PCX3_HUMAN
ID PCX3_HUMAN Reviewed; 2034 AA.
AC Q9H6A9; Q6MZN8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Pecanex-like protein 3;
DE AltName: Full=Pecanex homolog protein 3 {ECO:0000312|HGNC:HGNC:18760};
GN Name=PCNX3 {ECO:0000312|HGNC:HGNC:18760}; Synonyms=PCNXL3;
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).
RC TISSUE=Esophageal carcinoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 107-2034 (ISOFORM 2), AND VARIANT
RP ARG-258.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-370, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129; THR-370; SER-392;
RP SER-505; SER-1025; SER-1697; SER-1909 AND SER-1955, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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).
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=Q9H6A9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H6A9-2; Sequence=VSP_033242, VSP_033243;
CC Name=3;
CC IsoId=Q9H6A9-3; Sequence=VSP_033244, VSP_033245;
CC -!- SIMILARITY: Belongs to the pecanex family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15353.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX640978; CAE45990.2; -; mRNA.
DR EMBL; AP001362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK026080; BAB15353.1; ALT_INIT; mRNA.
DR CCDS; CCDS44650.1; -. [Q9H6A9-1]
DR RefSeq; NP_115599.2; NM_032223.3. [Q9H6A9-1]
DR AlphaFoldDB; Q9H6A9; -.
DR BioGRID; 134447; 77.
DR IntAct; Q9H6A9; 27.
DR MINT; Q9H6A9; -.
DR STRING; 9606.ENSP00000347931; -.
DR GlyGen; Q9H6A9; 2 sites.
DR iPTMnet; Q9H6A9; -.
DR PhosphoSitePlus; Q9H6A9; -.
DR SwissPalm; Q9H6A9; -.
DR BioMuta; PCNX3; -.
DR DMDM; 187471100; -.
DR EPD; Q9H6A9; -.
DR jPOST; Q9H6A9; -.
DR MassIVE; Q9H6A9; -.
DR MaxQB; Q9H6A9; -.
DR PaxDb; Q9H6A9; -.
DR PeptideAtlas; Q9H6A9; -.
DR PRIDE; Q9H6A9; -.
DR ProteomicsDB; 80969; -. [Q9H6A9-1]
DR ProteomicsDB; 80970; -. [Q9H6A9-2]
DR ProteomicsDB; 80971; -. [Q9H6A9-3]
DR Antibodypedia; 7459; 14 antibodies from 9 providers.
DR DNASU; 399909; -.
DR Ensembl; ENST00000355703.4; ENSP00000347931.3; ENSG00000197136.5. [Q9H6A9-1]
DR GeneID; 399909; -.
DR KEGG; hsa:399909; -.
DR MANE-Select; ENST00000355703.4; ENSP00000347931.3; NM_032223.4; NP_115599.2.
DR UCSC; uc001oey.3; human. [Q9H6A9-1]
DR CTD; 399909; -.
DR DisGeNET; 399909; -.
DR GeneCards; PCNX3; -.
DR HGNC; HGNC:18760; PCNX3.
DR HPA; ENSG00000197136; Low tissue specificity.
DR MIM; 617657; gene.
DR neXtProt; NX_Q9H6A9; -.
DR OpenTargets; ENSG00000197136; -.
DR PharmGKB; PA38680; -.
DR VEuPathDB; HostDB:ENSG00000197136; -.
DR eggNOG; KOG3604; Eukaryota.
DR GeneTree; ENSGT00940000158735; -.
DR HOGENOM; CLU_000602_0_1_1; -.
DR InParanoid; Q9H6A9; -.
DR OMA; QSWPHHP; -.
DR OrthoDB; 63639at2759; -.
DR PhylomeDB; Q9H6A9; -.
DR TreeFam; TF313570; -.
DR PathwayCommons; Q9H6A9; -.
DR SignaLink; Q9H6A9; -.
DR BioGRID-ORCS; 399909; 103 hits in 1067 CRISPR screens.
DR ChiTaRS; PCNX3; human.
DR GenomeRNAi; 399909; -.
DR Pharos; Q9H6A9; Tdark.
DR PRO; PR:Q9H6A9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9H6A9; protein.
DR Bgee; ENSG00000197136; Expressed in granulocyte and 93 other tissues.
DR Genevisible; Q9H6A9; HS.
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..2034
FT /note="Pecanex-like protein 3"
FT /id="PRO_0000331529"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 790..812
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..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1844..2034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1844..1866
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..1989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VI59"
FT MOD_RES 129
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 370
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VI59"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1025
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1697
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1909
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1955
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
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 1..1113
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_033244"
FT VAR_SEQ 927..982
FT /note="LMYLLEQIDMHGFGGTAATSPLTAVFSLSRSLLAAALLYGFCLGAIKTPWPE
FT QHVP -> PRPRSPPEALPCLHICFALTQFGNSNCPAEVHSPDPFPTLVRVAGFSKPLS
FT GISLC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033242"
FT VAR_SEQ 983..2034
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033243"
FT VAR_SEQ 1114..1126
FT /note="VLKPLEYSQYEVR -> MWKPGAESWPLHT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_033245"
FT VARIANT 258
FT /note="Q -> R (in dbSNP:rs1151489)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_042889"
FT VARIANT 458
FT /note="S -> C (in dbSNP:rs1193851)"
FT /id="VAR_042890"
FT VARIANT 564
FT /note="G -> S (in dbSNP:rs56232198)"
FT /id="VAR_061500"
FT VARIANT 813
FT /note="K -> N (in dbSNP:rs1144790)"
FT /id="VAR_042891"
FT VARIANT 1822
FT /note="H -> Q (in dbSNP:rs7114037)"
FT /id="VAR_061501"
SQ SEQUENCE 2034 AA; 222039 MW; C11C93DDFB2DA270 CRC64;
MGSQVLQILR QGVWASLTGG WFFDPHQSTF SNCFHLYVWI FLLIFPFLLY MVLPPSLMVA
GVYCLVVAVI FATIKTVNYR LHAMFDQGEI VEKRSSTMGE LEEEPAQGDS NPPRDPGVEM
TVFRKVSSTP PVRCSSQHSV FGFNQVSELL PRMEDSGPLR DIKELVREQG SNNVIVTSAD
REMLKLSSQE KLIGDLPQTP PGAVPDPSLA STDSSEPSPL AGDGAPWSGS SMADTPMSPL
LKGSLSQELS KSFLTLTQPD RALVRTSSRR EQRRGAGGYQ PLDRRGSGEP TPQKAGSSDS
CFSGTDRETL SSFKSEKTNS THLDSPPGGP APEGSDTDPP SEAELPASPD AGVPSDDTLR
SFDTVIGAGT PPGLAEPLLV VRPKDLALLR PSKRQPPLRR HSPPGRAPRR PLLEGGGFFE
DEDTSEGSEL SPASSLRSQR RYSTDSSSST SCYSPESSRG AAGGPRKRRA PHGAEEGTAV
PPKRPYGTQR TPSTASAKTH ARVLSMDGAG GDVLRPPLAG CKAELEAQVG VEQAASEPVV
LPAEARRGPA ANQPGWRGEL QEEGAVGGAA EETGRRDRSS SVRRTQAIRR RHNAGSNPTP
PASVMGSPPS SLQEAQRGRA ASHSRALTLP SALHFASSLL LTRAGANVHE ACTFDDTSEG
AVHYFYDESG VRRSYTFGLA GGGYENPVGQ QGEQTANGAW DRHSHSSSFH SADVPEATGG
LNLLQPRPVV LQGMQVRRVP LEIPEEQTLM EEAPPRAQHS YKYWLLPGRW TSVRYERLAL
LALLDRTRGV LENIFGVGLS SLVAFLGYLL LLKGFFTDIW VFQFCLVIAS CQYSLLKSVQ
PDAASPMHGH NWVIAYSRPV YFCICCLLIW LLDALGSAQP FPPVSLYGLT LFSASFFFCA
RDVATVFTLC FPFVFLLGLL PQVNTCLMYL LEQIDMHGFG GTAATSPLTA VFSLSRSLLA
AALLYGFCLG AIKTPWPEQH VPVLFSVFCG LLVALSYHLS RQSSDPTVLW SLIRSKLFPE
LEERSLETAR AEPPDPLPDK MRQSVREVLH SDLVMCVVIA VLTFAISAST VFIALKSVLG
FVLYALAGAV GFFTHYLLPQ LRKQLPWFCL SQPVLKPLEY SQYEVRGAAQ VMWFEKLYAG
LQCVEKYLIY PAVVLNALTV DAHTVVSHPD KYCFYCRALL MTVAGLKLLR SAFCCPPQQY
LTLAFTVLLF HFDYPRLSQG FLLDYFLMSL LCSKLWDLLY KLRFVLTYIA PWQITWGSAF
HAFAQPFAVP HSAMLFVQAL LSGLFSTPLN PLLGSAVFIM SYARPLKFWE RDYNTKRVDH
SNTRLVTQLD RNPGADDNNL NSIFYEHLTR SLQHTLCGDL VLGRWGNYGP GDCFVLASDY
LNALVHLIEV GNGLVTFQLR GLEFRGTYCQ QREVEAITEG VEEDEGCCCC EPGHLPRVLS
FNAAFGQRWL AWEVTASKYV LEGYSISDNN AASMLQVFDL RKILITYYVK SIIYYVSRSP
KLEVWLSHEG ITAALRPVRV PGYADSDPTF SLSVDEDYDL RLSGLSLPSF CAVHLEWIQY
CASRRSQPVD QDWNSPLVTL CFGLCVLGRR ALGTASHSMS ASLEPFLYGL HALFKGDFRI
TSPRDEWVFA DMDLLHRVVA PGVRMALKLH QDHFTSPDEY EEPAALYDAI AANEERLVIS
HEGDPAWRSA ILSNTPSLLA LRHVLDDASD EYKIIMLNRR HLSFRVIKVN RECVRGLWAG
QQQELVFLRN RNPERGSIQN AKQALRNMIN SSCDQPLGYP IYVSPLTTSL AGSHPQLRAL
WGGPISLGAI AHWLLRTWER LHKGCGAGCN SGGNVDDSDC SGGGGLTSLS NNPPVAHPTP
ENTAGNGDQP LPPGPGWGPR SSLSGSGDGR PPPLLQWPPP RLPGPPPASP IPTEGPRTSR
PPGPGLLSSE GPSGKWSLGG RKGLGGSDGE PASGSPKGGT PKSQAPLDLS LSLSLSLSPD
VSTEASPPRA SQDIPCLDSS APESGTPMGA LGDWPAPIEE RESPAAQPLL EHQY
