PIANP_MOUSE
ID PIANP_MOUSE Reviewed; 278 AA.
AC Q6P1B3; Q3UFR0; Q71A40; Q8BHU8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=PILR alpha-associated neural protein;
DE AltName: Full=Brain protein 1;
DE AltName: Full=PILR-associating neural protein;
DE AltName: Full=Paired immunoglobin-like type 2 receptor-associating neural protein;
DE Flags: Precursor;
GN Name=Pianp; Synonyms=Panp;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, AND GLYCOSYLATION
RP AT THR-136.
RX PubMed=21241660; DOI=10.1016/j.bbrc.2011.01.047;
RA Kogure A., Shiratori I., Wang J., Lanier L.L., Arase H.;
RT "PANP is a novel O-glycosylated PILRalpha ligand expressed in neural
RT tissues.";
RL Biochem. Biophys. Res. Commun. 405:428-433(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic spinal cord;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 103-278.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Liu Z., Li Y.;
RT "The cloning of mouse brain protein 1.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [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: Acts as a ligand for PILRA in neuronal tissues, where it may
CC be involved in immune regulation. {ECO:0000269|PubMed:21241660}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in brain and spinal cord. Weak
CC expression also detected in heart, kidney, spleen and lymph node.
CC Virtually no expression detected in liver and embryo relative to brain.
CC {ECO:0000269|PubMed:21241660}.
CC -!- PTM: O-glycosylation at Thr-136 is essential for recognition by PILRA.
CC {ECO:0000269|PubMed:21241660}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ11190.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
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DR EMBL; AK082984; BAC38721.1; -; mRNA.
DR EMBL; AK148352; BAE28500.1; -; mRNA.
DR EMBL; BC065170; AAH65170.1; -; mRNA.
DR EMBL; AF540035; AAQ11190.1; ALT_SEQ; mRNA.
DR CCDS; CCDS20540.1; -.
DR RefSeq; NP_001139398.1; NM_001145926.1.
DR RefSeq; NP_001139399.1; NM_001145927.1.
DR RefSeq; NP_783627.2; NM_175696.4.
DR RefSeq; XP_006506297.1; XM_006506234.2.
DR RefSeq; XP_006506299.1; XM_006506236.2.
DR AlphaFoldDB; Q6P1B3; -.
DR SMR; Q6P1B3; -.
DR STRING; 10090.ENSMUSP00000032479; -.
DR GlyGen; Q6P1B3; 1 site.
DR iPTMnet; Q6P1B3; -.
DR PhosphoSitePlus; Q6P1B3; -.
DR MaxQB; Q6P1B3; -.
DR PaxDb; Q6P1B3; -.
DR PeptideAtlas; Q6P1B3; -.
DR PRIDE; Q6P1B3; -.
DR ProteomicsDB; 301828; -.
DR Antibodypedia; 22637; 107 antibodies from 16 providers.
DR DNASU; 319352; -.
DR Ensembl; ENSMUST00000032479; ENSMUSP00000032479; ENSMUSG00000030329.
DR Ensembl; ENSMUST00000160704; ENSMUSP00000124160; ENSMUSG00000030329.
DR Ensembl; ENSMUST00000162170; ENSMUSP00000123940; ENSMUSG00000030329.
DR GeneID; 319352; -.
DR KEGG; mmu:319352; -.
DR UCSC; uc009dst.3; mouse.
DR CTD; 196500; -.
DR MGI; MGI:2441908; Pianp.
DR VEuPathDB; HostDB:ENSMUSG00000030329; -.
DR eggNOG; ENOG502RH1H; Eukaryota.
DR GeneTree; ENSGT00510000049460; -.
DR HOGENOM; CLU_089346_0_0_1; -.
DR InParanoid; Q6P1B3; -.
DR OMA; SMRDDGN; -.
DR OrthoDB; 1234686at2759; -.
DR PhylomeDB; Q6P1B3; -.
DR TreeFam; TF336539; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR BioGRID-ORCS; 319352; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Pianp; mouse.
DR PRO; PR:Q6P1B3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q6P1B3; protein.
DR Bgee; ENSMUSG00000030329; Expressed in superior frontal gyrus and 130 other tissues.
DR ExpressionAtlas; Q6P1B3; baseline and differential.
DR Genevisible; Q6P1B3; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0050776; P:regulation of immune response; IEA:InterPro.
DR InterPro; IPR029198; AJAP1_PANP_C.
DR InterPro; IPR039628; PIANP.
DR PANTHER; PTHR32023; PTHR32023; 1.
DR Pfam; PF15298; AJAP1_PANP_C; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..278
FT /note="PILR alpha-associated neural protein"
FT /id="PRO_0000285966"
FT TOPO_DOM 28..174
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 25..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..43
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 136
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:21241660"
FT CONFLICT 29
FT /note="S -> C (in Ref. 2; BAC38721)"
FT /evidence="ECO:0000305"
FT CONFLICT 72..73
FT /note="RQ -> WK (in Ref. 2; BAC38721)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="S -> P (in Ref. 2; BAE28500)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="F -> L (in Ref. 2; BAC38721)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="Q -> K (in Ref. 2; BAC38721)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 278 AA; 29744 MW; 8F9AA85EE7E3A69B CRC64;
MWSAQLLSQL LPLWPLLLLS VLPPAQGSSH RSPPAPARPP CVRGGPSAPR HVCVWERAPP
PSRSPRVPRS RRQVVPGTAP PATPSGFEEG PPSSQYPWAI VWGPTVSRED GGDPNSVNPG
FLPLDYGFAA PHGLATPHPN SDSMRDDGDG LILGETPATL RPFLFGGRGE GVDPQLYVTI
TISIIIVLVA TGIIFKFCWD RSQKRRRPSG QQGALRQEES QQPLTDLSPA GVTVLGAFGD
SPTPTPDHEE PRGGPRPGMP QPKGAPAFQL NRIPLVNL
