PRRT1_HUMAN
ID PRRT1_HUMAN Reviewed; 306 AA.
AC Q99946; A6ND08; A6ND40; B0S869; Q5SSW4; Q5SSX7; Q5STI1; Q96DW3; Q96NQ8;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Proline-rich transmembrane protein 1;
DE AltName: Full=Dispanin subfamily D member 1;
DE Short=DSPD1;
DE AltName: Full=Synapse differentiation-induced protein 4 {ECO:0000250|UniProtKB:O35449};
DE Short=SynDIG4 {ECO:0000250|UniProtKB:O35449};
GN Name=PRRT1 {ECO:0000312|HGNC:HGNC:13943};
GN Synonyms=C6orf31 {ECO:0000312|HGNC:HGNC:13943},
GN NG5 {ECO:0000250|UniProtKB:Q6MG82};
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] (ISOFORM 1).
RC TISSUE=Cerebellum;
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 GENOMIC DNA].
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
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] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Skin;
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 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 [7]
RP VARIANT [LARGE SCALE ANALYSIS] THR-94.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Required to maintain a pool of extrasynaptic AMPA-regulated
CC glutamate receptors (AMPAR) which is necessary for synapse development
CC and function. Regulates basal AMPAR function and synaptic transmission
CC during development but is dispensable at mature hippocampal synapses.
CC Plays a role in regulating basal phosphorylation levels of glutamate
CC receptor GRIA1 and promotes GRIA1 and GRIA2 cell surface expression.
CC {ECO:0000250|UniProtKB:O35449}.
CC -!- SUBUNIT: Component of the outer core of AMPAR complex. AMPAR complex
CC consists of an inner core made of 4 pore-forming GluA/GRIA proteins
CC (GRIA1, GRIA2, GRIA3 and GRIA4) and 4 major auxiliary subunits arranged
CC in a twofold symmetry. One of the two pairs of distinct binding sites
CC is occupied either by CNIH2, CNIH3 or CACNG2, CACNG3. The other harbors
CC CACNG2, CACNG3, CACNG4, CACNG8 or GSG1L. This inner core of AMPAR
CC complex is complemented by outer core constituents binding directly to
CC the GluA/GRIA proteins at sites distinct from the interaction sites of
CC the inner core constituents. Outer core constituents include at least
CC PRRT1, PRRT2, CKAMP44/SHISA9, FRRS1L and NRN1. The proteins of the
CC inner and outer core serve as a platform for other, more peripherally
CC associated AMPAR constituents. Alone or in combination, these auxiliary
CC subunits control the gating and pharmacology of the AMPAR complex and
CC profoundly impact their biogenesis and protein processing (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q99946-2; P21145: MAL; NbExp=3; IntAct=EBI-12211089, EBI-3932027;
CC Q99946-2; Q99946-2: PRRT1; NbExp=3; IntAct=EBI-12211089, EBI-12211089;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6MG82};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6MG82}.
CC Synapse {ECO:0000250|UniProtKB:Q6MG82}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99946-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99946-2; Sequence=VSP_003808;
CC -!- SIMILARITY: Belongs to the CD225/Dispanin family. {ECO:0000305}.
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DR EMBL; AK054885; BAB70821.1; -; mRNA.
DR EMBL; U89336; AAB47496.1; -; Genomic_DNA.
DR EMBL; AL662828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL845464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX284686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX927239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR753803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR933878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR812478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03589.1; -; Genomic_DNA.
DR EMBL; BC013201; AAH13201.1; -; mRNA.
DR EMBL; BC063046; AAH63046.1; -; mRNA.
DR CCDS; CCDS4739.1; -. [Q99946-1]
DR CCDS; CCDS87385.1; -. [Q99946-2]
DR RefSeq; NP_085154.3; NM_030651.3. [Q99946-1]
DR AlphaFoldDB; Q99946; -.
DR BioGRID; 123335; 8.
DR IntAct; Q99946; 1.
DR STRING; 9606.ENSP00000211413; -.
DR PhosphoSitePlus; Q99946; -.
DR BioMuta; PRRT1; -.
DR DMDM; 23821870; -.
DR MassIVE; Q99946; -.
DR PaxDb; Q99946; -.
DR PeptideAtlas; Q99946; -.
DR PRIDE; Q99946; -.
DR ProteomicsDB; 78536; -. [Q99946-1]
DR ProteomicsDB; 78537; -. [Q99946-2]
DR ABCD; Q99946; 1 sequenced antibody.
DR Antibodypedia; 61533; 90 antibodies from 18 providers.
DR DNASU; 80863; -.
DR Ensembl; ENST00000211413.10; ENSP00000211413.5; ENSG00000204314.12. [Q99946-1]
DR Ensembl; ENST00000375150.6; ENSP00000364292.2; ENSG00000204314.12. [Q99946-2]
DR Ensembl; ENST00000383309.6; ENSP00000372799.2; ENSG00000206331.11. [Q99946-2]
DR Ensembl; ENST00000414687.6; ENSP00000414711.2; ENSG00000235956.9. [Q99946-1]
DR Ensembl; ENST00000418753.5; ENSP00000411544.1; ENSG00000225141.9. [Q99946-2]
DR Ensembl; ENST00000419655.6; ENSP00000396427.2; ENSG00000229071.9. [Q99946-1]
DR Ensembl; ENST00000423671.5; ENSP00000411183.1; ENSG00000229071.9. [Q99946-2]
DR Ensembl; ENST00000425739.5; ENSP00000416064.1; ENSG00000229488.9. [Q99946-2]
DR Ensembl; ENST00000441129.5; ENSP00000411596.1; ENSG00000227122.9. [Q99946-2]
DR Ensembl; ENST00000444466.6; ENSP00000405389.2; ENSG00000225141.9. [Q99946-1]
DR Ensembl; ENST00000445122.5; ENSP00000396426.1; ENSG00000238056.9. [Q99946-2]
DR Ensembl; ENST00000451329.6; ENSP00000398756.2; ENSG00000238056.9. [Q99946-1]
DR Ensembl; ENST00000452030.5; ENSP00000394808.1; ENSG00000235956.9. [Q99946-2]
DR Ensembl; ENST00000454112.6; ENSP00000389058.2; ENSG00000206331.11. [Q99946-1]
DR Ensembl; ENST00000456814.6; ENSP00000397896.2; ENSG00000229488.9. [Q99946-1]
DR Ensembl; ENST00000458719.6; ENSP00000398252.2; ENSG00000227122.9. [Q99946-1]
DR GeneID; 80863; -.
DR KEGG; hsa:80863; -.
DR MANE-Select; ENST00000211413.10; ENSP00000211413.5; NM_030651.4; NP_085154.3.
DR UCSC; uc003nzt.4; human. [Q99946-1]
DR CTD; 80863; -.
DR DisGeNET; 80863; -.
DR GeneCards; PRRT1; -.
DR HGNC; HGNC:13943; PRRT1.
DR HPA; ENSG00000204314; Group enriched (brain, ovary).
DR MIM; 618297; gene.
DR neXtProt; NX_Q99946; -.
DR OpenTargets; ENSG00000204314; -.
DR PharmGKB; PA25932; -.
DR VEuPathDB; HostDB:ENSG00000204314; -.
DR eggNOG; ENOG502QWCK; Eukaryota.
DR GeneTree; ENSGT00940000162382; -.
DR HOGENOM; CLU_096299_0_0_1; -.
DR InParanoid; Q99946; -.
DR OMA; CHLSPYP; -.
DR PhylomeDB; Q99946; -.
DR TreeFam; TF331357; -.
DR PathwayCommons; Q99946; -.
DR SignaLink; Q99946; -.
DR BioGRID-ORCS; 80863; 6 hits in 1069 CRISPR screens.
DR ChiTaRS; PRRT1; human.
DR GenomeRNAi; 80863; -.
DR Pharos; Q99946; Tbio.
DR PRO; PR:Q99946; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q99946; protein.
DR Bgee; ENSG00000204314; Expressed in right hemisphere of cerebellum and 91 other tissues.
DR ExpressionAtlas; Q99946; baseline and differential.
DR Genevisible; Q99946; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:Ensembl.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030545; F:signaling receptor regulator activity; IEA:Ensembl.
DR GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR GO; GO:0060292; P:long-term synaptic depression; ISS:UniProtKB.
DR GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
DR GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; ISS:UniProtKB.
DR GO; GO:0050808; P:synapse organization; IEA:Ensembl.
DR InterPro; IPR007593; CD225/Dispanin_fam.
DR Pfam; PF04505; CD225; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Membrane; Reference proteome;
KW Signal-anchor; Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..306
FT /note="Proline-rich transmembrane protein 1"
FT /id="PRO_0000135697"
FT TOPO_DOM 1..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q6MG82"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..275
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q6MG82"
FT INTRAMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..306
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q6MG82"
FT REGION 1..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..37
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..106
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..140
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..113
FT /note="MSSEKSGLPDSVPHTSPPPYNAPQPPAEPPAPPPQAAPSSHHHHHHHYHQSG
FT TATLPRLGAGGLASSAATAQRGPSSSATLPRPPHHAPPGPAAGAPPPGCATLPRMPPDP
FT YL -> MPGTQTPAPAEDPHSGCRDPVPARPQACHPKS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_003808"
FT VARIANT 94
FT /note="A -> T (in a breast cancer sample; somatic mutation;
FT dbSNP:rs1427187570)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036212"
FT CONFLICT 20
FT /note="Y -> F (in Ref. 1; BAB70821)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="H -> Y (in Ref. 1; BAB70821)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 306 AA; 31430 MW; 4D3037FAF8EA516A CRC64;
MSSEKSGLPD SVPHTSPPPY NAPQPPAEPP APPPQAAPSS HHHHHHHYHQ SGTATLPRLG
AGGLASSAAT AQRGPSSSAT LPRPPHHAPP GPAAGAPPPG CATLPRMPPD PYLQETRFEG
PLPPPPPAAA APPPPAPAQT AQAPGFVVPT HAGTVGTLPL GGYVAPGYPL QLQPCTAYVP
VYPVGTPYAG GTPGGTGVTS TLPPPPQGPG LALLEPRRPP HDYMPIAVLT TICCFWPTGI
IAIFKAVQVR TALARGDMVS AEIASREARN FSFISLAVGI AAMVLCTILT VVIIIAAQHH
ENYWDP
