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Database: UniProt
Entry: A0A3Q4GX60_NEOBR
LinkDB: A0A3Q4GX60_NEOBR
Original site: A0A3Q4GX60_NEOBR 
ID   A0A3Q4GX60_NEOBR        Unreviewed;      1326 AA.
AC   A0A3Q4GX60;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Polycystic kidney disease 1 like 2a {ECO:0000313|Ensembl:ENSNBRP00000014600.1};
OS   Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX   NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000014600.1, ECO:0000313|Proteomes:UP000261580};
RN   [1] {ECO:0000313|Ensembl:ENSNBRP00000014600.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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   Ensembl; ENSNBRT00000014994.1; ENSNBRP00000014600.1; ENSNBRG00000011182.1.
DR   GeneTree; ENSGT00940000164905; -.
DR   Proteomes; UP000261580; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   CDD; cd00037; CLECT; 1.
DR   CDD; cd22831; Gal_Rha_Lectin_PKD1L2; 1.
DR   CDD; cd01752; PLAT_polycystin; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 2.60.120.740; -; 1.
DR   Gene3D; 2.60.220.50; -; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR046338; GAIN_dom_sf.
DR   InterPro; IPR000203; GPS.
DR   InterPro; IPR000922; Lectin_gal-bd_dom.
DR   InterPro; IPR043159; Lectin_gal-bd_sf.
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:SF195; POLYCYSTIC KIDNEY DISEASE 1 LIKE 2A-RELATED; 1.
DR   PANTHER; PTHR10877; POLYCYSTIN FAMILY MEMBER; 1.
DR   Pfam; PF02140; Gal_Lectin; 1.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF08016; PKD_channel; 1.
DR   Pfam; PF01477; PLAT; 1.
DR   Pfam; PF20519; Polycystin_dom; 1.
DR   PRINTS; PR01433; POLYCYSTIN2.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00303; GPS; 1.
DR   SMART; SM00308; LH2; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS50221; GPS; 1.
DR   PROSITE; PS50095; PLAT; 1.
DR   PROSITE; PS50228; SUEL_LECTIN; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261580};
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        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        565..583
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        603..624
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        743..765
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        836..857
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1078..1098
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1118..1139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1166..1186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1206..1230
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1264..1293
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          10..130
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          132..217
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50228"
FT   DOMAIN          401..518
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   REGION          631..657
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        643..657
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        930..943
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603915-2"
SQ   SEQUENCE   1326 AA;  150875 MW;  F24C5178E49306BB CRC64;
     QSCPEYQEGF DGSCYEFVDL QRSFQDAEEW CERGGGHLAF ILNDETQQFL QKHLKPDRNW
     WLGVAPAAPN LTLDSAATEV LAWLDSSDVS YSNWVNLPDD QAACAHVLRH SGFQWEATEN
     CSQEFNFICQ FATLQCGSGQ VIEIDDSFYG RKTIHYCRSQ LTPSSTSSKE ECSWIDVTDY
     VTHCHGLQAC QAGVDLSAFG EPCPALGSYL SAEYRCKNIT GTVGSVSLTR VNGDVIPVEN
     LPEEIEEKFT WVLSPKDRTD DVGVHYLVIK PIVEPGIKSI NASVTVISIA AQCKYWNETG
     SFWSEDGCRV GPLTTPLVTQ CLCNHLTFFG SSFFVMPNLV DVSRTAELFA TFTNNPVVVC
     FVGAIFCAYL LVVVWARRKD MQDSVKVKIT VLEDNDPLAQ YRYLLSINTG HRHGASTSSQ
     VTITLLGTEG ESEPHHLTDL EKPVFERGGG DMFLLTTHFS LGELQSIRLW HDNSGDHPAR
     YVSKVMVQDL ETGQKWHFLC NSWLAVDMEE CTLDKVFPVA TEVDLKRFNL FFMKTAKDFR
     DGHIWFSVIS RPPCSTFTRV QRVSCCFSLL LCTMLTSIMF WGIPTDPSEQ TMDLHIEFTW
     QQVMIGVQSS IIMFPINLLI VSIFRNTRPR EKTTKADAKQ GKTVRVSPSQ TSSPQKEIKD
     ITPDTVMKLY RQLQLIEKEL GMLGPSQFPN PDSYNRAMQQ VQGMKGLLEY HLPMSILDGD
     SCFPGPEESL GGKKKCCQGG LPWWFVFIGW ILVIATSGVS GYFTMMYGLT YGKDRSISWL
     ISMVVSFFES LFITQPLKNP DAVQAARRDS TCSFYKPPPP TDIEKMRNNM IKEQKVFALI
     REIVYTGFMW MLLLVAYGQR DPNGYFLTQH IRKSFSKGVS DTMSIQDVFN WANTTLLSNL
     FGEYPFITDG NSRLVGNARL RQVRVQKNSC HIARSMQESI PDCHTPYSWE LEDMGSYGPG
     WTQPVGRNAS TNIHDPWKYK SQRKLRAYPI WGNVKLYRGG GFVMDLGPDF QNSSILQYLY
     ENTWFDVYTQ AIFVEFTVYN ANVNLFCIVT LMLETTATAF QFRSELQTVR LYQSTGGLHI
     FVMASEIIYF LFIIYYMFVQ GKLMKKQKWT YLKNKWNLLE LAIIILSWSA LCVFIKRTLL
     GNRDMNYYQN NKEFVSFHET AKADAVLGYL IAFLVLLATV KLWHLLRLNP KLHMITATLQ
     RAWTDISGFL VVMTIMFLAY SIASNLMYGW KLYSYRTLLD AVQTMVSLQL GIFNYEEVLN
     YNPVLGAFLI GSCIVFMTFV VLNLFISVIL VAFTQEQIHH KPSEEDEIVD LMLMKICSLF
     GIKCKK
//
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