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 24-JAN-2024, entry version 151. 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 form of paroxysmal kinesigenic dyskinesia, a CC neurologic condition characterized by recurrent and brief attacks of CC abnormal involuntary movements, triggered by sudden voluntary movement. CC These attacks usually have onset during childhood or early adulthood CC and can involve dystonic postures, chorea, or athetosis. CC {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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 23. DR IntAct; Q7Z6L0; 16. 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; 9606-ENSP00000456226; -. DR PeptideAtlas; Q7Z6L0; -. DR ProteomicsDB; 69436; -. [Q7Z6L0-1] DR ProteomicsDB; 69437; -. [Q7Z6L0-2] DR ProteomicsDB; 69438; -. [Q7Z6L0-3] DR Antibodypedia; 3043; 123 antibodies from 23 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 AGR; HGNC:30500; -. DR CTD; 112476; -. DR DisGeNET; 112476; -. DR GeneCards; PRRT2; -. DR GeneReviews; PRRT2; -. DR HGNC; HGNC:30500; PRRT2. DR HPA; ENSG00000167371; Tissue enhanced (brain). 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; 4641723at2759; -. DR PhylomeDB; Q7Z6L0; -. DR TreeFam; TF331357; -. DR PathwayCommons; Q7Z6L0; -. DR SignaLink; Q7Z6L0; -. DR BioGRID-ORCS; 112476; 12 hits in 1148 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 140 other cell types or tissues. DR ExpressionAtlas; Q7Z6L0; baseline and differential. 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: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: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:0150037; P:regulation of calcium-dependent activation of synaptic vesicle fusion; IEA:Ensembl. DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; ISS:UniProtKB. DR InterPro; IPR007593; CD225/Dispanin_fam. DR PANTHER; PTHR14948; NG5; 1. DR PANTHER; PTHR14948:SF20; PROLINE-RICH TRANSMEMBRANE PROTEIN 2; 1. DR Pfam; PF04505; CD225; 1. DR Genevisible; Q7Z6L0; HS. 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 //