PCX3_MOUSE
ID PCX3_MOUSE Reviewed; 2028 AA.
AC Q8VI59;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Pecanex-like protein 3;
DE AltName: Full=Pecanex homolog protein 3 {ECO:0000312|MGI:MGI:1861733};
GN Name=Pcnx3 {ECO:0000312|MGI:MGI:1861733}; Synonyms=Pcnxl3;
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 [MRNA] (ISOFORM 2).
RX PubMed=10894943; DOI=10.1159/000015569;
RA Saridaki A., Ferraz C., Demaille J., Scherer G., Roux A.-F.;
RT "Genomic sequencing reveals the structure of the Kcnk6 and map3k11 genes
RT and their close vicinity to the sipa1 gene on mouse chromosome 19.";
RL Cytogenet. Cell Genet. 89:85-88(2000).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127; SER-431 AND SER-521, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VI59-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VI59-2; Sequence=VSP_033246;
CC -!- SIMILARITY: Belongs to the pecanex family. {ECO:0000305}.
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DR EMBL; BC096538; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF237953; AAL62024.1; -; mRNA.
DR CCDS; CCDS29475.2; -. [Q8VI59-1]
DR RefSeq; NP_659117.2; NM_144868.3. [Q8VI59-1]
DR AlphaFoldDB; Q8VI59; -.
DR STRING; 10090.ENSMUSP00000109245; -.
DR GlyGen; Q8VI59; 3 sites.
DR iPTMnet; Q8VI59; -.
DR PhosphoSitePlus; Q8VI59; -.
DR SwissPalm; Q8VI59; -.
DR EPD; Q8VI59; -.
DR MaxQB; Q8VI59; -.
DR PaxDb; Q8VI59; -.
DR PeptideAtlas; Q8VI59; -.
DR PRIDE; Q8VI59; -.
DR ProteomicsDB; 288008; -. [Q8VI59-1]
DR ProteomicsDB; 288009; -. [Q8VI59-2]
DR Antibodypedia; 7459; 14 antibodies from 9 providers.
DR DNASU; 104401; -.
DR Ensembl; ENSMUST00000068169; ENSMUSP00000063786; ENSMUSG00000054874. [Q8VI59-2]
DR Ensembl; ENSMUST00000113615; ENSMUSP00000109245; ENSMUSG00000054874. [Q8VI59-1]
DR GeneID; 104401; -.
DR KEGG; mmu:104401; -.
DR UCSC; uc008gep.2; mouse. [Q8VI59-2]
DR UCSC; uc008geq.2; mouse. [Q8VI59-1]
DR CTD; 399909; -.
DR MGI; MGI:1861733; Pcnx3.
DR VEuPathDB; HostDB:ENSMUSG00000054874; -.
DR eggNOG; KOG3604; Eukaryota.
DR GeneTree; ENSGT00940000158735; -.
DR HOGENOM; CLU_000602_0_1_1; -.
DR InParanoid; Q8VI59; -.
DR OMA; QSWPHHP; -.
DR OrthoDB; 63639at2759; -.
DR PhylomeDB; Q8VI59; -.
DR TreeFam; TF313570; -.
DR BioGRID-ORCS; 104401; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q8VI59; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8VI59; protein.
DR Bgee; ENSMUSG00000054874; Expressed in embryonic brain and 237 other tissues.
DR ExpressionAtlas; Q8VI59; baseline and differential.
DR Genevisible; Q8VI59; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR039797; Pecanex.
DR InterPro; IPR007735; Pecanex_C.
DR PANTHER; PTHR12372; PTHR12372; 1.
DR Pfam; PF05041; Pecanex_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..2028
FT /note="Pecanex-like protein 3"
FT /id="PRO_0000215796"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 793..815
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 819..836
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 852..872
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 880..900
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 903..923
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 946..968
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 980..1000
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1053..1073
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1078..1098
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1244..1264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1280..1300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 96..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1845..2028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1892..1919
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1957..1991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 129
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6A9"
FT MOD_RES 370
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6A9"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6A9"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1025
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6A9"
FT MOD_RES 1697
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6A9"
FT MOD_RES 1909
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6A9"
FT MOD_RES 1955
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6A9"
FT CARBOHYD 95
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 1770
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 161..568
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10894943"
FT /id="VSP_033246"
SQ SEQUENCE 2028 AA; 221573 MW; B51969382FBFCA89 CRC64;
MGSQVLQILR QGVWASLTGG WFFDPHQSTF SNCFHLYVWI FLLIFPFLLY MVLPPSLMVA
GVYCLVVAVI FATIKTVNYR LHAMFDQGEI VEKRNSTMGE QEEEAAQGES SLPRDPGVEM
TVFRKVSSTP PVRCSSQHSV FGFNQVSELL PRMEDSGPLR DIKELVREQG SNNVIVTSAD
REMLKLSSQE KLIGDLPQTP PGVVPDPSLP STDSSERSPM AGDGVPWGGS GVADTPMSPL
LKGSLSQELS KSFLTLTRPD RALVRTSSRR EQCRGTGGYQ PLDRRGSGDP MPQKAGSSDS
CFSGTDRETL SSFKSEKTNS THLDSPPGGH APEGSDTDPP SEAELPASPD AGVPSDDTLR
SFDTVIGAGT PPGQTEPLLV VRPKDLALLR PSKRRPPMRG HSPPGRTPRR PLLEGSGFFE
DEDTSEGSEL SPASSLRSQR RYSTDSSSST SCYSPESSQG AAGGPRKRRA PHGAEEGTAV
PPKRPYGTQR TPSTASAKTH ARVLSMDGAG GDVLRAPLAG SKAELEAQPG MELAAGEPAV
LPPEARRGPA ANQPGWRGEL QEEGAVGGAP EETGQRECTS NVRRAQAIRR RHNAGSNPTP
PASVMGSPPS SLQEAQRGRA ASHSRALTLP SALHFASSLL LTRAGPNVHE ASNFDDTSEG
AVHYFYDESG VRRSYTFGLA GGGYENPVSQ PGEQAANGAW DRHSHSSSFH SADVPEATGG
LNLLQPRPVV LQGMQVRRVP LEIPEEQTLM EEAPPRAQHS YKYWFLPGRW TSVRYERLAL
LALLDRTRGV MENIFGVGLS SLVAFLGYLL LLKGFFTDIW VFQFCLVIAS CQYSLLKSVQ
PDAASPMHGH NWVIAYSRPV YFCICCLLIW LLDALGTAQP FPPVSLYGLT LFSASFFFCA
RDVATVFTLC FPFVFLLGLL PQVNTCLMYL LEQIDMHGFG GTAATSPLTA VFSLTRSLLA
AALLYGFCLG AIKTPWPEQH VPVLFSVFCG LLVAMSYHLS RQSSDPTVLW SLVRSKLFPE
LEERSLETAR VEPPDPLPEK MRQSVREVLH SDLVMCVVIA VLTFAVSAST VFIALKSVLG
FVLYALAGAV GFFTHYLLPQ LRKQLPWFCL SQPVLKPLEY SQYEVRGAAQ VMWFEKLYAG
LQCAEKYLIY PAVVLNALTV DAHTVVSHPD KFCLYCRALL MTVAGLKLLR SAFCCPPQQY
LTLAFTVLLF HFDYPRLSQG FLLDYFLMSL LCSKLWDLLY KLRFVLTYIA PWQITWGSAF
HAFAQPFAVP HSAMLFLQAL LSGLFSTPLN PLLGSAVFIM SYARPLKFWE RDYNTKRVDH
SNTRLVTQLD RNPGADDNNL NSIFYEHLTR SLQHTLCGDL VLGRWGNYGP GDCFVLASDY
LNALVHLIEV GNGLITFQLR GLEFRGTYCQ QREVEAITEG VEEDEGCCCC EPGHLPRVLS
FNAAFGQRWL AWEVTASKYV LEGYSISDNN AASMLQVFDL RKILVTYYVK SIIYYVSRSP
KLETWLNHEG IAAALRPVRA LGYADSDPTF SLSVDEDYDL RLSGLSLPSF CAVHLEWIQY
CASRRSQPVD QDWNSPLVTL CFGLCVLGRR ALGTASHSMS ASLEPFLYGL HALFKGDFRI
TSPRDEWVFA DMDLLHRVVA PGVRMALKLH QDHFTSPDEY EEPAALYDAI AANEERLVIS
HEGDPAWRSA ILSNTPSLLA LRHVMDDASD EYKIIMLNRR HLSFRVIKVN RECVRGLWAG
QQQELVFLRN RNPERGSIQN AKQALRNMIN SSCDQPLGYP IYVSPLTTSL AGSHPQLRAL
WGGPVSLGAI ARWLLRSWER LHKGCGAGCN SGGNVDDSDC GGGGGLTSLS NHPPLAHPTP
ENAAGSSEQP LPPGPSWGPR PSLSGSGDGR PPPLLQWPPP RLPGPPPASP APTEGPRPSR
PSGPALLNSE GPSGKWSLGG RKGLGGPDGE PASGSPKGGT PKSQAPLDLS LSPDVSSEAS
PARTTQDLPC LDSSIPEGCT PSGAPGDWPV PAEERESPAA QPLLEHQY
