PITM2_HUMAN
ID PITM2_HUMAN Reviewed; 1349 AA.
AC Q9BZ72; Q9P271;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Membrane-associated phosphatidylinositol transfer protein 2;
DE AltName: Full=Phosphatidylinositol transfer protein, membrane-associated 2;
DE Short=PITPnm 2;
DE AltName: Full=Pyk2 N-terminal domain-interacting receptor 3;
DE Short=NIR-3;
GN Name=PITPNM2; Synonyms=KIAA1457, NIR3;
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), FUNCTION, ALTERNATIVE SPLICING
RP (ISOFORMS 1 AND 3), INTERACTION WITH PTK2B, CALCIUM-BINDING, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain, and Heart;
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;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=22361696; DOI=10.1016/j.jprot.2012.01.030;
RA Stadler C., Hjelmare M., Neumann B., Jonasson K., Pepperkok R., Uhlen M.,
RA Lundberg E.;
RT "Systematic validation of antibody binding and protein subcellular
RT localization using siRNA and confocal microscopy.";
RL J. Proteomics 75:2236-2251(2012).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-644 AND SER-1277, AND
RP IDENTIFICATION BY 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).
RN [5]
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).
CC -!- FUNCTION: Catalyzes the transfer of phosphatidylinositol and
CC phosphatidylcholine between membranes (in vitro). Binds calcium ions.
CC {ECO:0000269|PubMed:10022914}.
CC -!- SUBUNIT: Interacts with PTK2B via its C-terminus (PubMed:10022914).
CC Interacts with CPNE4 (via VWFA domain) (By similarity).
CC {ECO:0000250|UniProtKB:Q6ZPQ6, ECO:0000269|PubMed:10022914}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000269|PubMed:22361696}; Peripheral membrane protein
CC {ECO:0000269|PubMed:22361696}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BZ72-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BZ72-2; Sequence=VSP_017962, VSP_017963;
CC Name=3;
CC IsoId=Q9BZ72-3; Sequence=VSP_017961;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, heart, ovary, testis and
CC thymus. Detected in small intestine, prostate, pancreas, skeletal
CC muscle, liver, colon and placenta. {ECO:0000269|PubMed:10022914}.
CC -!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI transfer
CC class IIA subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95981.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AF334585; AAK01445.1; -; mRNA.
DR EMBL; AB040890; BAA95981.2; ALT_INIT; mRNA.
DR CCDS; CCDS73543.1; -. [Q9BZ72-2]
DR CCDS; CCDS9242.1; -. [Q9BZ72-1]
DR RefSeq; NP_001287730.1; NM_001300801.1. [Q9BZ72-2]
DR RefSeq; NP_065896.1; NM_020845.2. [Q9BZ72-1]
DR AlphaFoldDB; Q9BZ72; -.
DR SMR; Q9BZ72; -.
DR BioGRID; 121653; 5.
DR ELM; Q9BZ72; -.
DR IntAct; Q9BZ72; 4.
DR STRING; 9606.ENSP00000322218; -.
DR iPTMnet; Q9BZ72; -.
DR PhosphoSitePlus; Q9BZ72; -.
DR BioMuta; PITPNM2; -.
DR DMDM; 74717733; -.
DR EPD; Q9BZ72; -.
DR jPOST; Q9BZ72; -.
DR MassIVE; Q9BZ72; -.
DR MaxQB; Q9BZ72; -.
DR PaxDb; Q9BZ72; -.
DR PeptideAtlas; Q9BZ72; -.
DR PRIDE; Q9BZ72; -.
DR ProteomicsDB; 79773; -. [Q9BZ72-1]
DR ProteomicsDB; 79774; -. [Q9BZ72-2]
DR ProteomicsDB; 79775; -. [Q9BZ72-3]
DR Antibodypedia; 1085; 71 antibodies from 13 providers.
DR DNASU; 57605; -.
DR Ensembl; ENST00000280562.9; ENSP00000280562.5; ENSG00000090975.14. [Q9BZ72-2]
DR Ensembl; ENST00000320201.10; ENSP00000322218.4; ENSG00000090975.14. [Q9BZ72-1]
DR GeneID; 57605; -.
DR KEGG; hsa:57605; -.
DR MANE-Select; ENST00000320201.10; ENSP00000322218.4; NM_020845.3; NP_065896.1.
DR UCSC; uc001uej.2; human. [Q9BZ72-1]
DR CTD; 57605; -.
DR DisGeNET; 57605; -.
DR GeneCards; PITPNM2; -.
DR HGNC; HGNC:21044; PITPNM2.
DR HPA; ENSG00000090975; Tissue enriched (lymphoid).
DR MIM; 608920; gene.
DR neXtProt; NX_Q9BZ72; -.
DR OpenTargets; ENSG00000090975; -.
DR PharmGKB; PA134963002; -.
DR VEuPathDB; HostDB:ENSG00000090975; -.
DR eggNOG; KOG3668; Eukaryota.
DR GeneTree; ENSGT00940000153849; -.
DR HOGENOM; CLU_007179_0_0_1; -.
DR InParanoid; Q9BZ72; -.
DR OMA; TPPSKIH; -.
DR OrthoDB; 122895at2759; -.
DR PhylomeDB; Q9BZ72; -.
DR TreeFam; TF312967; -.
DR PathwayCommons; Q9BZ72; -.
DR Reactome; R-HSA-1483226; Synthesis of PI.
DR SignaLink; Q9BZ72; -.
DR BioGRID-ORCS; 57605; 10 hits in 1080 CRISPR screens.
DR ChiTaRS; PITPNM2; human.
DR GenomeRNAi; 57605; -.
DR Pharos; Q9BZ72; Tbio.
DR PRO; PR:Q9BZ72; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9BZ72; protein.
DR Bgee; ENSG00000090975; Expressed in metanephros cortex and 100 other tissues.
DR ExpressionAtlas; Q9BZ72; baseline and differential.
DR Genevisible; Q9BZ72; HS.
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:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR GO; GO:0008525; F:phosphatidylcholine transporter activity; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; IDA:UniProtKB.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IMP:UniProtKB.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IDA:UniProtKB.
DR Gene3D; 3.30.530.20; -; 1.
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 InterPro; IPR001666; PI_transfer.
DR InterPro; IPR023393; START-like_dom_sf.
DR PANTHER; PTHR10658; PTHR10658; 1.
DR Pfam; PF02862; DDHD; 1.
DR Pfam; PF02121; IP_trans; 1.
DR PRINTS; PR00391; PITRANSFER.
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 Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..1349
FT /note="Membrane-associated phosphatidylinositol transfer
FT protein 2"
FT /id="PRO_0000232741"
FT DOMAIN 715..963
FT /note="DDHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00378"
FT REGION 262..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1296..1326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPQ6"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPQ6"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPQ6"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPQ6"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPQ6"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPQ6"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPQ6"
FT MOD_RES 828
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPQ6"
FT MOD_RES 1277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 50..328
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_017961"
FT VAR_SEQ 802
FT /note="A -> VETVQRNPELVLEGGPLAPLPHGDGFLETSMPVPAPTWQDGPRPGCA
FT ES (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10819331"
FT /id="VSP_017962"
FT VAR_SEQ 857..911
FT /note="KAPDALSHTPSVRRLSLLALPAPSPTTPGPHPPARKASPGLERAPGLPELDI
FT GEV -> I (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10819331"
FT /id="VSP_017963"
FT VARIANT 9
FT /note="P -> L (in dbSNP:rs17884869)"
FT /id="VAR_053584"
FT VARIANT 661
FT /note="L -> M (in dbSNP:rs55813219)"
FT /id="VAR_062131"
SQ SEQUENCE 1349 AA; 148933 MW; E9EB51FBF8E708F1 CRC64;
MIIKEYRIPL PMTVEEYRIA QLYMIQKKSR NETYGEGSGV EILENRPYTD GPGGSGQYTH
KVYHVGMHIP SWFRSILPKA ALRVVEESWN AYPYTRTRFT CPFVEKFSID IETFYKTDAG
ENPDVFNLSP VEKNQLTIDF IDIVKDPVPH NEYKTEEDPK LFQSTKTQRG PLSENWIEEY
KKQVFPIMCA YKLCKVEFRY WGMQSKIERF IHDTGLRRVM VRAHRQAWCW QDEWYGLSME
NIRELEKEAQ LMLSRKMAQF NEDGEEATEL VKHEAVSDQT SGEPPEPSSS NGEPLVGRGL
KKQWSTSSKS SRSSKRGASP SRHSISEWRM QSIARDSDES SDDEFFDAHE DLSDTEEMFP
KDITKWSSND LMDKIESPEP EDTQDGLYRQ GAPEFRVASS VEQLNIIEDE VSQPLAAPPS
KIHVLLLVLH GGTILDTGAG DPSSKKGDAN TIANVFDTVM RVHYPSALGR LAIRLVPCPP
VCSDAFALVS NLSPYSHDEG CLSSSQDHIP LAALPLLATS SPQYQEAVAT VIQRANLAYG
DFIKSQEGMT FNGQVCLIGD CVGGILAFDA LCYSNQPVSE SQSSSRRGSV VSMQDNDLLS
PGILMNAAHC CGGGGGGGGG GGSSGGGGSS GGSSLESSRH LSRSNVDIPR SNGTEDPKRQ
LPRKRSDSST YELDTIQQHQ AFLSSLHASV LRTEPCSRHS SSSTMLDGTG ALGRFDFEIT
DLFLFGCPLG LVLALRKTVI PALDVFQLRP ACQQVYNLFH PADPSASRLE PLLERRFHAL
PPFSVPRYQR YPLGDGCSTL LADVLQTHNA AFQEHGAPSS PGTAPASRGF RRASEISIAS
QVSGMAESYT ASSIAQKAPD ALSHTPSVRR LSLLALPAPS PTTPGPHPPA RKASPGLERA
PGLPELDIGE VAAKWWGQKR IDYALYCPDA LTAFPTVALP HLFHASYWES TDVVSFLLRQ
VMRHDNSSIL ELDGKEVSVF TPSKPREKWQ RKRTHVKLRN VTANHRINDA LANEDGPQVL
TGRFMYGPLD MVTLTGEKVD VHIMTQPPSG EWLYLDTLVT NNSGRVSYTI PESHRLGVGV
YPIKMVVRGD HTFADSYITV LPKGTEFVVF SIDGSFAASV SIMGSDPKVR AGAVDVVRHW
QDLGYLIIYV TGRPDMQKQR VVAWLAQHNF PHGVVSFCDG LVHDPLRHKA NFLKLLISEL
HLRVHAAYGS TKDVAVYSAI SLSPMQIYIV GRPTKKLQQQ CQFITDGYAA HLAQLKYSHR
ARPARNTATR MALRKGSFGL PGQGDFLRSR NHLLRTISAQ PSGPSHRHER TQSQADGEQR
GQRSMSVAAG CWGRAMTGRL EPGAAAGPK
