TRPC5_HUMAN
ID TRPC5_HUMAN Reviewed; 973 AA.
AC Q9UL62; B2RP53; O75233; Q5JXY8; Q9Y514;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Short transient receptor potential channel 5;
DE Short=TrpC5;
DE AltName: Full=Transient receptor protein 5;
DE Short=TRP-5;
DE Short=hTRP-5;
DE Short=hTRP5;
GN Name=TRPC5; Synonyms=TRP5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal brain;
RX PubMed=10493832; DOI=10.1006/geno.1999.5924;
RA Sossey-Alaoui K., Lyon J.A., Jones L., Abidi F.E., Hartung A.J., Hane B.,
RA Schwartz C.E., Stevenson R.E., Srivastava A.K.;
RT "Molecular cloning and characterization of TRPC5 (HTRP5), the human
RT homologue of a mouse brain receptor-activated capacitative Ca(2+) entry
RT channel.";
RL Genomics 60:330-340(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=9687496; DOI=10.1093/emboj/17.15.4274;
RA Philipp S., Hambrecht J., Braslavski L., Schroth G., Freichel M.,
RA Murakami M., Cavalie A., Flockerzi V.;
RT "A novel capacitative calcium entry channel expressed in excitable cells.";
RL EMBO J. 17:4274-4282(1998).
RN [6]
RP SUBUNIT.
RX PubMed=12032305; DOI=10.1073/pnas.102596199;
RA Hofmann T., Schaefer M., Schultz G., Gudermann T.;
RT "Subunit composition of mammalian transient receptor potential channels in
RT living cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7461-7466(2002).
RN [7]
RP INTERACTION WITH MX1.
RX PubMed=15757897; DOI=10.1074/jbc.m500391200;
RA Lussier M.P., Cayouette S., Lepage P.K., Bernier C.L., Francoeur N.,
RA St-Hilaire M., Pinard M., Boulay G.;
RT "MxA, a member of the dynamin superfamily, interacts with the ankyrin-like
RT repeat domain of TRPC.";
RL J. Biol. Chem. 280:19393-19400(2005).
RN [8]
RP INTERACTION WITH CABP1.
RX PubMed=15895247; DOI=10.1007/s00424-005-1419-1;
RA Kinoshita-Kawada M., Tang J., Xiao R., Kaneko S., Foskett J.K., Zhu M.X.;
RT "Inhibition of TRPC5 channels by Ca2+-binding protein 1 in Xenopus
RT oocytes.";
RL Pflugers Arch. 450:345-354(2005).
RN [9]
RP FUNCTION AS CALCIUM CHANNEL, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=16284075; DOI=10.1113/jphysiol.2005.097998;
RA Shimizu S., Yoshida T., Wakamori M., Ishii M., Okada T., Takahashi M.,
RA Seto M., Sakurada K., Kiuchi Y., Mori Y.;
RT "Ca2+-calmodulin-dependent myosin light chain kinase is essential for
RT activation of TRPC5 channels expressed in HEK293 cells.";
RL J. Physiol. (Lond.) 570:219-235(2006).
RN [10]
RP INTERACTION WITH RNF24.
RX PubMed=17850865; DOI=10.1016/j.ceca.2007.07.009;
RA Lussier M.P., Lepage P.K., Bousquet S.M., Boulay G.;
RT "RNF24, a new TRPC interacting protein, causes the intracellular retention
RT of TRPC.";
RL Cell Calcium 43:432-443(2008).
RN [11]
RP INTERACTION WITH SESTD1.
RX PubMed=20164195; DOI=10.1074/jbc.m109.068304;
RA Miehe S., Bieberstein A., Arnould I., Ihdene O., Rutten H., Strubing C.;
RT "The phospholipid-binding protein SESTD1 is a novel regulator of the
RT transient receptor potential channels TRPC4 and TRPC5.";
RL J. Biol. Chem. 285:12426-12434(2010).
RN [12]
RP INTERACTION WITH PLSCR1.
RX PubMed=32110987; DOI=10.3390/cells9030547;
RA Guo J., Li J., Xia L., Wang Y., Zhu J., Du J., Lu Y., Liu G., Yao X.,
RA Shen B.;
RT "Transient Receptor Potential Canonical 5-Scramblase Signaling Complex
RT Mediates Neuronal Phosphatidylserine Externalization and Apoptosis.";
RL Cells 9:0-0(2020).
RN [13]
RP VARIANT THR-667.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
CC -!- FUNCTION: Thought to form a receptor-activated non-selective calcium
CC permeant cation channel. Probably is operated by a phosphatidylinositol
CC second messenger system activated by receptor tyrosine kinases or G-
CC protein coupled receptors. Has also been shown to be calcium-selective
CC (By similarity). May also be activated by intracellular calcium store
CC depletion. Mediates calcium-dependent phosphatidylserine
CC externalization and apoptosis in neurons via its association with
CC PLSCR1 (By similarity). {ECO:0000250|UniProtKB:Q9QX29,
CC ECO:0000269|PubMed:16284075}.
CC -!- ACTIVITY REGULATION: Calcium channel activity is enhanced by MYLK, that
CC promotes its subcellular localization at the plasma membrane.
CC {ECO:0000269|PubMed:16284075}.
CC -!- SUBUNIT: Interacts with TRPC4AP (By similarity). Homotetramer and
CC heterotetramer with TRPC1 and/or TRPC4 (PubMed:12032305). Interacts
CC with SLC9A3R1/NHERF (By similarity). Interacts with MX1 and RNF24
CC (PubMed:15757897, PubMed:17850865). Interacts (via C-terminus) with
CC CABP1 (PubMed:15895247). Interacts with SESTD1 (via the spectrin 1
CC repeat) (PubMed:20164195). Interacts with PLSCR1 (PubMed:32110987).
CC {ECO:0000250|UniProtKB:Q9QX29, ECO:0000269|PubMed:12032305,
CC ECO:0000269|PubMed:15757897, ECO:0000269|PubMed:15895247,
CC ECO:0000269|PubMed:17850865, ECO:0000269|PubMed:20164195,
CC ECO:0000269|PubMed:32110987}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16284075};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16284075}.
CC -!- TISSUE SPECIFICITY: Expressed in brain with higher levels in fetal
CC brain. Found in cerebellum and occipital pole.
CC {ECO:0000269|PubMed:9687496}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. STrpC
CC subfamily. TRPC5 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF054568; AAF00002.1; -; mRNA.
DR EMBL; AC005191; AAC24563.1; -; Genomic_DNA.
DR EMBL; AL049563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471120; EAX02630.1; -; Genomic_DNA.
DR EMBL; BC137271; AAI37272.1; -; mRNA.
DR EMBL; BC137274; AAI37275.1; -; mRNA.
DR CCDS; CCDS14561.1; -.
DR RefSeq; NP_036603.1; NM_012471.2.
DR RefSeq; XP_016885263.1; XM_017029774.1.
DR PDB; 6YSN; EM; 3.00 A; A/B/C/D=1-765.
DR PDB; 7D4P; EM; 2.70 A; A/B/C/D=1-764.
DR PDB; 7D4Q; EM; 2.74 A; A/B/C/D=1-764.
DR PDB; 7E4T; EM; 3.00 A; A/B/C/D=1-764.
DR PDB; 7WDB; EM; 2.40 A; A/B/C/D=1-764.
DR PDBsum; 6YSN; -.
DR PDBsum; 7D4P; -.
DR PDBsum; 7D4Q; -.
DR PDBsum; 7E4T; -.
DR PDBsum; 7WDB; -.
DR AlphaFoldDB; Q9UL62; -.
DR SMR; Q9UL62; -.
DR BioGRID; 113075; 21.
DR IntAct; Q9UL62; 3.
DR STRING; 9606.ENSP00000262839; -.
DR BindingDB; Q9UL62; -.
DR ChEMBL; CHEMBL1250411; -.
DR DrugCentral; Q9UL62; -.
DR GuidetoPHARMACOLOGY; 490; -.
DR TCDB; 1.A.4.1.7; the transient receptor potential ca(2+) channel (trp-cc) family.
DR GlyGen; Q9UL62; 1 site.
DR iPTMnet; Q9UL62; -.
DR PhosphoSitePlus; Q9UL62; -.
DR SwissPalm; Q9UL62; -.
DR BioMuta; TRPC5; -.
DR DMDM; 10720321; -.
DR EPD; Q9UL62; -.
DR jPOST; Q9UL62; -.
DR MassIVE; Q9UL62; -.
DR MaxQB; Q9UL62; -.
DR PaxDb; Q9UL62; -.
DR PeptideAtlas; Q9UL62; -.
DR PRIDE; Q9UL62; -.
DR ProteomicsDB; 84958; -.
DR ABCD; Q9UL62; 1 sequenced antibody.
DR Antibodypedia; 356; 306 antibodies from 32 providers.
DR DNASU; 7224; -.
DR Ensembl; ENST00000262839.3; ENSP00000262839.2; ENSG00000072315.4.
DR GeneID; 7224; -.
DR KEGG; hsa:7224; -.
DR MANE-Select; ENST00000262839.3; ENSP00000262839.2; NM_012471.3; NP_036603.1.
DR UCSC; uc004epl.2; human.
DR CTD; 7224; -.
DR DisGeNET; 7224; -.
DR GeneCards; TRPC5; -.
DR HGNC; HGNC:12337; TRPC5.
DR HPA; ENSG00000072315; Tissue enriched (brain).
DR MIM; 300334; gene.
DR neXtProt; NX_Q9UL62; -.
DR OpenTargets; ENSG00000072315; -.
DR PharmGKB; PA37010; -.
DR VEuPathDB; HostDB:ENSG00000072315; -.
DR eggNOG; KOG3609; Eukaryota.
DR GeneTree; ENSGT01050000244831; -.
DR HOGENOM; CLU_005716_4_1_1; -.
DR InParanoid; Q9UL62; -.
DR OMA; ACSQSEM; -.
DR OrthoDB; 824310at2759; -.
DR PhylomeDB; Q9UL62; -.
DR TreeFam; TF313147; -.
DR PathwayCommons; Q9UL62; -.
DR Reactome; R-HSA-3295583; TRP channels.
DR Reactome; R-HSA-418890; Role of second messengers in netrin-1 signaling.
DR SignaLink; Q9UL62; -.
DR BioGRID-ORCS; 7224; 15 hits in 693 CRISPR screens.
DR ChiTaRS; TRPC5; human.
DR GeneWiki; TRPC5; -.
DR GenomeRNAi; 7224; -.
DR Pharos; Q9UL62; Tchem.
DR PRO; PR:Q9UL62; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9UL62; protein.
DR Bgee; ENSG00000072315; Expressed in cortical plate and 26 other tissues.
DR Genevisible; Q9UL62; HS.
DR GO; GO:0034704; C:calcium channel complex; IDA:UniProtKB.
DR GO; GO:0034703; C:cation channel complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0003779; F:actin binding; IEA:Ensembl.
DR GO; GO:0042805; F:actinin binding; IEA:Ensembl.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:0005262; F:calcium channel activity; IDA:UniProtKB.
DR GO; GO:0030276; F:clathrin binding; IEA:Ensembl.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IBA:GO_Central.
DR GO; GO:0015279; F:store-operated calcium channel activity; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; TAS:ProtInc.
DR GO; GO:0006828; P:manganese ion transport; IBA:GO_Central.
DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0070782; P:phosphatidylserine exposure on apoptotic cell surface; ISS:UniProtKB.
DR GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IEA:Ensembl.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:1902630; P:regulation of membrane hyperpolarization; IEA:Ensembl.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR013555; TRP_dom.
DR InterPro; IPR005461; TRPC5_channel.
DR InterPro; IPR002153; TRPC_channel.
DR PANTHER; PTHR10117; PTHR10117; 1.
DR PANTHER; PTHR10117:SF76; PTHR10117:SF76; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF08344; TRP_2; 1.
DR PRINTS; PR01097; TRNSRECEPTRP.
DR PRINTS; PR01646; TRPCHANNEL5.
DR SMART; SM00248; ANK; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Calcium; Calcium channel; Calcium transport;
KW Cell membrane; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..973
FT /note="Short transient receptor potential channel 5"
FT /id="PRO_0000215318"
FT TOPO_DOM 1..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..398
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..470
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..512
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 534..603
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 604..624
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 625..973
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 31..60
FT /note="ANK 1"
FT REPEAT 69..97
FT /note="ANK 2"
FT REPEAT 98..124
FT /note="ANK 3"
FT REPEAT 141..170
FT /note="ANK 4"
FT REGION 766..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..973
FT /note="Essential for binding to SLC9A3R1 PDZ domain"
FT /evidence="ECO:0000250|UniProtKB:Q9QX29"
FT COMPBIAS 820..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 667
FT /note="P -> T (found in a patient with severe delayed
FT speech, autism spectrum and Gilles de la Tourette
FT disorders)"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_069415"
FT VARIANT 702
FT /note="R -> H (in dbSNP:rs36047478)"
FT /id="VAR_052369"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 45..58
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 145..152
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:7D4P"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 189..203
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 216..233
FT /evidence="ECO:0007829|PDB:7D4P"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:6YSN"
FT HELIX 238..257
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 262..269
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 288..295
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 305..315
FT /evidence="ECO:0007829|PDB:7D4P"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:7E4T"
FT TURN 320..323
FT /evidence="ECO:0007829|PDB:6YSN"
FT HELIX 327..339
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 341..350
FT /evidence="ECO:0007829|PDB:7D4P"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:7D4P"
FT TURN 355..359
FT /evidence="ECO:0007829|PDB:7D4P"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 363..383
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 402..425
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 428..432
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 434..459
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 474..491
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 492..499
FT /evidence="ECO:0007829|PDB:7D4P"
FT TURN 501..503
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 504..539
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 540..542
FT /evidence="ECO:0007829|PDB:7D4P"
FT TURN 546..548
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 550..552
FT /evidence="ECO:0007829|PDB:6YSN"
FT STRAND 555..560
FT /evidence="ECO:0007829|PDB:7D4P"
FT STRAND 564..567
FT /evidence="ECO:0007829|PDB:6YSN"
FT HELIX 568..579
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 585..588
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 595..614
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 616..631
FT /evidence="ECO:0007829|PDB:7D4P"
FT TURN 632..634
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 635..649
FT /evidence="ECO:0007829|PDB:7D4P"
FT STRAND 651..653
FT /evidence="ECO:0007829|PDB:7D4P"
FT TURN 659..662
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 707..733
FT /evidence="ECO:0007829|PDB:7D4P"
FT HELIX 740..761
FT /evidence="ECO:0007829|PDB:7D4P"
SQ SEQUENCE 973 AA; 111412 MW; FBC8CBF17BE42166 CRC64;
MAQLYYKKVN YSPYRDRIPL QIVRAETELS AEEKAFLNAV EKGDYATVKQ ALQEAEIYYN
VNINCMDPLG RSALLIAIEN ENLEIMELLL NHSVYVGDAL LYAIRKEVVG AVELLLSYRR
PSGEKQVPTL MMDTQFSEFT PDITPIMLAA HTNNYEIIKL LVQKRVTIPR PHQIRCNCVE
CVSSSEVDSL RHSRSRLNIY KALASPSLIA LSSEDPILTA FRLGWELKEL SKVENEFKAE
YEELSQQCKL FAKDLLDQAR SSRELEIILN HRDDHSEELD PQKYHDLAKL KVAIKYHQKE
FVAQPNCQQL LATLWYDGFP GWRRKHWVVK LLTCMTIGFL FPMLSIAYLI SPRSNLGLFI
KKPFIKFICH TASYLTFLFM LLLASQHIVR TDLHVQGPPP TVVEWMILPW VLGFIWGEIK
EMWDGGFTEY IHDWWNLMDF AMNSLYLATI SLKIVAYVKY NGSRPREEWE MWHPTLIAEA
LFAISNILSS LRLISLFTAN SHLGPLQISL GRMLLDILKF LFIYCLVLLA FANGLNQLYF
YYETRAIDEP NNCKGIRCEK QNNAFSTLFE TLQSLFWSVF GLLNLYVTNV KARHEFTEFV
GATMFGTYNV ISLVVLLNML IAMMNNSYQL IADHADIEWK FARTKLWMSY FDEGGTLPPP
FNIIPSPKSF LYLGNWFNNT FCPKRDPDGR RRRRNLRSFT ERNADSLIQN QHYQEVIRNL
VKRYVAAMIR NSKTHEGLTE ENFKELKQDI SSFRYEVLDL LGNRKHPRSF STSSTELSQR
DDNNDGSGGA RAKSKSVSFN LGCKKKTCHG PPLIRTMPRS SGAQGKSKAE SSSKRSFMGP
SLKKLGLLFS KFNGHMSEPS SEPMYTISDG IVQQHCMWQD IRYSQMEKGK AEACSQSEIN
LSEVELGEVQ GAAQSSECPL ACSSSLHCAS SICSSNSKLL DSSEDVFETW GEACDLLMHK
WGDGQEEQVT TRL
