PK1L_ACRMI
ID PK1L_ACRMI Reviewed; 3029 AA.
AC B8UU59;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Polycystic kidney disease 1-related protein {ECO:0000303|PubMed:23765379};
DE Flags: Precursor; Fragment;
OS Acropora millepora (Staghorn coral) (Heteropora millepora).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Acroporidae; Acropora.
OX NCBI_TaxID=45264;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=22490231; DOI=10.1111/j.1365-294x.2012.05554.x;
RA Moya A., Huisman L., Ball E.E., Hayward D.C., Grasso L.C., Chua C.M.,
RA Woo H.N., Gattuso J.P., Foret S., Miller D.J.;
RT "Whole transcriptome analysis of the coral Acropora millepora reveals
RT complex responses to CO(2)-driven acidification during the initiation of
RT calcification.";
RL Mol. Ecol. 21:2440-2454(2012).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 834-846; 960-977; 1088-1101 AND 1322-1334, TISSUE
RP SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23765379; DOI=10.1093/molbev/mst109;
RA Ramos-Silva P., Kaandorp J., Huisman L., Marie B., Zanella-Cleon I.,
RA Guichard N., Miller D.J., Marin F.;
RT "The skeletal proteome of the coral Acropora millepora: the evolution of
RT calcification by co-option and domain shuffling.";
RL Mol. Biol. Evol. 30:2099-2112(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}. Note=Presence in the organic matrix of the
CC skeleton may be due to shedding of a soluble peptide. {ECO:0000255,
CC ECO:0000303|PubMed:23765379}.
CC -!- TISSUE SPECIFICITY: Component of the acid-insoluble and acid-soluble
CC organic matrix of the aragonitic skeleton (at protein level).
CC {ECO:0000269|PubMed:23765379}.
CC -!- SIMILARITY: Belongs to the polycystin family. {ECO:0000305}.
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DR EMBL; JR978931; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; JR991141; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; JR991355; -; NOT_ANNOTATED_CDS; mRNA.
DR GO; GO:0005929; C:cilium; IEA:UniProt.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0001822; P:kidney development; IEA:InterPro.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000434; PC1.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR002859; PKD/REJ-like.
DR InterPro; IPR013122; PKD1_2_channel.
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; IPR014010; REJ_dom.
DR InterPro; IPR002889; WSC_carb-bd.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF00801; PKD; 2.
DR Pfam; PF08016; PKD_channel; 1.
DR Pfam; PF01477; PLAT; 1.
DR Pfam; PF02010; REJ; 1.
DR Pfam; PF01822; WSC; 1.
DR PRINTS; PR00500; POLYCYSTIN1.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00308; LH2; 1.
DR SMART; SM00089; PKD; 2.
DR SMART; SM00321; WSC; 1.
DR SUPFAM; SSF49299; SSF49299; 2.
DR SUPFAM; SSF49723; SSF49723; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50093; PKD; 2.
DR PROSITE; PS50095; PLAT; 1.
DR PROSITE; PS51111; REJ; 1.
DR PROSITE; PS51212; WSC; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Membrane; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..>3029
FT /note="Polycystic kidney disease 1-related protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000429553"
FT TOPO_DOM 22..1685
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1686..1706
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1707..1895
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1896..1916
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1917..1933
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1934..1954
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1955..2101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2102..2122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2123..2140
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2141..2161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2162..2250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2251..2271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2272..2462
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2463..2483
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2484..2496
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2497..2517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2518..2538
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2539..2559
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2560..2586
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2587..2607
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2608..2651
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2652..2672
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2673..3029
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..121
FT /note="WSC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00558"
FT DOMAIN 364..450
FT /note="PKD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 546..634
FT /note="PKD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT DOMAIN 633..1476
FT /note="REJ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00511"
FT DOMAIN 1621..1669
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT DOMAIN 1733..1851
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT REGION 754..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2704..2726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1051
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 3029
FT /evidence="ECO:0000305"
SQ SEQUENCE 3029 AA; 339369 MW; F8D915A0E6EC3601 CRC64;
MAKHLYLAFS LILVPFLVSK AKQTSNGEVP WLVGCYRYDF DSSIEVSYHL DHAEPFSCVR
LCASNESFRY AAVKNGRSCL CLARVEEKNR LNSSFCDVSC SEEMVNFTCG GKNVASVYST
AVPVIVSLKI RIPSKVKANA SVLAVSEVLF RRRKEVSYLN TIALGNETAD GVSVTWFLER
ELYNMTGYLQ NKTLKVHSRI WNTLDGNYTN TSSVFLFVIP GVNHVCVLAR NLFSQQKKCV
PVDVVVPVTG LQLEAIFFKG TMLSVSSSSL SVPLSKYVEI KYAISSGSKP QFLVSLGNRT
FHKAYNISGA AALSSSCLAV FPVFKSCGKK TIVVKAGNDF SLKSLRHLLV VHPFTEVLEF
EKTEGHCIFT RVNTSVTLKA TVGKDAPFGC PMSFEWNFND SSSIIITDGT SVSHVFSSIQ
TYLVTVTLNN KFQRKQAAQQ VCVQDNIKGV TLLPNVSYLI VSTNHEENLF SVQLSPSADC
CGEVSYQFYK NETAFPLTAG RNSPVFHDSK PGRYVVFVQA SNGISYATSN KILVDVMEPI
SSLFIDHLFL NHSHLSPGGK QVHFVAHLAT GTNITYSWKF IGGSWENSIN TTSNKVNYTF
SKNGRYEVVL TASNAISKET ASVDIVISDI PECYTRGVAI VGGMREVIRS QEIHLEAKLN
LTCNVVNELR YLWKVTRRSD DDYDDDNHLS FFTYQVLIPP CTLEYGMYSI QLEVTMIDAK
GIYLSSKNKK EIMITKSPLV AVISGGTERT VSKRKGPITL SASSSHDPDH PDEHKNLRFK
WTCRPHGSSI SCFNESTLPE IDFSKDALTF NVDWLMADFS HEFEVEVSKQ DDPRSSTAFQ
ILYVREKDEL FEHVLSLNCI QCEKGHINPS QSLVIRGSCL SCSLDNPQIT YRWKLYEVDS
FVEGNTWECP SDDHSDRVTP STTPMTDSNS PSVLQITDSY LEFTIGPCLG NKFEKSAGNK
SGLASGSGDG TGNEIKYSSV KAPLKGNETS AIKADDSGDV DDDEVNNDND DDSSSYSRST
LPTPLSMTNA NSVNKPIITT DTPSFNKPNK PINPSMLWSR RRELRHLGEQ TTTGIENQNL
VLLGKFLKGG QTYLATFDVR DLETKQKGLA SIIFQTSVSL KCGVCQITPA VGFSLQTTFQ
LVCSNWRSRQ LLQYHVRYTI EGDRKEFIYS GLRDVTLFVL PAGNPFSNRT VEVHVEVSDG
YSPSRTFRPI KVQVKPQTVA KGSSEEEVLL NETDGNNLSL LQMAGDEQRV LQFIMALSIS
LNRLSQVKNV SSNFHLRVAI REKLLNRFQN LSVYDKYSAL QTCLALQSLT SKPDEIGANN
VKVASQVLYN VIKNVTSKHK RKKKSLIEAR QLLSQELIDC ATTVTSNLIE AASLAVQRQD
TTEKMLVMVT EATEQLIMAK LSTQVYGEHS LKVSTRNIIA EATQKRSVSN FSSSLSEFQF
FMPSHLEEQL NITERCFGTM ITCFQENPYF SDMNHTKVGS LSINHCSGEE IQVKNLGSDI
TILIPMGHGG AEKHPLNFML KWNHRNVHVI NQTAKMENQS LQLHLRPRSV LPSAFNVKFV
VRTGKETLLF RSSGEAVNLF VDQEQLRSGS LNASVELEDT AYYRLKSVKG VSFNYSLGMQ
WIGCFYWNKR GKHWASDGCR LEKSINHTLV CRCNHLTAFS GGFIQPPNSL HLEDLRDTDK
LKNSPLTMVL VISILVMYFL LLGFCVKADR HDKKKLGVIF LDDSTTFDAN SQSRFQLSVQ
TGHWFGAGTS ADVYLILHDN DVVSHPVELK YVGKPLFQRS SCDVFLLSFP KNLIRNISKI
HVWHDNKGDY PSWFLERITI KNVQTGERWV FECNRWLAVD EGNGKVECEL FAKKSWSTGL
KESFLQHSAK AFLDYHLWLS LLGRPSYSRF TRAQRLSCCL SLLLSFLCVN IAWYRPKIEV
TEVLGVLDVS ANSIMIGVLG SLMVLPVNFL WIFFFRYSRR SLSRRVKACY PKSEHHTEIT
ELVSSSVIDQ SLETVQILSN FGAMRRMLQT RGTQVSGGNV PMSNPNGSGV CYLSAHDDLI
SDLPLPKGSA GLVETCDFLA ALAPTRKKHD VAFDQQSTYS VYAPTTEGRG FYRSKFSLPH
GFVYVAWFGC LITGTVTSAI TIWYGLSFGW DLSVHWFQSL VFSLLESLLL SQPIMVLAFI
FYMSHKTKSG KEDEDNDEGF EDLSTSDVNN IHYGYLNPGF DGQTTKKTPI DKALADRRRQ
RHLKYLKPPP LSQLAETREK SLKNRVLRNY VVELFVFIMF FVVTCALVFS VADPDVYHLN
QSIRTSFLRS HYFTRPENVV DAWKRMSAVL VENASAPSPL MMLLPGTQSL LFGRTKVKKY
YSPNVKVCHE APAIQNSNTS TPLCYAGCHA SKGLWITIDL NLTRAAAARQ LTQFADTQWN
NSCTREVSLD FAIYTPFLRA ISAVTLSVKS SFVGTAKCDM ELISAPVVFS SNGYSYFIRF
TKLLFVVFFL YLLQHEFFLA LKMTFSYFTN FWRVYQLLTI AISSACIVSY IHWSLSLYAL
LREVETERQS RVFYLSRQIS WSQGFLQASY SLLLFLLLIR CLHLLRPFRF VRHFGRILST
SISSLLACWV FGFILVVAFA HPGYLLFGSV HSSFKSFGDA FLLVTSFFRL EGVARYQDFA
LEEQTLLLST YFALFLIGFC VIVRGSTAAV VLHGIRCLGK RRRGLLSTVF EEFIRIKLQL
SKEKKPKKPR PNSVSDLEET DDEDDLEQEA FLEEGPFFPT DHVLDELDAQ IEEMSWRVES
LFDDDPCADS ISCTNSLLST WLEDCDQGDV EYLYEAGNDP SVYSAGSGYE SDHSAMSNSR
CYFSSSSSLD IPDERIRHER VIGAKVGSHG CRGDHSLLTV APNKTTAKQS YFCSSGRDES
GSSINFSGDG YESPACSVPQ GNMCDLPGAC ENPNILRNIV LRDSDLREGV LRDRTVWWDG
ETKKDMSLGA HTLHREKEPI KPKVMYGMVR GCSQKGEKAF PELANIAPHM EATTAGESSE
EATCSSSDYE IGKEEASVIP VGQRVVSAM
