PTHD1_MOUSE
ID PTHD1_MOUSE Reviewed; 888 AA.
AC Q14B62; B1AZU9; Q14B63; Q8BZA5;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Patched domain-containing protein 1 {ECO:0000305};
GN Name=ptchd1 {ECO:0000312|MGI:MGI:2685233};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-852 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20844286; DOI=10.1126/scitranslmed.3001267;
RA Noor A., Whibley A., Marshall C.R., Gianakopoulos P.J., Piton A.,
RA Carson A.R., Orlic-Milacic M., Lionel A.C., Sato D., Pinto D., Drmic I.,
RA Noakes C., Senman L., Zhang X., Mo R., Gauthier J., Crosbie J.,
RA Pagnamenta A.T., Munson J., Estes A.M., Fiebig A., Franke A., Schreiber S.,
RA Stewart A.F., Roberts R., McPherson R., Guter S.J., Cook E.H. Jr.,
RA Dawson G., Schellenberg G.D., Battaglia A., Maestrini E., Jeng L.,
RA Hutchison T., Rajcan-Separovic E., Chudley A.E., Lewis S.M., Liu X.,
RA Holden J.J., Fernandez B., Zwaigenbaum L., Bryson S.E., Roberts W.,
RA Szatmari P., Gallagher L., Stratton M.R., Gecz J., Brady A.F.,
RA Schwartz C.E., Schachar R.J., Monaco A.P., Rouleau G.A., Hui C.C.,
RA Lucy Raymond F., Scherer S.W., Vincent J.B.;
RT "Disruption at the PTCHD1 Locus on Xp22.11 in Autism spectrum disorder and
RT intellectual disability.";
RL Sci. Transl. Med. 2:49RA68-49RA68(2010).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27007844; DOI=10.1038/nature17427;
RA Wells M.F., Wimmer R.D., Schmitt L.I., Feng G., Halassa M.M.;
RT "Thalamic reticular impairment underlies attention deficit in Ptchd1(Y/-)
RT mice.";
RL Nature 532:58-63(2016).
CC -!- FUNCTION: Required for the development and function of the thalamic
CC reticular nucleus (TRN), a part of the thalamus that is critical for
CC thalamocortical transmission, generation of sleep rhythms, sensorimotor
CC processing and attention. {ECO:0000269|PubMed:27007844}.
CC -!- INTERACTION:
CC Q14B62; Q62108: Dlg4; NbExp=8; IntAct=EBI-27105784, EBI-300895;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96NR3};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96NR3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14B62-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14B62-2; Sequence=VSP_023514;
CC -!- TISSUE SPECIFICITY: Broadly expressed in the brain (PubMed:20844286).
CC Selectively expressed in the thalamic reticular nucleus (TRN) in early
CC development and continues to be enriched in this structure throughout
CC adult life (PubMed:27007844). {ECO:0000269|PubMed:20844286,
CC ECO:0000269|PubMed:27007844}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed in the developing brain from 9.5
CC day post coitum (dpc) to postnatal day 1 (P1) (PubMed:20844286).
CC Specifically expressed in the thalamic reticular nucleus (TRN) at
CC birth. Expressed in the striatum, cortex and cerebellum by P15 onwards
CC (PubMed:27007844). {ECO:0000269|PubMed:20844286,
CC ECO:0000269|PubMed:27007844}.
CC -!- DISRUPTION PHENOTYPE: Mice show decreased spindles and sleep
CC fragmentation, learning defects, hyper-aggressive behavior and motor
CC defects. Selective deletion in the thalamic reticular nucleus (TRN)
CC leads to attention deficits and hyperactivity. Defects are probably due
CC to dcreased TRN activity through mechanisms involving small conductance
CC calcium-dependent potassium currents (SK).
CC {ECO:0000269|PubMed:27007844}.
CC -!- SIMILARITY: Belongs to the patched family. {ECO:0000305}.
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DR EMBL; BX088539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX119953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC116312; AAI16313.1; -; mRNA.
DR EMBL; BC116313; AAI16314.1; -; mRNA.
DR EMBL; AK036111; BAC29308.1; -; mRNA.
DR CCDS; CCDS41188.1; -. [Q14B62-1]
DR RefSeq; NP_001087219.1; NM_001093750.1. [Q14B62-1]
DR RefSeq; XP_006528856.1; XM_006528793.3. [Q14B62-2]
DR RefSeq; XP_011246114.1; XM_011247812.2. [Q14B62-1]
DR AlphaFoldDB; Q14B62; -.
DR SMR; Q14B62; -.
DR IntAct; Q14B62; 36.
DR MINT; Q14B62; -.
DR STRING; 10090.ENSMUSP00000039443; -.
DR GlyConnect; 2576; 1 N-Linked glycan (1 site).
DR GlyGen; Q14B62; 10 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q14B62; -.
DR PhosphoSitePlus; Q14B62; -.
DR EPD; Q14B62; -.
DR PaxDb; Q14B62; -.
DR PRIDE; Q14B62; -.
DR ProteomicsDB; 291587; -. [Q14B62-1]
DR ProteomicsDB; 291588; -. [Q14B62-2]
DR Antibodypedia; 55285; 93 antibodies from 21 providers.
DR Ensembl; ENSMUST00000038665; ENSMUSP00000039443; ENSMUSG00000041552. [Q14B62-1]
DR GeneID; 211612; -.
DR KEGG; mmu:211612; -.
DR UCSC; uc009urw.1; mouse. [Q14B62-1]
DR CTD; 139411; -.
DR MGI; MGI:2685233; Ptchd1.
DR VEuPathDB; HostDB:ENSMUSG00000041552; -.
DR eggNOG; KOG1934; Eukaryota.
DR GeneTree; ENSGT00940000157080; -.
DR HOGENOM; CLU_002359_2_2_1; -.
DR InParanoid; Q14B62; -.
DR OMA; MYTRYQE; -.
DR PhylomeDB; Q14B62; -.
DR TreeFam; TF331806; -.
DR BioGRID-ORCS; 211612; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Ptchd1; mouse.
DR PRO; PR:Q14B62; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q14B62; protein.
DR Bgee; ENSMUSG00000041552; Expressed in metencephalon and 51 other tissues.
DR ExpressionAtlas; Q14B62; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0050890; P:cognition; IMP:UniProtKB.
DR GO; GO:0098976; P:excitatory chemical synaptic transmission; IMP:MGI.
DR GO; GO:0098977; P:inhibitory chemical synaptic transmission; IMP:MGI.
DR GO; GO:0007616; P:long-term memory; IMP:MGI.
DR GO; GO:0007614; P:short-term memory; IMP:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; ISO:MGI.
DR GO; GO:0035176; P:social behavior; IMP:UniProtKB.
DR GO; GO:0021794; P:thalamus development; IMP:UniProtKB.
DR InterPro; IPR003392; Ptc/Disp.
DR InterPro; IPR000731; SSD.
DR Pfam; PF02460; Patched; 1.
DR PROSITE; PS50156; SSD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..888
FT /note="Patched domain-containing protein 1"
FT /id="PRO_0000280041"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 502..522
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 707..727
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 738..758
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 795..815
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 826..846
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 268..427
FT /note="SSD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00199"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 599
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 608
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 762
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 818
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..105
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023514"
FT CONFLICT 767
FT /note="N -> D (in Ref. 2; AAI16313)"
FT /evidence="ECO:0000305"
FT CONFLICT 840
FT /note="A -> T (in Ref. 2; AAI16314)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 888 AA; 101506 MW; 685615193583F149 CRC64;
MLRQVLHRGL RTCFSRLGHF IASHPVFFAS APVLISILLG ASFSRYQVEE SVEHLLAPQH
SLAKIERNLV NSLFPVNRSK HRLYSDLQTP GRYGRVIVTS YQKANMLDQH HTDLILKLHT
AVTKIQVPRP GFNYTFAHIC VLNNDKTCIV DDIVHVLEEL KNARATNRTN FAITYPITHL
KDGRAVYNGH QLGGVTVHSK DRVKSAEAIQ LTYYLQSINS LNDMVAERWE SSFCDTVKLF
QKSNSKVKIY PYTSSSLRED FQKTSRVSER YLVTSLILVV TMAILCCSMQ DCVRSKPWLG
LLGLVTISLA TLTAAGIINL TGGKYNSTFL GVPFVMLGHG LYGTFEMLSS WRKTREDQHV
KERTAEVYAD SMLSFSLTTA MYLVTFGIGA SPFTNIEAAR IFCCNSCIAI LFNYLYVLSF
YGSSLVFTGY IENNYQHSIF CRKVPKPDVL QEKPAWYRFL LTARFSEETA EGEEANTYES
HLLVCFLKRY YCDWITNTYV KPFVVLFYLI YISFALMGYL QVSEGSDLSN IVATATQTIE
YTTAHQKYFN NYSPVIGFYI YESIEYWNSS VQEDVLEYTK GFVRISWFES YLNYLRKLNV
STDLPKKNFT DMLRNSFLKT PQFSHFQEDI IFSKKYNDEV DVVASRMFLV AKTMETNREE
LYDLLETLRR LSVTSKVKFI VFNPSFVYMD RYASSLGAPL HNSCISALFL LFFSAFLVAD
SLINVWITLT VVSVEFGVIG FMTLWKVELD CISVLCLIYG INYTIDNCAP LLSTFVLGKD
FTRTKWVKNA LEVHGVAILQ SYLCYIVGLF PLAAVPSNLT CTLFRCLFLI AFVTFFHCFA
ILPVILTFLP PSKKKRKEKK NPENREEIEC VEMVDIDSTR VVDQITTV
