PITM3_MOUSE
ID PITM3_MOUSE Reviewed; 974 AA.
AC Q3UHE1; A6QRE8; Q3UH22; Q5RIT9;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 119.
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 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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-31; SER-109; SER-295;
RP SER-298; SER-495 AND SER-928, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 -!- FUNCTION: Catalyzes the transfer of phosphatidylinositol and
CC phosphatidylcholine between membranes (in vitro). Binds calcium ions
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PTK2B via its C-terminus. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UHE1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UHE1-2; Sequence=VSP_017966;
CC -!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI transfer
CC class IIA subfamily. {ECO:0000305}.
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DR EMBL; AK147444; BAE27916.1; -; mRNA.
DR EMBL; AK147630; BAE28035.1; -; mRNA.
DR EMBL; BX119911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS24978.1; -. [Q3UHE1-1]
DR CCDS; CCDS36213.1; -. [Q3UHE1-2]
DR RefSeq; NP_001020098.1; NM_001024927.2. [Q3UHE1-1]
DR RefSeq; NP_001075110.1; NM_001081641.1. [Q3UHE1-2]
DR AlphaFoldDB; Q3UHE1; -.
DR STRING; 10090.ENSMUSP00000074737; -.
DR iPTMnet; Q3UHE1; -.
DR PhosphoSitePlus; Q3UHE1; -.
DR SwissPalm; Q3UHE1; -.
DR MaxQB; Q3UHE1; -.
DR PaxDb; Q3UHE1; -.
DR PeptideAtlas; Q3UHE1; -.
DR PRIDE; Q3UHE1; -.
DR ProteomicsDB; 289580; -. [Q3UHE1-1]
DR ProteomicsDB; 289581; -. [Q3UHE1-2]
DR Antibodypedia; 23792; 119 antibodies from 27 providers.
DR Ensembl; ENSMUST00000075258; ENSMUSP00000074737; ENSMUSG00000040543. [Q3UHE1-1]
DR Ensembl; ENSMUST00000108508; ENSMUSP00000104148; ENSMUSG00000040543. [Q3UHE1-2]
DR GeneID; 327958; -.
DR KEGG; mmu:327958; -.
DR UCSC; uc007jya.1; mouse. [Q3UHE1-1]
DR UCSC; uc007jyb.1; mouse. [Q3UHE1-2]
DR CTD; 83394; -.
DR MGI; MGI:2685726; Pitpnm3.
DR VEuPathDB; HostDB:ENSMUSG00000040543; -.
DR eggNOG; KOG3668; Eukaryota.
DR GeneTree; ENSGT00940000153849; -.
DR HOGENOM; CLU_007179_1_0_1; -.
DR InParanoid; Q3UHE1; -.
DR OMA; KKYQSQC; -.
DR OrthoDB; 122895at2759; -.
DR PhylomeDB; Q3UHE1; -.
DR TreeFam; TF312967; -.
DR Reactome; R-MMU-1483226; Synthesis of PI.
DR BioGRID-ORCS; 327958; 10 hits in 76 CRISPR screens.
DR ChiTaRS; Pitpnm3; mouse.
DR PRO; PR:Q3UHE1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q3UHE1; protein.
DR Bgee; ENSMUSG00000040543; Expressed in retinal neural layer and 142 other tissues.
DR Genevisible; Q3UHE1; MM.
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:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:MGI.
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; Lipid-binding; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..974
FT /note="Membrane-associated phosphatidylinositol transfer
FT protein 3"
FT /id="PRO_0000232744"
FT DOMAIN 390..594
FT /note="DDHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00378"
FT REGION 310..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..535
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:21183079"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ71"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ71"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ71"
FT MOD_RES 907
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ71"
FT MOD_RES 928
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 946
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZ71"
FT VAR_SEQ 77..92
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017966"
FT CONFLICT 849
FT /note="S -> N (in Ref. 1; BAE27916)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 974 AA; 106462 MW; 285A581AFDE92626 CRC64;
MAKAGSAGGP SPGGGAPWHL RNVLSDSVES SDDEFFDARE EVAEGKNAIL IGMSQWSSND
LVEQIETIGK LDERQGDGAT ACTSSILQEK QRELYRVSLR RQRFPAQGSI EIHEDGEEGC
SQRSCKTHVL LLVLHGGNVL DTGSGDPSCK AADIHTFSSV LEKVMRAHFP AALGHILIKF
VPCPAICSEA FSLVSNLNPY SHDEGCLGTS QDHVPLAALP LLAISSPQYQ DAVATVIERA
NHIYGEFLKS SDGIGFNGQV CLIGDCVGGL LAFDAICYSA GPSGDSPGSS SRKGSISSTQ
DTPVVVEEDC SLASSKRLSK SNVDVSSGVE DEDPKRPLPR KQSDSSTYDC EAITQHHAFL
SSIHSSVLKD EAEAPAAGTP QLSEVSLGRF DFDVSDFFLF GSPLGLVLAM RRTVLPGIDG
FQMRPACSQV YSFFHCADPS ASRLEPLLEP KFHLVPPVSV PRYQRFPLGD GQSLLLADAL
HTHSPLFLEG SSRGSPPLLD APASPPQAPR FQRTERRLSK GSSHSDSSES SDSLAPMGAS
RITAKWWGTK RIDYALYCPD VLTAFPTVAL PHLFHASYWE STDVVAFILR QVMRYESASV
KESTGLDPTA LSPANPREKW LRKRTQVKLR NVTANHRAND VIAAEDGPQV LVGRFMYGPL
DMVALTGEKV DILVMTEPSS GRWVHLDTEI TNNSGRITYN VPRPRRLGVG VYPVKMVVRG
DQTCAMSYLT VLPRGMECVV FSIDGSFAAS VSIMGSDPKV RPGAVDVVRH WQDLGYMILY
ITGRPDMQKQ RVVSWLSQHN FPQGMIFFSD GLVHDPLRQK AIFLRNLMQE CFIKITAAYG
STKDISVYSV LGLPASQIFI VGRSTKKYQT QCQFLSEGYA AHLAALEASH RSRPKKNNSR
MILRKGSFGL HAQPEFLRKR NHLRRTMSVQ QPDPPAANPK PERAQSQPES DKDHERPLPA
LSWARGPPKF ESVP
