ID   CNPY2_MOUSE             Reviewed;         182 AA.
AC   Q9QXT0; Q3UBH8;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 144.
DE   RecName: Full=Protein canopy homolog 2;
DE   AltName: Full=MIR-interacting saposin-like protein;
DE   AltName: Full=Putative secreted protein ZSIG9;
DE   AltName: Full=Transmembrane protein 4;
DE   Flags: Precursor;
GN   Name=Cnpy2; Synonyms=Msap, Tmem4, Zsig9;
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].
RA   Sheppard P., Jelinek L., Whitmore T., Blumberg H., Lehner J., O'Hara P.;
RT   "Mus musculus putative secreted protein.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow, Hippocampus, Pancreas, and Pituitary;
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=129; TISSUE=Mammary tumor;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
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: Positive regulator of neurite outgrowth by stabilizing myosin
CC       regulatory light chain (MRLC). It prevents MIR-mediated MRLC
CC       ubiquitination and its subsequent proteasomal degradation (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with MYLIP/MIR. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9QXT0; Q9Z2B5: Eif2ak3; NbExp=7; IntAct=EBI-8321111, EBI-1226344;
CC       Q9QXT0; P11021: HSPA5; Xeno; NbExp=2; IntAct=EBI-8321111, EBI-354921;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-
CC       ProRule:PRU10138}.
CC   -!- SIMILARITY: Belongs to the canopy family. {ECO:0000305}.
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DR   EMBL; AF186115; AAF01433.1; -; mRNA.
DR   EMBL; AK007914; BAB25346.1; -; mRNA.
DR   EMBL; AK013014; BAB28597.1; -; mRNA.
DR   EMBL; AK013568; BAB28909.1; -; mRNA.
DR   EMBL; AK019927; BAB31921.1; -; mRNA.
DR   EMBL; AK150953; BAE29986.1; -; mRNA.
DR   EMBL; BC008261; AAH08261.1; -; mRNA.
DR   CCDS; CCDS24272.1; -.
DR   RefSeq; NP_064337.1; NM_019953.1.
DR   RefSeq; XP_006513965.1; XM_006513902.3.
DR   AlphaFoldDB; Q9QXT0; -.
DR   SMR; Q9QXT0; -.
DR   BioGRID; 208040; 4.
DR   IntAct; Q9QXT0; 4.
DR   MINT; Q9QXT0; -.
DR   STRING; 10090.ENSMUSP00000151918; -.
DR   iPTMnet; Q9QXT0; -.
DR   PhosphoSitePlus; Q9QXT0; -.
DR   SwissPalm; Q9QXT0; -.
DR   REPRODUCTION-2DPAGE; IPI00135512; -.
DR   EPD; Q9QXT0; -.
DR   jPOST; Q9QXT0; -.
DR   MaxQB; Q9QXT0; -.
DR   PaxDb; 10090-ENSMUSP00000026446; -.
DR   PeptideAtlas; Q9QXT0; -.
DR   ProteomicsDB; 283655; -.
DR   Pumba; Q9QXT0; -.
DR   TopDownProteomics; Q9QXT0; -.
DR   DNASU; 56530; -.
DR   Ensembl; ENSMUST00000026446.4; ENSMUSP00000026446.3; ENSMUSG00000025381.4.
DR   Ensembl; ENSMUST00000219037.2; ENSMUSP00000151918.2; ENSMUSG00000025381.4.
DR   GeneID; 56530; -.
DR   KEGG; mmu:56530; -.
DR   UCSC; uc007hmi.1; mouse.
DR   AGR; MGI:1928477; -.
DR   CTD; 10330; -.
DR   MGI; MGI:1928477; Cnpy2.
DR   VEuPathDB; HostDB:ENSMUSG00000025381; -.
DR   eggNOG; KOG3782; Eukaryota.
DR   GeneTree; ENSGT00940000161158; -.
DR   HOGENOM; CLU_095726_2_1_1; -.
DR   InParanoid; Q9QXT0; -.
DR   OMA; VWARRSQ; -.
DR   OrthoDB; 2878740at2759; -.
DR   PhylomeDB; Q9QXT0; -.
DR   TreeFam; TF318578; -.
DR   BioGRID-ORCS; 56530; 1 hit in 78 CRISPR screens.
DR   ChiTaRS; Cnpy2; mouse.
DR   PRO; PR:Q9QXT0; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q9QXT0; Protein.
DR   Bgee; ENSMUSG00000025381; Expressed in renal medulla collecting duct and 260 other cell types or tissues.
DR   ExpressionAtlas; Q9QXT0; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
DR   GO; GO:1905599; P:positive regulation of low-density lipoprotein receptor activity; IMP:BHF-UCL.
DR   GO; GO:0010988; P:regulation of low-density lipoprotein particle clearance; IMP:BHF-UCL.
DR   Gene3D; 1.10.225.10; Saposin-like; 1.
DR   InterPro; IPR042415; CNPY.
DR   InterPro; IPR021852; DUF3456.
DR   InterPro; IPR008139; SaposinB_dom.
DR   PANTHER; PTHR13341; MIR-INTERACTING SAPOSIN-LIKE PROTEIN; 1.
DR   PANTHER; PTHR13341:SF6; PROTEIN CANOPY HOMOLOG 2; 1.
DR   Pfam; PF11938; DUF3456; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS50015; SAP_B; 1.
DR   Genevisible; Q9QXT0; MM.
PE   1: Evidence at protein level;
KW   Disulfide bond; Endoplasmic reticulum; Phosphoprotein; Reference proteome;
KW   Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..182
FT                   /note="Protein canopy homolog 2"
FT                   /id="PRO_0000031667"
FT   DOMAIN          24..175
FT                   /note="Saposin B-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   MOTIF           179..182
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   MOD_RES         115
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355"
FT   DISULFID        28..171
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   DISULFID        31..164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT   DISULFID        86..137
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
SQ   SEQUENCE   182 AA;  20767 MW;  83E54E7F01EE9B87 CRC64;
     MKGWGWLALL LGVLLGTAWA RRSQDLHCGA CRALVDELEW EIARVDPKKT IQMGSFRINP
     DGSQSVVEVP YARSEAHLTE LLEEVCDRMK EYGEQIDPST HRKNYVRVVS RNGESSELDL
     QGIRIDSDIS GTLKFACESI VEEYEDELIE FFSREADNVK DKLCSKRTDL CDHALHRSHD
     EL
//