ID A0A1S3KUG3_SALSA Unreviewed; 2003 AA.
AC A0A1S3KUG3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Polycystic kidney disease protein 1-like 2 {ECO:0000313|RefSeq:XP_013982341.1};
GN Name=LOC106562168 {ECO:0000313|RefSeq:XP_013982341.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013982341.1};
RN [1] {ECO:0000313|RefSeq:XP_013982341.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013982341.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_013982341.1; XM_014126866.1.
DR STRING; 8030.ENSSSAP00000091805; -.
DR PaxDb; 8030-ENSSSAP00000091805; -.
DR KEGG; sasa:106562168; -.
DR OrthoDB; 52189at2759; -.
DR Proteomes; UP000087266; Chromosome ssa11.
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; 2.60.220.50; -; 1.
DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR000203; GPS.
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; PF01825; GPS; 1.
DR Pfam; PF08016; PKD_channel; 1.
DR Pfam; PF01477; PLAT; 1.
DR Pfam; PF20519; Polycystin_dom; 1.
DR PRINTS; PR01433; POLYCYSTIN2.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR PROSITE; PS50221; GPS; 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 Reference proteome {ECO:0000313|Proteomes:UP000087266};
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 863..883
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1071..1091
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1111..1133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1354..1376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1388..1421
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1480..1502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1728..1746
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1766..1783
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1815..1835
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1855..1875
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1916..1942
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 908..1025
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT REGION 1138..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1323..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1976..2003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1984..2003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1576..1589
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-2"
SQ SEQUENCE 2003 AA; 223781 MW; 7DAC0DAC2AF1DC80 CRC64;
MNDPDPGAGC GHMLRGSGFQ WEATSNCSQE LLFICQFGLY LMRVCVCEAE SKECSWIELW
ITQQPIFSRP QFQKNIILQK PIGEFGVIKC YSMNQSTDGA NCKVLYGSPL QIQVEVESGT
NVTYKLHRCE MLVANSSAVR GIIPHNITVG PEVEKQLGSG CHQLTLHASN GVSVLGVSTE
LQVCLLEPVE GLLGSVMAEE GECPDSDLYV SVSLDRGAPV QLLFQVSGAN DSISETRDME
NTSMQVYNIS TTIQGFLQVK VRAWNVFSHM DVDVGNTTVV CHNSSDLRQN GYANTTEKHM
RVRRANNLRI TAIPETASQD TESVKLEVTG LGGLSNGKQS KFEWECSNHL RCSSVNKVTL
LFLPVGEITS NYMLSLEVTV TELNTKTCGS TTITTEVRPA KSGTPVQELQ SAVADIVANL
GQQGMLSGET LGQMFKSVSD ILNKGSSEEK NNRMKLREQM LMNISEALEN SSSSTLQKVQ
LTARAVAGLT KRGDELSPNA QAYWSKCAQN KDLISDGLFF QLEASFLVAN LSSSLLSMNV
SEHVGEEELV QAAIPIVEAA SNILDVSSNR EVSDLLLKGM DSVQSALLNG KKVDEASVIV
NSPHITVFVN RYEPVDVRML SLKKNPFSWS EENNITGTVG SVSLTRGNGS VIPIENLSEE
IEVRVLQTPS YSMSFESIFL PRPEGGQANS TILYLGNYST LMVDVPSPDV TLVLKIKPLK
DITFQLFLGY KDYPNDKQYI AKTQMPHQSN TQEEKYTWVL GPNDLIGKVG LHYLVVRPIV
KAGVKSVNAT VTVTSIAAQC KYWNETLSTW SEDGCRVGPL TTLLATQCLC THLTFFGNSF
FVMPNLVDVS RTAELFGTFA QNPVVVCFIG SIFVAYVLVV IWARRKDIQD IAKVKVTLLD
DNDPLAEYRY MLNISTGHRR GASTSSQVTV TLLGMEGESE PHHLTDPDKP VFERGAVDMF
LLTTPFSLGE LQSIRLWHDN SGRHPAWYIN KVTVQDVETG QKWHFLCNSW LAIDMSECTL
DKVFPVATEM DLKKFSNMFF MRTAKDFRDG HIWFSVISRP PTSTFTCVQR VSCCFSLLLC
TMLTSIMFWG IPTDPSEQTM DLGHIEFTWQ QLMIGVQSSI IMFPINLLIV SIFRNTRPRE
TKPGKPKAEV SKQGKTGRVS RSQPSSPQRD RELTPDTVIK DIKKIAQSLS KAMKSPIPRL
ELEMKPGQQT DINTLLSLVE DIIQQQNRAG GEFYTDASKK EGSLILSLGV TNLQETSMCG
SPEKTGDGSQ KRSTNSQYLY RQLCHVEKEL SLLGPSRFPN PDSYCRAVQQ VQGMKGLLES
SSLGGDELAQ SPGQAESSDG DSGSKKCCQD GLPWWFVFIG WILVAATSGV SGYFTMMYGL
TYGKDRSINW LISMVVSFFQ SLLIIQPLKV LAFAAFFALV LKKVDQDEYG DPKIEGALRN
PDDPDVVWAV RRDSTCSFYQ PPPPTDIERM RNNMIKEHKV FALIKEILTY MGFMWMLLLV
AYGQRDPNAY FLTQHIRQSF SQGISDSMSH GNVFTWANTS LLSNLFGEYP GFITDGNSKL
VGNARLRQVR VQKNSCRIAR SMRQAVPDCH APYSWEVEDT GSYGPGWNRS VSENTSRTLR
SPWQYQTQAR LRAQPIWGSV VLYRGGGFVV DLGPDSQNAS STLQYLFDNT WLDLFTQAVF
VEFTVYNANV NLFCIVTLML ETTAVGAFQF RSELQSVRLY QSTGGLHIFV MASEVIYFLF
IFYYMYVQGK LMKQQKWAYF KTKWNLLELA IILLSWSALS VFIKRTLLGN RDMEYYHNHK
DQFASFHETA TADAVLGYLI AFLVLLATVK LWHLLRFNPK LNMITATLQR AWTDISGFLV
VITIMFLAYS IISNLMYGWK LYSYRTLLDS AMTMVSLQLG IFNYDEVLDY NPVLGAFLIG
SCVIFMTFVV LNLFISVILV AFTQEQIHHK PSEEEEIVDL MLMKLCSLFG IKYKKEDKEE
SNSPKVNANN ASITKKEPST ISS
//
