ID A0A2Y9IF23_NEOSC Unreviewed; 2441 AA.
AC A0A2Y9IF23;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=LOW QUALITY PROTEIN: polycystic kidney disease protein 1-like 2 {ECO:0000313|RefSeq:XP_021560994.1};
GN Name=PKD1L2 {ECO:0000313|RefSeq:XP_021560994.1};
OS Neomonachus schauinslandi (Hawaiian monk seal) (Monachus schauinslandi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Neomonachus.
OX NCBI_TaxID=29088 {ECO:0000313|Proteomes:UP000248481, ECO:0000313|RefSeq:XP_021560994.1};
RN [1] {ECO:0000313|RefSeq:XP_021560994.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_021560994.1};
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_021560994.1; XM_021705319.1.
DR STRING; 29088.A0A2Y9IF23; -.
DR KEGG; nsu:110593882; -.
DR InParanoid; A0A2Y9IF23; -.
DR OrthoDB; 52189at2759; -.
DR Proteomes; UP000248481; Chromosome 16.
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; IPR002859; PKD/REJ-like.
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 InterPro; IPR014010; REJ_dom.
DR PANTHER; PTHR10877:SF134; POLYCYSTIC KIDNEY DISEASE PROTEIN 1-LIKE 2; 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 Pfam; PF02010; REJ; 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; PS51111; REJ; 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:UP000248481};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..2441
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015873432"
FT TRANSMEM 1339..1358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1546..1567
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1587..1608
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1809..1835
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1847..1878
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1936..1959
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1979..1997
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2147..2169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2181..2201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2221..2242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2270..2290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2310..2332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2372..2397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..154
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 162..251
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 421..1116
FT /note="REJ"
FT /evidence="ECO:0000259|PROSITE:PS51111"
FT DOMAIN 1383..1500
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DISULFID 2032..2045
FT /evidence="ECO:0000256|PIRSR:PIRSR603915-2"
SQ SEQUENCE 2441 AA; 271228 MW; A4F1DF8C2D902771 CRC64;
MSTVGLVLLG LALRFRATIS NPEEGNFCSK SQVAFRDSCY EFVPLSHTFY GAQSWCEEQG
GHLVFIHDED TQQFLQKHIS QDREWWTGLT GNSAQNGTTE GPGSWLDTSN ASYSHWRRGQ
ASLAPNTCCY IGRDASFGWA ASDNCTQPFA FICEFGAGQS VACDGLNATM HCGSGEVIQI
QDAFYGRQTP HYCTQGAAGP SEEECSWASI KDKVAGQCQG LQVCQVAADG TYFGDLCPTQ
GSYLWVHYQC QEGLQLMVSN ESFIFENVTI SLTWLLSPFT GNLSCIISTG DGHTFNPYYP
PSSSSNVTHQ FRAPGEFTVF AECTTTEWHV MAQKHVTIRD KMERLHVTGC SSLSKSGASP
LCRAVFGDPL WIQVVLDGGT GVTYTALLGN ITLAEFTTPR GLLPYNLTLD RAAQQRMGPG
MHHLEIRATS NTTTSAPSRN ITVHFMEPLS GLQASWGSDH LELGEDLLVN ISVAHGIPEG
LTFEVAGLNA TFTHQEESLQ RPFGIYHVAV PLEGTFLVTV MVRNAFSNLS LEVGSITVTA
PSSLQEPSGT NAKEKNREKG NVQVYVEPGQ YVNPFTTVTL GWPDSDKDLH FQWSCGHCWA
HWSYCVERQL LCTDQRELVL PPSRLPPPNS AITLHLATWR GRELENREEK CLYVSAPLEL
KPRVSCENCR PANASEDVML RVTVGDDSSV AMFNWYLEDT SLEKAEPLPA ACRFQEFWLS
ALILLQSNTS MLWLNSSFRQ TWGQAIRIRA TALDRHAYGE DTXVISSLPA PEVPICTITP
EEGTILTSFT IFCNTSSALG PLEYCFCLES GSCLHCGPEP ALLSVYLPLG KVNNDFMLTV
VISVSNLSGD KQQAHAVVKV GLGDTHVDNV AFQAAVLENI TATLQGERDP ERLFQLSRAV
SSMLDQECQE QGCRGLLNMD VRQKVREHAQ GSLSAVTPTL GDIQXQVLRE VTHPNEELMP
MAQREATWAL QHASEALLAV SSKAHPEDQG RQAATKDLFQ AVSSTLEASL REGPEDPAEA
KGTQMASVPQ LLRVVEHVQA ALLLGTLPGG LPATLATPSI SIYTNRIQPR SWRGSSVHAA
AASSATFTLP AASSLGSMGD SPEPVDIRVM SFPKGPFPAW SHFDVSGTVG GLCLSSPSGH
LIPMKNLSEN IEILLPRLLE GHSEPTVLNL TSPEALWVNL TSDGAALGIQ LHWRPDIPFI
LSLGYGYHPN KTSYDAKAHL PPGATADGLS TWILNPEDLH FGKGVYYLTV IPESDLELTL
GRDFTVGITT FLSHCVFWDE VWGTWDNSGC QVGPRTTHSQ THCLCNHLTF FGSTFLVMPN
TIDICQIAEL FATFEDNPVV VTTVGCLCVA YVLVVIWARR KDAQDQAKVK VTVLEDNDPF
AQYHYLVTVY TGHRRGAATS SKVTVTLYGL DGESEPHHLS DPDIPVFERG GVDVFLLSTL
FPLGELRGLR LWHDNSGDRP SWYVSRVLVH DLARDRKWHF LCNSWLSTDV GDCVPDKVFP
VATEQDRKRF SHLFFMKTST GFHDGHIWYS IFRCSAWSNF TRVQRVSCCF SLLLCTMLTS
IMFWGVPKDP AEQKMDLGKI EFTWQEVMIG LESSLLMFPI NLLIVQIFRK TRPRVTKEQN
TGKCDRGSPS LASSLQPMEN GLLTLEVVTK DMWRLVSSLF KALKVPSPAS GWDSATLMDI
NQLLALEEVV CLQNMVGPEF WEEAKQRKDP LMLPLGSLRV QEQMQCLMPE VGPSDPQKDN
AYKQCLYLQL EHMEQELQLV GPRGFPQSQS HARALSQLQM LKGCLEGQLG TPPPGYTSFS
TASKHPRGLP WWCVLVGWLL VAATSGVAAF FTMLYGLHYG RASSLKWLIS VAVSFMESVF
VTQPLKVLGF AAFFALVLKR VEDEEELVAS LPGHLSGPGP SALFXVQRCS RKDIYQPPLA
TDIEKMKTTH LKEQKAFAFI REILAYLGFL WMLLLVAYGQ RDPSTYHFNR HLEHSFTQGF
SAVLSFKEFF MWANXTLMSN LYSHYPGFIT DGNSKLAGSA QIRQVRVLES SCPLVPQLQA
SLDECHAPYS LDIEDLSDYG EGWNASIPNN SSGFSQAWQY QSQSQCREYP IWGKLTVYRG
GGYVVPLGTD RKSASRILQY LFDNTWLDRL TRAVFVEFTV YNAKVNLFCI ITLTLEASAL
GTFFAHMSLQ SLRLYPFTDG WHPFVLAAEA IYLLFLLYYM ILQAKLMRKQ RWCYFHSKWN
LLELTIILAS WSALAMFVKR AILAEREIQR YRNHGEEGIS FSETAAADAA VGYIIAFLVL
LSTVKLWHLL RLNPKMNMIT SALCRAWGDI SGFIIVILIM LLAYSIASNL IFGWKPRSYK
TLFDAAETMI SLQLGIFNYE EVLDYSPVLG SFLIGSCIIF MTFVVLNLFI SVILVAFNEE
QKYDQLSEEG EIVDLLLMKI LGFLGIKCKK KEPSNSSEQP K
//
