PRRT3_HUMAN
ID PRRT3_HUMAN Reviewed; 981 AA.
AC Q5FWE3; Q49AD0; Q6UXY6; Q8NBC9;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 3.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Proline-rich transmembrane protein 3;
DE Flags: Precursor;
GN Name=PRRT3; ORFNames=UNQ5823/PRO19642;
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 3).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain, and Chondrosarcoma;
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 1-667 (ISOFORM 1), AND VARIANTS
RP PRO-213; PHE-233 AND GLY-334.
RC TISSUE=Brain;
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 [4]
RP PROTEIN SEQUENCE OF 28-42.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-815, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [6]
RP GLYCOSYLATION AT SER-329 AND THR-363, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=23234360; DOI=10.1021/pr300963h;
RA Halim A., Ruetschi U., Larson G., Nilsson J.;
RT "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT of human cerebrospinal fluid glycoproteins.";
RL J. Proteome Res. 12:573-584(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5FWE3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5FWE3-2; Sequence=VSP_020845;
CC Name=3;
CC IsoId=Q5FWE3-3; Sequence=VSP_020846, VSP_020847;
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; AY358158; AAQ88525.1; -; mRNA.
DR EMBL; BC040508; AAH40508.1; -; mRNA.
DR EMBL; BC089447; AAH89447.1; -; mRNA.
DR EMBL; BC111555; AAI11556.1; -; mRNA.
DR EMBL; AK090993; BAC03564.1; -; mRNA.
DR CCDS; CCDS43049.1; -. [Q5FWE3-1]
DR CCDS; CCDS82732.1; -. [Q5FWE3-3]
DR RefSeq; NP_001305800.1; NM_001318871.1. [Q5FWE3-3]
DR RefSeq; NP_997234.3; NM_207351.4. [Q5FWE3-1]
DR RefSeq; XP_011531930.1; XM_011533628.2. [Q5FWE3-1]
DR RefSeq; XP_011531931.1; XM_011533629.2. [Q5FWE3-1]
DR RefSeq; XP_016861745.1; XM_017006256.1.
DR AlphaFoldDB; Q5FWE3; -.
DR BioGRID; 130093; 10.
DR IntAct; Q5FWE3; 1.
DR STRING; 9606.ENSP00000392511; -.
DR CarbonylDB; Q5FWE3; -.
DR GlyConnect; 724; 1 O-Linked glycan (1 site).
DR GlyGen; Q5FWE3; 4 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q5FWE3; -.
DR PhosphoSitePlus; Q5FWE3; -.
DR BioMuta; PRRT3; -.
DR DMDM; 160332300; -.
DR jPOST; Q5FWE3; -.
DR MassIVE; Q5FWE3; -.
DR PaxDb; Q5FWE3; -.
DR PeptideAtlas; Q5FWE3; -.
DR PRIDE; Q5FWE3; -.
DR ProteomicsDB; 62807; -. [Q5FWE3-1]
DR ProteomicsDB; 62808; -. [Q5FWE3-2]
DR ProteomicsDB; 62809; -. [Q5FWE3-3]
DR Antibodypedia; 25871; 28 antibodies from 11 providers.
DR DNASU; 285368; -.
DR Ensembl; ENST00000295984.7; ENSP00000295984.3; ENSG00000163704.12. [Q5FWE3-1]
DR Ensembl; ENST00000411976.2; ENSP00000404512.2; ENSG00000163704.12. [Q5FWE3-3]
DR Ensembl; ENST00000412055.6; ENSP00000392511.1; ENSG00000163704.12. [Q5FWE3-1]
DR GeneID; 285368; -.
DR KEGG; hsa:285368; -.
DR MANE-Select; ENST00000412055.6; ENSP00000392511.1; NM_207351.5; NP_997234.3.
DR UCSC; uc003bul.2; human. [Q5FWE3-1]
DR CTD; 285368; -.
DR GeneCards; PRRT3; -.
DR HGNC; HGNC:26591; PRRT3.
DR HPA; ENSG00000163704; Group enriched (brain, fallopian tube, parathyroid gland, pituitary gland).
DR neXtProt; NX_Q5FWE3; -.
DR OpenTargets; ENSG00000163704; -.
DR PharmGKB; PA142671133; -.
DR VEuPathDB; HostDB:ENSG00000163704; -.
DR eggNOG; ENOG502QSMJ; Eukaryota.
DR GeneTree; ENSGT00730000111360; -.
DR HOGENOM; CLU_304190_0_0_1; -.
DR InParanoid; Q5FWE3; -.
DR OMA; NCYARPS; -.
DR OrthoDB; 441294at2759; -.
DR PhylomeDB; Q5FWE3; -.
DR TreeFam; TF333410; -.
DR PathwayCommons; Q5FWE3; -.
DR SignaLink; Q5FWE3; -.
DR BioGRID-ORCS; 285368; 7 hits in 1069 CRISPR screens.
DR GenomeRNAi; 285368; -.
DR Pharos; Q5FWE3; Tdark.
DR PRO; PR:Q5FWE3; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q5FWE3; protein.
DR Bgee; ENSG00000163704; Expressed in oviduct epithelium and 112 other tissues.
DR Genevisible; Q5FWE3; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR043242; PRRT3.
DR PANTHER; PTHR47400; PTHR47400; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Glycoprotein; Membrane;
KW Methylation; Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 28..981
FT /note="Proline-rich transmembrane protein 3"
FT /id="PRO_0000251978"
FT TOPO_DOM 28..474
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 496..501
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 502..522
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 523..542
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 543..563
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 564..570
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 571..591
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 592..598
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 599..619
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 620..638
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 639..659
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 660..679
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 680..700
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 701..981
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 43..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..302
FT /note="O-glycosylated at one site"
FT REGION 759..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PE13"
FT MOD_RES 780
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6PE13"
FT MOD_RES 789
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PE13"
FT MOD_RES 798
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PE13"
FT MOD_RES 808
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PE13"
FT MOD_RES 815
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 854
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PE13"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PE13"
FT MOD_RES 902
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PE13"
FT MOD_RES 903
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PE13"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PE13"
FT CARBOHYD 329
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:23234360"
FT CARBOHYD 363
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:23234360"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..384
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020845"
FT VAR_SEQ 391..421
FT /note="DEAEEWPGRPQSHPPAPPVQAPSTSRRGLIR -> GESMAGVWGEGVLCLVT
FT ENLCWGCMGAEGGE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_020846"
FT VAR_SEQ 422..981
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_020847"
FT VARIANT 138
FT /note="Q -> E (in dbSNP:rs279601)"
FT /id="VAR_027745"
FT VARIANT 213
FT /note="S -> P (in dbSNP:rs55847610)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_061695"
FT VARIANT 233
FT /note="L -> F (in dbSNP:rs55847233)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_061696"
FT VARIANT 334
FT /note="R -> G (in dbSNP:rs59465469)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_061697"
FT VARIANT 860
FT /note="L -> I (in dbSNP:rs2279794)"
FT /id="VAR_027746"
FT CONFLICT 410
FT /note="Q -> K (in Ref. 2; AAH40508)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="A -> T (in Ref. 2; AAH40508)"
FT /evidence="ECO:0000305"
FT CONFLICT 819
FT /note="A -> T (in Ref. 2; AAH40508)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 981 AA; 102197 MW; 19632A8EA8CCEA1F CRC64;
MASSPWGCVC GLLLLLLPLL GTGPALGRGF PRPLENSEIP MIPGAHPKGS VGSEPQAFDV
FPENPRADSH RNSDVRHAPA EEMPEKPVAS PLGPALYGPK AAQGAQRERL PVTDDLQMAQ
GPSSHGWTGP LDSQELLQQE AVAPHPVGHP HLTFIPTTPR RQLRVATVPP SLQHEGQEGQ
WPPRDEGLKA KTKSRVPPTS PSDHQGPPHT LVSHSGTVKR PVLEGQGGFE EHLQEAAQGP
HFTQQDPAAP DVGSVPPVEV VYSQEPGAQP DLALARSLPP AEELPVETPK RAGAEVSWEV
SSPGPPPKQA DLPDAKDSPG PQPTDPPASE APDRPSKPER AAMNGADPIS PQRVRGAVEA
PGTPKSLIPG PSDPGPAVNR TESPMGALQP DEAEEWPGRP QSHPPAPPVQ APSTSRRGLI
RVTTQRALGQ PPPPEPTASS MASAPASSPP ANATAPPLRW GPLRRVLSFS WELHVYGVGV
LFLLPALLAL AALAAAPAGP RLALVAAVLV LVASALRSAY MLTDPYGSQA RLGVRGGLVL
YNLPFPLLLT ALAALTLLGL GAGLPPPLQN PLLLGAVALV HGVGLLATDL LSTWSVLNLL
TQGLSCAWGA AVALGTLCLC RRRLLDGPRG WDASPGPRLL AVAGALGLLA SGLQLAAALW
LYPGPGRVGR FSWAWWGVHF WLRLLELTWA LALALAAVAA ARPRPPTEHA CWAKLMRLAC
PAPSGKSEVP ERPNNCYAGP SNVGAGSLDI SKSLIRNPAE SGQLATPSSG AWGSAASLGR
GPQGGPGLSR NGVGPAPSLS ELDLRPPSPI NLSRSIDAAL FREHLVRDSV FQRCGLRGLA
SPPPGGALRP RRGSHPKAEL DDAGSSLLRG RCRSLSDVRV RGPVPQHVVE APDGAAAAAS
GSSLDSFSRG SLKISWNPWR HGLSSVDSLP LDELPSTVQL LPAPTPAPDS TAARQGDGQG
EVQPRGKPGE SRSASSDTIE L
