PRRT2_HUMAN
ID PRRT2_HUMAN Reviewed; 340 AA.
AC Q7Z6L0; A8K8M8; Q8N2N8; Q8NAQ7; Q8ND36; Q96FA8;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Proline-rich transmembrane protein 2;
DE AltName: Full=Dispanin subfamily B member 3;
DE Short=DSPB3;
GN Name=PRRT2;
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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Teratocarcinoma, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryo;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Eye;
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 [6]
RP INTERACTION WITH GRIA1 AND SNAP25, SUBCELLULAR LOCATION, AND
RP CHARACTERIZATION OF VARIANT EKD1 THR-287.
RX PubMed=25915028; DOI=10.3390/ijms16059134;
RA Li M., Niu F., Zhu X., Wu X., Shen N., Peng X., Liu Y.;
RT "PRRT2 Mutant Leads to Dysfunction of Glutamate Signaling.";
RL Int. J. Mol. Sci. 16:9134-9151(2015).
RN [7]
RP INVOLVEMENT IN EKD1, SUBCELLULAR LOCATION, AND VARIANTS ALA-138; HIS-147;
RP PRO-214; ARG-237 AND HIS-245.
RX PubMed=22101681; DOI=10.1038/ng.1008;
RA Chen W.J., Lin Y., Xiong Z.Q., Wei W., Ni W., Tan G.H., Guo S.L., He J.,
RA Chen Y.F., Zhang Q.J., Li H.F., Lin Y., Murong S.X., Xu J., Wang N.,
RA Wu Z.Y.;
RT "Exome sequencing identifies truncating mutations in PRRT2 that cause
RT paroxysmal kinesigenic dyskinesia.";
RL Nat. Genet. 43:1252-1255(2011).
RN [8]
RP INVOLVEMENT IN BFIS2 AND ICCA, VARIANT ICCA ASN-317, AND VARIANTS ARG-215
RP AND LEU-216.
RX PubMed=22243967; DOI=10.1016/j.ajhg.2011.12.003;
RA Heron S.E., Grinton B.E., Kivity S., Afawi Z., Zuberi S.M., Hughes J.N.,
RA Pridmore C., Hodgson B.L., Iona X., Sadleir L.G., Pelekanos J.,
RA Herlenius E., Goldberg-Stern H., Bassan H., Haan E., Korczyn A.D.,
RA Gardner A.E., Corbett M.A., Gecz J., Thomas P.Q., Mulley J.C.,
RA Berkovic S.F., Scheffer I.E., Dibbens L.M.;
RT "PRRT2 mutations cause benign familial infantile epilepsy and infantile
RT convulsions with choreoathetosis syndrome.";
RL Am. J. Hum. Genet. 90:152-160(2012).
RN [9]
RP INVOLVEMENT IN ICCA, VARIANT ICCA 240-ARG--LYS-340 DEL, INTERACTION WITH
RP SNAP25, AND SUBCELLULAR LOCATION.
RX PubMed=22832103; DOI=10.1016/j.celrep.2011.11.001;
RA Lee H.Y., Huang Y., Bruneau N., Roll P., Roberson E.D., Hermann M.,
RA Quinn E., Maas J., Edwards R., Ashizawa T., Baykan B., Bhatia K.,
RA Bressman S., Bruno M.K., Brunt E.R., Caraballo R., Echenne B., Fejerman N.,
RA Frucht S., Gurnett C.A., Hirsch E., Houlden H., Jankovic J., Lee W.L.,
RA Lynch D.R., Mohammed S., Mueller U., Nespeca M.P., Renner D., Rochette J.,
RA Rudolf G., Saiki S., Soong B.W., Swoboda K.J., Tucker S., Wood N.,
RA Hanna M., Bowcock A.M., Szepetowski P., Fu Y.H., Ptacek L.J.;
RT "Mutations in the gene PRRT2 cause paroxysmal kinesigenic dyskinesia with
RT infantile convulsions.";
RL Cell Rep. 1:2-12(2012).
RN [10]
RP INVOLVEMENT IN BFIS2.
RX PubMed=22399141; DOI=10.1038/jhg.2012.23;
RA Ono S., Yoshiura K.I., Kinoshita A., Kikuchi T., Nakane Y., Kato N.,
RA Sadamatsu M., Konishi T., Nagamitsu S., Matsuura M., Yasuda A., Komine M.,
RA Kanai K., Inoue T., Osamura T., Saito K., Hirose S., Koide H., Tomita H.,
RA Ozawa H., Niikawa N., Kurotaki N.;
RT "Mutations in PRRT2 responsible for paroxysmal kinesigenic dyskinesias also
RT cause benign familial infantile convulsions.";
RL J. Hum. Genet. 57:338-341(2012).
RN [11]
RP VARIANT EKD1 ARG-305.
RX PubMed=22209761; DOI=10.1136/jmedgenet-2011-100653;
RA Liu Q., Qi Z., Wan X.H., Li J.Y., Shi L., Lu Q., Zhou X.Q., Qiao L.,
RA Wu L.W., Liu X.Q., Yang W., Liu Y., Cui L.Y., Zhang X.;
RT "Mutations in PRRT2 result in paroxysmal dyskinesias with marked
RT variability in clinical expression.";
RL J. Med. Genet. 49:79-82(2012).
RN [12]
RP GENE FAMILY.
RX PubMed=22363774; DOI=10.1371/journal.pone.0031961;
RA Sallman Almen M., Bringeland N., Fredriksson R., Schioth H.B.;
RT "The dispanins: a novel gene family of ancient origin that contains 14
RT human members.";
RL PLoS ONE 7:E31961-E31961(2012).
RN [13]
RP SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT EKD1 CYS-308.
RX PubMed=27172900; DOI=10.18632/oncotarget.9258;
RA Liu Y.T., Nian F.S., Chou W.J., Tai C.Y., Kwan S.Y., Chen C., Kuo P.W.,
RA Lin P.H., Chen C.Y., Huang C.W., Lee Y.C., Soong B.W., Tsai J.W.;
RT "PRRT2 mutations lead to neuronal dysfunction and neurodevelopmental
RT defects.";
RL Oncotarget 7:39184-39196(2016).
RN [14]
RP VARIANT EKD1 TRP-266.
RX PubMed=22120146; DOI=10.1093/brain/awr289;
RA Wang J.L., Cao L., Li X.H., Hu Z.M., Li J.D., Zhang J.G., Liang Y., San A.,
RA Li N., Chen S.Q., Guo J.F., Jiang H., Shen L., Zheng L., Mao X., Yan W.Q.,
RA Zhou Y., Shi Y.T., Ai S.X., Dai M.Z., Zhang P., Xia K., Chen S.D.,
RA Tang B.S.;
RT "Identification of PRRT2 as the causative gene of paroxysmal kinesigenic
RT dyskinesias.";
RL Brain 134:3493-3501(2011).
RN [15]
RP VARIANT BFIS2 GLU-323.
RX PubMed=22623405; DOI=10.1002/humu.22126;
RA Schubert J., Paravidino R., Becker F., Berger A., Bebek N., Bianchi A.,
RA Brockmann K., Capovilla G., Bernardina B.D., Fukuyama Y., Hoffmann G.F.,
RA Jurkat-Rott K., Antonnen A.K., Kurlemann G., Lehesjoki A.E.,
RA Lehmann-Horn F., Mastrangelo M., Mause U., Muller S., Neubauer B., Pust B.,
RA Rating D., Robbiano A., Ruf S., Schroeder C., Seidel A., Specchio N.,
RA Stephani U., Striano P., Teichler J., Turkdogan D., Vigevano F., Viri M.,
RA Bauer P., Zara F., Lerche H., Weber Y.G.;
RT "PRRT2 Mutations are the major cause of benign familial infantile
RT seizures.";
RL Hum. Mutat. 33:1439-1443(2012).
RN [16]
RP VARIANTS EKD1 ARG-281; THR-287 AND CYS-308.
RX PubMed=22131361; DOI=10.1136/jmedgenet-2011-100635;
RA Li J., Zhu X., Wang X., Sun W., Feng B., Du T., Sun B., Niu F., Wei H.,
RA Wu X., Dong L., Li L., Cai X., Wang Y., Liu Y.;
RT "Targeted genomic sequencing identifies PRRT2 mutations as a cause of
RT paroxysmal kinesigenic choreoathetosis.";
RL J. Med. Genet. 49:76-78(2012).
CC -!- FUNCTION: As a component of the outer core of AMPAR complex, may be
CC involved in synaptic transmission in the central nervous system. In
CC hippocampal neurons, in presynaptic terminals, plays an important role
CC in the final steps of neurotransmitter release, possibly by regulating
CC Ca(2+)-sensing. In the cerebellum, may inhibit SNARE complex formation
CC and down-regulate short-term facilitation.
CC {ECO:0000250|UniProtKB:E9PUL5}.
CC -!- SUBUNIT: Component of the outer core of AMPAR complex
CC (PubMed:25915028). AMPAR complex consists of an inner core made of 4
CC pore-forming GluA/GRIA proteins (GRIA1, GRIA2, GRIA3 and GRIA4) and 4
CC major auxiliary subunits arranged in a twofold symmetry. One of the two
CC pairs of distinct binding sites is occupied either by CNIH2, CNIH3 or
CC CACNG2, CACNG3. The other harbors CACNG2, CACNG3, CACNG4, CACNG8 or
CC GSG1L. This inner core of AMPAR complex is complemented by outer core
CC constituents binding directly to the GluA/GRIA proteins at sites
CC distinct from the interaction sites of the inner core constituents.
CC Outer core constituents include at least PRRT1, PRRT2, CKAMP44/SHISA9,
CC FRRS1L and NRN1. The proteins of the inner and outer core serve as a
CC platform for other, more peripherally associated AMPAR constituents.
CC Alone or in combination, these auxiliary subunits control the gating
CC and pharmacology of the AMPAR complex and profoundly impact their
CC biogenesis and protein processing (By similarity). Interacts with
CC intersectin 1/ITSN1 (By similarity). Interacts with SNARE complex
CC components, including SNAP25, STX1A, SYT1 and SYT2; this interaction
CC may inhibit SNARE complex formation (PubMed:25915028, PubMed:22832103).
CC {ECO:0000250|UniProtKB:E9PUL5, ECO:0000269|PubMed:22832103,
CC ECO:0000269|PubMed:25915028}.
CC -!- INTERACTION:
CC Q7Z6L0; Q13520: AQP6; NbExp=3; IntAct=EBI-722696, EBI-13059134;
CC Q7Z6L0; Q9NZD1: GPRC5D; NbExp=3; IntAct=EBI-722696, EBI-13067820;
CC Q7Z6L0; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-722696, EBI-373355;
CC Q7Z6L0; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-722696, EBI-18159983;
CC Q7Z6L0; Q71RC9: SMIM5; NbExp=3; IntAct=EBI-722696, EBI-12334905;
CC Q7Z6L0; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-722696, EBI-12947623;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22101681,
CC ECO:0000269|PubMed:25915028, ECO:0000269|PubMed:27172900}; Single-pass
CC membrane protein {ECO:0000250|UniProtKB:E9PUL5}. Presynaptic cell
CC membrane {ECO:0000250|UniProtKB:E9PUL5}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:E9PUL5}. Synapse {ECO:0000250|UniProtKB:E9PUL5}.
CC Cell projection, axon {ECO:0000269|PubMed:22832103}. Cytoplasmic
CC vesicle, secretory vesicle, synaptic vesicle membrane
CC {ECO:0000250|UniProtKB:D3ZFB6}. Postsynaptic density membrane
CC {ECO:0000250|UniProtKB:D3ZFB6}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:D3ZFB6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7Z6L0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z6L0-2; Sequence=VSP_028815;
CC Name=3;
CC IsoId=Q7Z6L0-3; Sequence=VSP_028814;
CC -!- DISEASE: Episodic kinesigenic dyskinesia 1 (EKD1) [MIM:128200]: An
CC autosomal dominant neurologic condition characterized by recurrent and
CC brief attacks of abnormal involuntary movements, triggered by sudden
CC voluntary movement. These attacks usually have onset during childhood
CC or early adulthood and can involve dystonic postures, chorea, or
CC athetosis. {ECO:0000269|PubMed:22101681, ECO:0000269|PubMed:22120146,
CC ECO:0000269|PubMed:22131361, ECO:0000269|PubMed:22209761,
CC ECO:0000269|PubMed:25915028, ECO:0000269|PubMed:27172900}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry. Disease-causing mutations that produce truncation of the C-
CC terminus of the protein alter subcellular location, from plasma
CC membrane to cytoplasm (PubMed:22101681). {ECO:0000269|PubMed:22101681}.
CC -!- DISEASE: Convulsions, familial infantile, with paroxysmal
CC choreoathetosis (ICCA) [MIM:602066]: A syndrome characterized by
CC clinical features of benign familial infantile seizures and episodic
CC kinesigenic dyskinesia. Benign familial infantile seizures is a
CC disorder characterized by afebrile seizures occurring during the first
CC year of life, without neurologic sequelae. Paroxysmal choreoathetosis
CC is a disorder of involuntary movements characterized by attacks that
CC occur spontaneously or are induced by a variety of stimuli.
CC {ECO:0000269|PubMed:22243967, ECO:0000269|PubMed:22832103}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Seizures, benign familial infantile, 2 (BFIS2) [MIM:605751]: A
CC form of benign familial infantile epilepsy, a neurologic disorder
CC characterized by afebrile seizures occurring in clusters during the
CC first year of life, without neurologic sequelae. BFIS2 inheritance is
CC autosomal dominant. {ECO:0000269|PubMed:22243967,
CC ECO:0000269|PubMed:22399141, ECO:0000269|PubMed:22623405}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the CD225/Dispanin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Proline-rich transmembrane protein 2 (PRRT2);
CC Note=Leiden Open Variation Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/PRRT2";
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DR EMBL; AK092265; BAC03843.1; -; mRNA.
DR EMBL; AK074572; BAC11067.1; -; mRNA.
DR EMBL; AK292393; BAF85082.1; -; mRNA.
DR EMBL; AL834185; CAD38881.1; -; mRNA.
DR EMBL; CH471238; EAW79991.1; -; Genomic_DNA.
DR EMBL; BC011405; AAH11405.1; -; mRNA.
DR EMBL; BC053594; AAH53594.1; -; mRNA.
DR CCDS; CCDS10654.1; -. [Q7Z6L0-1]
DR CCDS; CCDS58445.1; -. [Q7Z6L0-2]
DR CCDS; CCDS58446.1; -. [Q7Z6L0-3]
DR RefSeq; NP_001243371.1; NM_001256442.1. [Q7Z6L0-2]
DR RefSeq; NP_001243372.1; NM_001256443.1. [Q7Z6L0-3]
DR RefSeq; NP_660282.2; NM_145239.2. [Q7Z6L0-1]
DR RefSeq; XP_011544017.1; XM_011545715.2. [Q7Z6L0-2]
DR RefSeq; XP_011544018.1; XM_011545716.2.
DR RefSeq; XP_016878377.1; XM_017022888.1. [Q7Z6L0-1]
DR AlphaFoldDB; Q7Z6L0; -.
DR BioGRID; 125188; 22.
DR IntAct; Q7Z6L0; 15.
DR MINT; Q7Z6L0; -.
DR STRING; 9606.ENSP00000456226; -.
DR TCDB; 8.A.58.2.1; the dispanin (dispanin) family.
DR iPTMnet; Q7Z6L0; -.
DR PhosphoSitePlus; Q7Z6L0; -.
DR BioMuta; PRRT2; -.
DR DMDM; 74738828; -.
DR MassIVE; Q7Z6L0; -.
DR PaxDb; Q7Z6L0; -.
DR PeptideAtlas; Q7Z6L0; -.
DR PRIDE; Q7Z6L0; -.
DR ProteomicsDB; 69436; -. [Q7Z6L0-1]
DR ProteomicsDB; 69437; -. [Q7Z6L0-2]
DR ProteomicsDB; 69438; -. [Q7Z6L0-3]
DR Antibodypedia; 3043; 108 antibodies from 22 providers.
DR DNASU; 112476; -.
DR Ensembl; ENST00000300797.7; ENSP00000300797.6; ENSG00000167371.21. [Q7Z6L0-3]
DR Ensembl; ENST00000358758.12; ENSP00000351608.7; ENSG00000167371.21. [Q7Z6L0-1]
DR Ensembl; ENST00000567659.3; ENSP00000456226.1; ENSG00000167371.21. [Q7Z6L0-2]
DR Ensembl; ENST00000572820.2; ENSP00000458291.2; ENSG00000167371.21. [Q7Z6L0-1]
DR Ensembl; ENST00000636131.1; ENSP00000490390.1; ENSG00000167371.21. [Q7Z6L0-3]
DR Ensembl; ENST00000637064.1; ENSP00000490826.1; ENSG00000167371.21. [Q7Z6L0-1]
DR Ensembl; ENST00000647876.1; ENSP00000498021.1; ENSG00000167371.21. [Q7Z6L0-3]
DR GeneID; 112476; -.
DR KEGG; hsa:112476; -.
DR MANE-Select; ENST00000358758.12; ENSP00000351608.7; NM_145239.3; NP_660282.2.
DR UCSC; uc002dud.4; human. [Q7Z6L0-1]
DR CTD; 112476; -.
DR DisGeNET; 112476; -.
DR GeneCards; PRRT2; -.
DR GeneReviews; PRRT2; -.
DR HGNC; HGNC:30500; PRRT2.
DR HPA; ENSG00000167371; Tissue enhanced (ovary).
DR MalaCards; PRRT2; -.
DR MIM; 128200; phenotype.
DR MIM; 602066; phenotype.
DR MIM; 605751; phenotype.
DR MIM; 614386; gene.
DR neXtProt; NX_Q7Z6L0; -.
DR OpenTargets; ENSG00000167371; -.
DR Orphanet; 306; Benign familial infantile epilepsy.
DR Orphanet; 569; Familial or sporadic hemiplegic migraine.
DR Orphanet; 31709; Infantile convulsions and choreoathetosis.
DR Orphanet; 98811; Paroxysmal exertion-induced dyskinesia.
DR Orphanet; 98809; Paroxysmal kinesigenic dyskinesia.
DR Orphanet; 98810; Paroxysmal non-kinesigenic dyskinesia.
DR PharmGKB; PA142671132; -.
DR VEuPathDB; HostDB:ENSG00000167371; -.
DR eggNOG; ENOG502S2U1; Eukaryota.
DR GeneTree; ENSGT00940000161103; -.
DR HOGENOM; CLU_070349_0_0_1; -.
DR InParanoid; Q7Z6L0; -.
DR OMA; DPQPDCQ; -.
DR OrthoDB; 1101977at2759; -.
DR PhylomeDB; Q7Z6L0; -.
DR TreeFam; TF331357; -.
DR PathwayCommons; Q7Z6L0; -.
DR SignaLink; Q7Z6L0; -.
DR BioGRID-ORCS; 112476; 12 hits in 1072 CRISPR screens.
DR ChiTaRS; PRRT2; human.
DR GeneWiki; PRRT2; -.
DR GenomeRNAi; 112476; -.
DR Pharos; Q7Z6L0; Tbio.
DR PRO; PR:Q7Z6L0; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q7Z6L0; protein.
DR Bgee; ENSG00000167371; Expressed in right hemisphere of cerebellum and 139 other tissues.
DR ExpressionAtlas; Q7Z6L0; baseline and differential.
DR Genevisible; Q7Z6L0; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR GO; GO:0017075; F:syntaxin-1 binding; ISS:UniProtKB.
DR GO; GO:0099502; P:calcium-dependent activation of synaptic vesicle fusion; IEA:Ensembl.
DR GO; GO:1905513; P:negative regulation of short-term synaptic potentiation; ISS:UniProtKB.
DR GO; GO:0035544; P:negative regulation of SNARE complex assembly; ISS:UniProtKB.
DR GO; GO:0050884; P:neuromuscular process controlling posture; IMP:MGI.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; ISS:UniProtKB.
DR InterPro; IPR007593; CD225/Dispanin_fam.
DR Pfam; PF04505; CD225; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cytoplasmic vesicle;
KW Disease variant; Dystonia; Epilepsy; Membrane; Methylation; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Synapse; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..340
FT /note="Proline-rich transmembrane protein 2"
FT /id="PRO_0000307745"
FT TOPO_DOM 1..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5, ECO:0000255"
FT INTRAMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5, ECO:0000255"
FT TOPO_DOM 290..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5, ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5, ECO:0000255"
FT TOPO_DOM 339..340
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5, ECO:0000255"
FT REGION 1..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..161
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5"
FT MOD_RES 74
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZFB6"
FT MOD_RES 240
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PUL5"
FT VAR_SEQ 294..340
FT /note="SRNSLQQGDVDGAQRLGRVAKLLSIVALVGGVLIIIASCVINLGVYK -> V
FT SPMGP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028814"
FT VAR_SEQ 337
FT /note="G -> GGEWGLGTGRGGMEGLARAALLTPAPALSCLSSLPLLCLSLSPPPPV
FT CPSLSSPT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:16303743"
FT /id="VSP_028815"
FT VARIANT 138
FT /note="P -> A (in dbSNP:rs79182085)"
FT /evidence="ECO:0000269|PubMed:22101681"
FT /id="VAR_067010"
FT VARIANT 147
FT /note="D -> H (in dbSNP:rs79568162)"
FT /evidence="ECO:0000269|PubMed:22101681"
FT /id="VAR_067011"
FT VARIANT 214
FT /note="A -> P (in dbSNP:rs745594874)"
FT /evidence="ECO:0000269|PubMed:22101681"
FT /id="VAR_067012"
FT VARIANT 215
FT /note="P -> R (in dbSNP:rs200926711)"
FT /evidence="ECO:0000269|PubMed:22243967"
FT /id="VAR_067320"
FT VARIANT 216
FT /note="P -> L (in dbSNP:rs76335820)"
FT /evidence="ECO:0000269|PubMed:22243967"
FT /id="VAR_067321"
FT VARIANT 237
FT /note="G -> R (in dbSNP:rs199556853)"
FT /evidence="ECO:0000269|PubMed:22101681"
FT /id="VAR_067013"
FT VARIANT 240..340
FT /note="Missing (in ICCA; may be produced at very low levels
FT due to a premature stop codon in the mRNA, that could lead
FT to nonsense-mediated mRNA decay; dbSNP:rs387907126)"
FT /evidence="ECO:0000269|PubMed:22832103"
FT /id="VAR_080269"
FT VARIANT 245
FT /note="R -> H (in dbSNP:rs754897123)"
FT /evidence="ECO:0000269|PubMed:22101681"
FT /id="VAR_067014"
FT VARIANT 266
FT /note="R -> W (in EKD1; dbSNP:rs387907128)"
FT /evidence="ECO:0000269|PubMed:22120146"
FT /id="VAR_067322"
FT VARIANT 281
FT /note="W -> R (in EKD1)"
FT /evidence="ECO:0000269|PubMed:22131361"
FT /id="VAR_067323"
FT VARIANT 287
FT /note="A -> T (in EKD1; may affect subcellular location,
FT becoming predominantly cytoplasmic; impairs interaction
FT with GRIA1 and SNAP25)"
FT /evidence="ECO:0000269|PubMed:22131361,
FT ECO:0000269|PubMed:25915028"
FT /id="VAR_067324"
FT VARIANT 305
FT /note="G -> R (in EKD1; dbSNP:rs767799831)"
FT /evidence="ECO:0000269|PubMed:22209761"
FT /id="VAR_067325"
FT VARIANT 308
FT /note="R -> C (in EKD1; no effect on location at the plasma
FT membrane; dbSNP:rs932713001)"
FT /evidence="ECO:0000269|PubMed:22131361,
FT ECO:0000269|PubMed:27172900"
FT /id="VAR_067326"
FT VARIANT 317
FT /note="S -> N (in ICCA; dbSNP:rs387907125)"
FT /evidence="ECO:0000269|PubMed:22243967"
FT /id="VAR_067327"
FT VARIANT 323
FT /note="G -> E (in BFIS2)"
FT /evidence="ECO:0000269|PubMed:22623405"
FT /id="VAR_068426"
FT CONFLICT 151
FT /note="T -> S (in Ref. 5; AAH11405)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="A -> AP (in Ref. 3; CAD38881)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="S -> P (in Ref. 3; CAD38881)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 340 AA; 34945 MW; F4BBA6559F081E34 CRC64;
MAASSSEISE MKGVEESPKV PGEGPGHSEA ETGPPQVLAG VPDQPEAPQP GPNTTAAPVD
SGPKAGLAPE TTETPAGASE TAQATDLSLS PGGESKANCS PEDPCQETVS KPEVSKEATA
DQGSRLESAA PPEPAPEPAP QPDPRPDSQP TPKPALQPEL PTQEDPTPEI LSESVGEKQE
NGAVVPLQAG DGEEGPAPEP HSPPSKKSPP ANGAPPRVLQ QLVEEDRMRR AHSGHPGSPR
GSLSRHPSSQ LAGPGVEGGE GTQKPRDYII LAILSCFCPM WPVNIVAFAY AVMSRNSLQQ
GDVDGAQRLG RVAKLLSIVA LVGGVLIIIA SCVINLGVYK
