PITM3_HUMAN
ID PITM3_HUMAN Reviewed; 974 AA.
AC Q9BZ71; A1A5D0; F8WEW5; Q59GH9; Q9NPQ4;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Membrane-associated phosphatidylinositol transfer protein 3;
DE AltName: Full=Phosphatidylinositol transfer protein, membrane-associated 3;
DE Short=PITPnm 3;
DE AltName: Full=Pyk2 N-terminal domain-interacting receptor 1;
DE Short=NIR-1;
GN Name=PITPNM3; Synonyms=NIR1;
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 [MRNA] (ISOFORM 1), INTERACTION WITH PTK2B,
RP CALCIUM-BINDING, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10022914; DOI=10.1128/mcb.19.3.2278;
RA Lev S., Hernandez J., Martinez R., Chen A., Plowman G., Schlessinger J.;
RT "Identification of a novel family of targets of PYK2 related to Drosophila
RT retinal degeneration B (rdgB) protein.";
RL Mol. Cell. Biol. 19:2278-2288(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-954 (ISOFORM 3), AND VARIANT THR-80.
RC TISSUE=Hippocampus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-954 (ISOFORM 1), AND VARIANT
RP THR-80.
RG The European IMAGE consortium;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-31 AND SER-928, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; SER-612; SER-907 AND
RP SER-946, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343 AND SER-928, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP VARIANT CORD5 HIS-626.
RX PubMed=17377520; DOI=10.1038/sj.ejhg.5201817;
RA Koehn L., Kadzhaev K., Burstedt M.S., Haraldsson S., Hallberg B.,
RA Sandgren O., Golovleva I.;
RT "Mutation in the PYK2-binding domain of PITPNM3 causes autosomal dominant
RT cone dystrophy (CORD5) in two Swedish families.";
RL Eur. J. Hum. Genet. 15:664-671(2007).
CC -!- FUNCTION: Catalyzes the transfer of phosphatidylinositol and
CC phosphatidylcholine between membranes (in vitro) (By similarity). Binds
CC calcium ions. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PTK2B via its C-terminus.
CC {ECO:0000269|PubMed:10022914}.
CC -!- INTERACTION:
CC Q9BZ71; P55774: CCL18; NbExp=4; IntAct=EBI-2815766, EBI-711240;
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BZ71-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BZ71-2; Sequence=VSP_017965;
CC Name=3;
CC IsoId=Q9BZ71-3; Sequence=VSP_046060;
CC -!- TISSUE SPECIFICITY: Detected in brain and spleen, and at low levels in
CC ovary. {ECO:0000269|PubMed:10022914}.
CC -!- DISEASE: Cone-rod dystrophy 5 (CORD5) [MIM:600977]: An inherited
CC retinal dystrophy characterized by retinal pigment deposits visible on
CC fundus examination, predominantly in the macular region, and initial
CC loss of cone photoreceptors followed by rod degeneration. This leads to
CC decreased visual acuity and sensitivity in the central visual field,
CC followed by loss of peripheral vision. Severe loss of vision occurs
CC earlier than in retinitis pigmentosa, due to cone photoreceptors
CC degenerating at a higher rate than rod photoreceptors.
CC {ECO:0000269|PubMed:17377520}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI transfer
CC class IIA subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92367.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF334586; AAK01446.1; -; mRNA.
DR EMBL; AB209130; BAD92367.1; ALT_INIT; mRNA.
DR EMBL; AC055872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC035799; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC128584; AAI28585.1; -; mRNA.
DR EMBL; AL389994; CAB97544.1; -; mRNA.
DR CCDS; CCDS11076.1; -. [Q9BZ71-1]
DR CCDS; CCDS54080.1; -. [Q9BZ71-3]
DR RefSeq; NP_112497.2; NM_031220.3. [Q9BZ71-1]
DR AlphaFoldDB; Q9BZ71; -.
DR BioGRID; 123636; 12.
DR ELM; Q9BZ71; -.
DR IntAct; Q9BZ71; 8.
DR MINT; Q9BZ71; -.
DR STRING; 9606.ENSP00000262483; -.
DR iPTMnet; Q9BZ71; -.
DR PhosphoSitePlus; Q9BZ71; -.
DR BioMuta; PITPNM3; -.
DR DMDM; 93140544; -.
DR EPD; Q9BZ71; -.
DR jPOST; Q9BZ71; -.
DR MassIVE; Q9BZ71; -.
DR MaxQB; Q9BZ71; -.
DR PaxDb; Q9BZ71; -.
DR PeptideAtlas; Q9BZ71; -.
DR PRIDE; Q9BZ71; -.
DR ProteomicsDB; 31981; -.
DR ProteomicsDB; 79771; -. [Q9BZ71-1]
DR ProteomicsDB; 79772; -. [Q9BZ71-2]
DR Antibodypedia; 23792; 119 antibodies from 27 providers.
DR DNASU; 83394; -.
DR Ensembl; ENST00000262483.13; ENSP00000262483.8; ENSG00000091622.16. [Q9BZ71-1]
DR Ensembl; ENST00000421306.7; ENSP00000407882.3; ENSG00000091622.16. [Q9BZ71-3]
DR GeneID; 83394; -.
DR KEGG; hsa:83394; -.
DR MANE-Select; ENST00000262483.13; ENSP00000262483.8; NM_031220.4; NP_112497.2.
DR UCSC; uc002gdd.5; human. [Q9BZ71-1]
DR CTD; 83394; -.
DR DisGeNET; 83394; -.
DR GeneCards; PITPNM3; -.
DR HGNC; HGNC:21043; PITPNM3.
DR HPA; ENSG00000091622; Tissue enhanced (lymphoid).
DR MalaCards; PITPNM3; -.
DR MIM; 600977; phenotype.
DR MIM; 608921; gene.
DR neXtProt; NX_Q9BZ71; -.
DR OpenTargets; ENSG00000091622; -.
DR Orphanet; 1872; Cone rod dystrophy.
DR PharmGKB; PA134971883; -.
DR VEuPathDB; HostDB:ENSG00000091622; -.
DR eggNOG; KOG3668; Eukaryota.
DR GeneTree; ENSGT00940000153849; -.
DR HOGENOM; CLU_007179_1_0_1; -.
DR InParanoid; Q9BZ71; -.
DR OMA; KKYQSQC; -.
DR OrthoDB; 122895at2759; -.
DR PhylomeDB; Q9BZ71; -.
DR TreeFam; TF312967; -.
DR PathwayCommons; Q9BZ71; -.
DR Reactome; R-HSA-1483226; Synthesis of PI.
DR SignaLink; Q9BZ71; -.
DR BioGRID-ORCS; 83394; 8 hits in 1072 CRISPR screens.
DR GenomeRNAi; 83394; -.
DR Pharos; Q9BZ71; Tbio.
DR PRO; PR:Q9BZ71; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9BZ71; protein.
DR Bgee; ENSG00000091622; Expressed in pancreatic ductal cell and 159 other tissues.
DR ExpressionAtlas; Q9BZ71; baseline and differential.
DR Genevisible; Q9BZ71; HS.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0042995; C:cell projection; IEA:Ensembl.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; TAS:Reactome.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IMP:UniProtKB.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR004177; DDHD_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR031315; LNS2/PITP.
DR Pfam; PF02862; DDHD; 1.
DR SMART; SM01127; DDHD; 1.
DR SMART; SM00775; LNS2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR PROSITE; PS51043; DDHD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cone-rod dystrophy; Disease variant;
KW Lipid-binding; Membrane; Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..974
FT /note="Membrane-associated phosphatidylinositol transfer
FT protein 3"
FT /id="PRO_0000232743"
FT DOMAIN 390..594
FT /note="DDHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00378"
FT REGION 284..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..959
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHE1"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHE1"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHE1"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHE1"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 907
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 928
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 946
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..409
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_017965"
FT VAR_SEQ 40..75
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046060"
FT VARIANT 17
FT /note="P -> S (in dbSNP:rs28493751)"
FT /id="VAR_062132"
FT VARIANT 80
FT /note="A -> T (in dbSNP:rs3809835)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.5"
FT /id="VAR_026014"
FT VARIANT 626
FT /note="Q -> H (in CORD5; dbSNP:rs76024428)"
FT /evidence="ECO:0000269|PubMed:17377520"
FT /id="VAR_046787"
FT CONFLICT 885
FT /note="A -> V (in Ref. 1; AAK01446)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 974 AA; 106781 MW; C4A653710140895E CRC64;
MAKAGRAGGP PPGGGAPWHL RNVLSDSVES SDDEFFDARE EMAEGKNAIL IGMSQWNSND
LVEQIETMGK LDEHQGEGTA PCTSSILQEK QRELYRVSLR RQRFPAQGSI EIHEDSEEGC
PQRSCKTHVL LLVLHGGNIL DTGAGDPSCK AADIHTFSSV LEKVTRAHFP AALGHILIKF
VPCPAICSEA FSLVSHLNPY SHDEGCLSSS QDHVPLAALP LLAISSPQYQ DAVATVIERA
NQVYREFLKS SDGIGFSGQV CLIGDCVGGL LAFDAICYSA GPSGDSPASS SRKGSISSTQ
DTPVAVEEDC SLASSKRLSK SNIDISSGLE DEEPKRPLPR KQSDSSTYDC EAITQHHAFL
SSIHSSVLKD ESETPAAGGP QLPEVSLGRF DFDVSDFFLF GSPLGLVLAM RRTVLPGLDG
FQVRPACSQV YSFFHCADPS ASRLEPLLEP KFHLVPPVSV PRYQRFPLGD GQSLLLADAL
HTHSPLFLEG SSRDSPPLLD APASPPQASR FQRPGRRMSE GSSHSESSES SDSMAPVGAS
RITAKWWGSK RIDYALYCPD VLTAFPTVAL PHLFHASYWE STDVVAFILR QVMRYESVNI
KESARLDPAA LSPANPREKW LRKRTQVKLR NVTANHRAND VIAAEDGPQV LVGRFMYGPL
DMVALTGEKV DILVMAEPSS GRWVHLDTEI TNSSGRITYN VPRPRRLGVG VYPVKMVVRG
DQTCAMSYLT VLPRGMECVV FSIDGSFAAS VSIMGSDPKV RPGAVDVVRH WQDLGYMILY
ITGRPDMQKQ RVVSWLSQHN FPQGMIFFSD GLVHDPLRQK AIFLRNLMQE CFIKISAAYG
STKDISVYSV LGLPASQIFI VGRPTKKYQT QCQFLSEGYA AHLAALEASH RSRPKKNNSR
MILRKGSFGL HAQPEFLRKR NHLRRTMSVQ QPDPPAANPK PERAQSQPES DKDHERPLPA
LSWARGPPKF ESVP
