ID A0A3B4AQ41_9GOBI Unreviewed; 1916 AA.
AC A0A3B4AQ41;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Polycystic kidney disease 1 like 1 {ECO:0008006|Google:ProtNLM};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000018815.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000018815.1}
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 STRING; 409849.ENSPMGP00000018815; -.
DR Ensembl; ENSPMGT00000020061.1; ENSPMGP00000018815.1; ENSPMGG00000015319.1.
DR Proteomes; UP000261520; Unplaced.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd00146; PKD; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR002859; PKD/REJ-like.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR046791; Polycystin_dom.
DR InterPro; IPR014010; REJ_dom.
DR PANTHER; PTHR46730:SF4; POLYCYSTIC KIDNEY DISEASE PROTEIN 1-LIKE 1; 1.
DR PANTHER; PTHR46730; POLYCYSTIN-1; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF00801; PKD; 2.
DR Pfam; PF01477; PLAT; 1.
DR Pfam; PF20519; Polycystin_dom; 1.
DR Pfam; PF02010; REJ; 2.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00089; PKD; 2.
DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR SUPFAM; SSF49299; PKD domain; 2.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50093; PKD; 2.
DR PROSITE; PS50095; PLAT; 1.
DR PROSITE; PS51111; REJ; 1.
PE 3: Inferred from homology;
KW Cell projection {ECO:0000256|ARBA:ARBA00023069};
KW Cilium {ECO:0000256|ARBA:ARBA00023069};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1110..1130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1320..1339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1351..1375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1463..1484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1490..1510
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1577..1596
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1850..1867
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1888..1908
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 48..112
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 156..210
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 215..377
FT /note="REJ"
FT /evidence="ECO:0000259|PROSITE:PS51111"
FT DOMAIN 1154..1276
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
SQ SEQUENCE 1916 AA; 218460 MW; CF48BC202AD3E44D CRC64;
VTVEFLGMTP KGQSSLHVNI LDQGSFNVSS NWSLELQLFI ILKCAYFPVV EVYAAKQAYP
TNTDVHLSAL TDAQGAMEFL WRFGDSTSAR NILKAITKRY RKPGRYNVTV VMVTPRMSIT
SEPFPVIIQR AVKLNRLIHQ ASVLQNQTVV FSCRVNTGTD LYFLWTFGDG SSKHGHSTEQ
HVFQSLGEFM VEVTVFNLVS SASLRSLIFV VDKPCQPPPV KNMGPLTVKV PRYEPVRLGV
TYEAEFNCDV FVSGGVHYTW KLYNSMGQAI FLPHIETHRQ TLVLPSHFLH YDTYTAIAKV
QVVGSVVYSN YSVKVQVTSS APVAFIQGGT NVFINNKNTT VVTLDGTKSH DPDFPHNVTR
FSWVCKPVSS IPSSCFDCEF PMSSAVISFL SSFLKPNFDQ FQFTLTIENK KIYVYFYCQN
NKVNWDESFS VQAFCEQCKL PSDFILYSWR LYQVNASSRP ISEVPFCHTL DLSAPSAIKD
TPTETSPSQR KWRKELDLFD SSPISPEHSG HQEIKALTET SSDWDFPFAI SEDADLQNGI
VEDGEDFSLG EDLDFDPGSH REEGSNLVDV RPHVAVQERT LLDLPRDPVP QWIFESYTYT
GISSPELNFK PFSLQPGSRY MLDVIATHNS QKPFLGRTQF FFQTRQAPKG MTCQVQPTTG
VELLTVFSDL TYKYSYSVGN EPPQTLYQGT DFEHYFSLPL GDLHNDYKVT VSIEIRSSID
GGTTPCPVSV TVQPQFTRDT YSSSDPVLEL SHIAMKNLSS RLGNSFEILN EIRIVTNILN
RLSVEPGVNM ASLVFLRNAL VCIICDIEVI DQVLFHYKNL RQSATLLCYI TMTAGFVSVY
STYPIQKTTV SSGFRVFYLP QSFLRHRDTC VIGVVTELNQ NPYFWANYPG ELIGPVVELS
LFRCNAKRKI PIQFFAEPFE IEVQTPEKQT PTPEHILQHN KINYHGFNIS HEHLQYVFQL
HVQFTPPATR VFPVVLLFRM FAKPTPSEYH LRKIHHWGRS VIHMTLPSSF LSAGGVGYLT
LLNADFERPQ RWTNTKVSYR VRVDRSQCVS WDAQRGAWST HNCKTQAKDK PSAVNCRCRQ
LYPVTVVQEQ IPTNLDAGEL GAFFSVSYNW TVLIVLVLGV ALFIGALVLS PNADVASGER
RAHYLSDNLQ CEPHLYAVTI YTGLCSAPEM SAKVCIVLCG EDGFTQTKEL QVPGCTLFRR
NSQDTFIVGA AESLGSLCGI HIWHDNSGPT PTWYLKRVEV FEVNRDHQVK GRMWLFVSEC
WLAVDRSDGR VERMLRVYDQ KTRFGKMLRL KVWDYMTDFH IWISVYSCPN LKPFTQGQRL
SVCALLWLGY ACVSTVIISQ RNDKVSTLLT LRVSILATLC VALVLPVVTL LSFMFRLSQL
KIMRPATKSP DIDLFPVSSW GLDNTVLNEI QNNVTEDVVV IDGAAENKDS SLFRHEKKKE
DGTYKARESC QDDPKMPQWF NNVAWVLCLL FCVTCLASSA ILGVREAVLW IQSLLFSLLF
CIFFFHPLLV NSIQNWALRQ TGRPTLLKVN KMYLNLYNLL EVRQRQRFLR LVRPPVFTEL
RKSRWNRKRD RVIKYNLWFL LFRDWIVFGS MFSLMLCITY ESSSSDYYNL NKTVKKHFIS
DSFKSVQTYD EWWRWAQTSL LNALYRNTSS TLAAFQNSHI LIGEPVLWKT EKYYCFTTNI
THSFSSYSII FCRTIAELKL KQLNSEHWIG KSTVALKVHF ALYSPAPNLF TSVTLTIKQS
PFGILLPSAS VQSVRVCDST SQWDYVVMTC KVSVVLNTLP VKEKNILNEM VNNTVSLLQV
GVFVVAIVYH FYCIYRSAVV GEVEEWLQRQ NSKTHIDFSQ LATWDQSNTW KGPILLCFLI
YVIMLFLHQK HTRSCVLFHS HMFNTNPXXX XXXXXXXXXX LYISHLVMSY GGTLYF
//
