDHQFAYMA ETSKFEQQVE ELDDKLFELE FYIRNMGILN GQELQESATA KKRVKGKVFL
SE
//
