LOCUS       NP_001008370            1242 aa            linear   ROD 02-JUN-2024
DEFINITION  membrane-associated phosphatidylinositol transfer protein 1 [Rattus
            norvegicus].
ACCESSION   NP_001008370 XP_341978
VERSION     NP_001008370.1
DBSOURCE    REFSEQ: accession NM_001008369.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 1242)
  AUTHORS   Garner,K., Hunt,A.N., Koster,G., Somerharju,P., Groves,E., Li,M.,
            Raghu,P., Holic,R. and Cockcroft,S.
  TITLE     Phosphatidylinositol transfer protein, cytoplasmic 1 (PITPNC1)
            binds and transfers phosphatidic acid
  JOURNAL   J Biol Chem 287 (38), 32263-32276 (2012)
   PUBMED   22822086
REFERENCE   2  (residues 1 to 1242)
  AUTHORS   Lev,S., Hernandez,J., Martinez,R., Chen,A., Plowman,G. and
            Schlessinger,J.
  TITLE     Identification of a novel family of targets of PYK2 related to
            Drosophila retinal degeneration B (rdgB) protein
  JOURNAL   Mol Cell Biol 19 (3), 2278-2288 (1999)
   PUBMED   10022914
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC085945.1.
            
            On Dec 16, 2004 this sequence version replaced XP_341978.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC085945.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132263, SAMD00132265
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1242
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="1"
                     /map="1q43"
     Protein         1..1242
                     /product="membrane-associated phosphatidylinositol
                     transfer protein 1"
                     /note="NIR-2; pyk2 N-terminal domain-interacting receptor
                     2; PITPnm 1; phosphatidylinositol membrane-associated"
                     /calculated_mol_wt=134854
     Region          1..257
                     /region_name="SRPBCC_PITPNM1-2_like"
                     /note="Lipid-binding SRPBCC domain of mammalian PITPNM1-2
                     and related proteins (Class IIA PITPs); cd08889"
                     /db_xref="CDD:176898"
     Site            order(21..22,25,29,32,40,59,61,63,65,68,70,73,77,81..82,
                     84,86,88,90,95,97,99,102..103,109,111,191,197,199,209,
                     217..219,222)
                     /site_type="other"
                     /note="putative lipid binding site [chemical binding]"
                     /db_xref="CDD:176898"
     Site            59
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O00562; propagated from
                     UniProtKB/Swiss-Prot (Q5U2N3.1)"
     Site            65..83
                     /site_type="active"
                     /note="putative lipid exchange loop [active]"
                     /db_xref="CDD:176898"
     Site            order(118..147,153..177,185..186)
                     /site_type="active"
                     /note="putatative regulatory loop [active]"
                     /db_xref="CDD:176898"
     Site            164
                     /site_type="other"
                     /note="putative PKC phosphorylation site
                     [posttranslational modification]"
                     /db_xref="CDD:176898"
     Region          259..330
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2N3.1)"
     Site            282
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O35954; propagated from
                     UniProtKB/Swiss-Prot (Q5U2N3.1)"
     Site            287
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2N3.1)"
     Site            300
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2N3.1)"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2N3.1)"
     Site            319
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35954; propagated from
                     UniProtKB/Swiss-Prot (Q5U2N3.1)"
     Site            326
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35954; propagated from
                     UniProtKB/Swiss-Prot (Q5U2N3.1)"
     Site            329
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O35954; propagated from
                     UniProtKB/Swiss-Prot (Q5U2N3.1)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2N3.1)"
     Site            345
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2N3.1)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2N3.1)"
     Site            373
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2N3.1)"
     Site            382
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CDK1.
                     /evidence=ECO:0000250|UniProtKB:O00562; propagated from
                     UniProtKB/Swiss-Prot (Q5U2N3.1)"
     Region          581..678
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2N3.1)"
     Site            593
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2N3.1)"
     Site            600
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2N3.1)"
     Site            621
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (Q5U2N3.1)"
     Region          684..877
                     /region_name="DDHD"
                     /note="DDHD domain; pfam02862"
                     /db_xref="CDD:460725"
     Site            894
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00562; propagated from
                     UniProtKB/Swiss-Prot (Q5U2N3.1)"
     Region          1021..1152
                     /region_name="LNS2"
                     /note="This domain is found in Saccharomyces cerevisiae
                     protein SMP2, proteins with an N-terminal lipin domain and
                     phosphatidylinositol transfer proteins; smart00775"
                     /db_xref="CDD:197870"
     Region          1207..1242
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5U2N3.1)"
     Site            1209
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:O35954; propagated from
                     UniProtKB/Swiss-Prot (Q5U2N3.1)"
     Site            1235
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00562; propagated from
                     UniProtKB/Swiss-Prot (Q5U2N3.1)"
     CDS             1..1242
                     /gene="Pitpnm1"
                     /gene_synonym="Pitpnm"
                     /coded_by="NM_001008369.1:193..3921"
                     /db_xref="GeneID:361694"
                     /db_xref="RGD:1306710"
ORIGIN      
        1 mlikeyhill pmsldeyqva qlymiqkksr eessgegsgv eilanrpytd gpggngqyth
       61 kvyhvgship gwfrallpka alqveeeswn aypytrtryt cpfvekfsie ietyylpdgg
      121 qqpnvfnlsg aerrqrildt idivrdavap geykaeedpr lyrsvktgrg pladdwarta
      181 aqtgplmcay klckvefryw gmqakieqfi hdvglrrvml rahrqawcwq dewielsmad
      241 iraleeetar mlaqrmakcn tgsegpeaqt pgkpstetqp gtrtagtpdg peappgpdas
      301 pdasfgkqws sssrssyssq hgggvspqsl sewrmqniar dsensseeef fdahegfsds
      361 devfpkemtk wnsndfidaf asptevegvp dpaimatkgi edearaprds egldgtgdlg
      421 veacsvhalf lilhsgsild sgpgdtnskq advqtlstaf eavtrvhfpe alghvalrlv
      481 pcppicaaay alvsnlspys hdgdslsrsq dhiplaalpl latsssryqg avatviartn
      541 qayaaflrss egtgfcgqvv ligdgvggil gfdalchsas agtgsrgssr rgsmnnemls
      601 pevgpvrdpl adgvevlgra spepsalpaq rtssdmanpd pdgsqnslqv aptvtsgepr
      661 rastascppa sseapdgptn aarldfkvsg fflfgsplgl vlalrktvmp alevaqmrpa
      721 ceqiynlfha adpcasrlep llapkfqaia plavpryqkf plgdgsslll adtlqthssl
      781 fleelemmvp stptsasgaf wkgnelgnep aaqpaapstt sevvkildrw wgnkridysl
      841 ycpealtafp tvtlphlfha sywesadvva filrqvieke rpqlteceep siyspafpre
      901 kwqrkrtqvk irnvtsnhra sdtvvcegrp qvlngrfmyg pldvvtltge kvdvyvmtqp
      961 lsgkwihfgt evtnssgrlt fpvpseralg igvypvrmvv rgdhtyaecc ltvvsrgtea
     1021 vvfsidgsft asvsimgsdp kvragavdvv rhwqdsgyli vyvtgrpdmq khrvvawlsq
     1081 hnfphgvvsf cdglthdplr qkamflqslv qevelnivag ygspkdvavy aalglspsqt
     1141 yivgravrkl qaqcqflsdg yvahlgqlea gshshapsgp praalakssy avaapvdflr
     1201 kqsqllrsrg psqvdlegpg tppttlargk trsislklds ee
//
