SLUR1_MOUSE
ID SLUR1_MOUSE Reviewed; 110 AA.
AC Q9Z0K7; Q2TA55;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Secreted Ly-6/uPAR-related protein 1;
DE Short=SLURP-1;
DE AltName: Full=ARS component B;
DE Flags: Precursor;
GN Name=Slurp1; Synonyms=Ars;
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 [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RA Mastrangeli R., Donini S., Kelton C., Lou S., Serlupi-Crescenzi O.,
RA Vaccaro R., Renda T., Bressan A., Micangeli E., Milazzo F., Ciolli V.,
RA Biffoni M., El Tayar N., Lisciani R., Borrelli F., Martelli F., Serani S.,
RA Papoian R.;
RT "Cloning of ARS gene, component B, a new member of Ly-6-related family.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Skin;
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].
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 TISSUE SPECIFICITY.
RX PubMed=14721776;
RA Mastrangeli R., Donini S., Kelton C.A., He C., Bressan A., Milazzo F.,
RA Ciolli V., Borrelli F., Martelli F., Biffoni M., Serlupi-Crescenzi O.,
RA Serani S., Micangeli E., El Tayar N., Vaccaro R., Renda T., Lisciani R.,
RA Rossi M., Papoian R.;
RT "ARS component B: structural characterization, tissue expression and
RT regulation of the gene and protein (SLURP-1) associated with Mal de
RT Meleda.";
RL Eur. J. Dermatol. 13:560-570(2003).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17286989; DOI=10.1016/j.lfs.2006.12.028;
RA Moriwaki Y., Yoshikawa K., Fukuda H., Fujii Y.X., Misawa H., Kawashima K.;
RT "Immune system expression of SLURP-1 and SLURP-2, two endogenous nicotinic
RT acetylcholine receptor ligands.";
RL Life Sci. 80:2365-2368(2007).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=19396877; DOI=10.1002/jnr.22102;
RA Horiguchi K., Horiguchi S., Yamashita N., Irie K., Masuda J.,
RA Takano-Ohmuro H., Himi T., Miyazawa M., Moriwaki Y., Okuda T., Misawa H.,
RA Ozaki H., Kawashima K.;
RT "Expression of SLURP-1, an endogenous alpha7 nicotinic acetylcholine
RT receptor allosteric ligand, in murine bronchial epithelial cells.";
RL J. Neurosci. Res. 87:2740-2747(2009).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=20621062; DOI=10.1016/j.bbrc.2010.07.006;
RA Narumoto O., Horiguchi K., Horiguchi S., Moriwaki Y., Takano-Ohmuro H.,
RA Shoji S., Misawa H., Yamashita N., Nagase T., Kawashima K., Yamashita N.;
RT "Down-regulation of secreted lymphocyte antigen-6/urokinase-type
RT plasminogen activator receptor-related peptide-1 (SLURP-1), an endogenous
RT allosteric alpha7 nicotinic acetylcholine receptor modulator, in murine and
RT human asthmatic conditions.";
RL Biochem. Biophys. Res. Commun. 398:713-718(2010).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=23139280; DOI=10.1167/iovs.12-10759;
RA Swamynathan S., Buela K.A., Kinchington P., Lathrop K.L., Misawa H.,
RA Hendricks R.L., Swamynathan S.K.;
RT "Klf4 regulates the expression of Slurp1, which functions as an
RT immunomodulatory peptide in the mouse cornea.";
RL Invest. Ophthalmol. Vis. Sci. 53:8433-8446(2012).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=24499735; DOI=10.1038/jid.2014.19;
RA Adeyo O., Allan B.B., Barnes R.H. II, Goulbourne C.N., Tatar A., Tu Y.,
RA Young L.C., Weinstein M.M., Tontonoz P., Fong L.G., Beigneux A.P.,
RA Young S.G.;
RT "Palmoplantar keratoderma along with neuromuscular and metabolic phenotypes
RT in Slurp1-deficient mice.";
RL J. Invest. Dermatol. 134:1589-1598(2014).
RN [10]
RP FUNCTION, AND INTERACTION WITH PLAU.
RX PubMed=25168896; DOI=10.1167/iovs.14-15107;
RA Swamynathan S., Swamynathan S.K.;
RT "SLURP-1 modulates corneal homeostasis by serving as a soluble scavenger of
RT urokinase-type plasminogen activator.";
RL Invest. Ophthalmol. Vis. Sci. 55:6251-6261(2014).
CC -!- FUNCTION: Has an antitumor activity. Was found to be a marker of late
CC differentiation of the skin. Implicated in maintaining the
CC physiological and structural integrity of the keratinocyte layers of
CC the skin. In vitro down-regulates keratinocyte proliferation; the
CC function may involve the proposed role as modulator of nicotinic
CC acetylcholine receptors (nAChRs) activity. In vitro inhibits alpha-7-
CC dependent nAChR currents in an allosteric manner (By similarity). In T
CC cells may be involved in regulation of intracellular Ca(2+) signaling
CC (PubMed:17286989). Seems to have a immunomodulatory function in the
CC cornea. The function may implicate a possible role as a scavenger
CC receptor for PLAU thereby blocking PLAU-dependent functions of PLAUR
CC such as in cell migration and proliferation (PubMed:23139280,
CC PubMed:25168896). {ECO:0000250|UniProtKB:P55000,
CC ECO:0000269|PubMed:17286989, ECO:0000269|PubMed:23139280,
CC ECO:0000269|PubMed:25168896}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with PLAU
CC (PubMed:25168896). Interacts with CHRNA7. {ECO:0000250,
CC ECO:0000250|UniProtKB:P55000, ECO:0000269|PubMed:25168896}.
CC -!- INTERACTION:
CC Q9Z0K7; P06869: Plau; NbExp=4; IntAct=EBI-14060702, EBI-8365661;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P55000}.
CC -!- TISSUE SPECIFICITY: Expressed in skin, eye, whole lung, trachea,
CC esophagus and stomach (PubMed:14721776). Widely expressed in various
CC tissues including spleen and thymus but not pancreas. Expressed in
CC macrophages, dendritic cells, T and B cells (PubMed:17286989).
CC Expressed in lung specifically in ciliated bronchial epithelial cells
CC (at protein level). Expression is decreased in lungs of asthmatic model
CC mice(PubMed:19396877, PubMed:20621062). Expressed in the cornea
CC (PubMed:23139280). {ECO:0000269|PubMed:14721776,
CC ECO:0000269|PubMed:17286989, ECO:0000269|PubMed:19396877,
CC ECO:0000269|PubMed:20621062, ECO:0000269|PubMed:23139280}.
CC -!- INDUCTION: Down-regulated in the cornea under pro-inflammatory
CC conditions. {ECO:0000269|PubMed:23139280}.
CC -!- DISRUPTION PHENOTYPE: Severe palmoplantar keratoderma, reduced
CC adiposity, protection from obesity on a high-fat diet, low plasma lipid
CC levels, and neuromuscular abnormality (hind-limb clasping).
CC {ECO:0000269|PubMed:24499735}.
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DR EMBL; AJ132356; CAA10646.1; -; Genomic_DNA.
DR EMBL; AK003904; BAB23068.1; -; mRNA.
DR EMBL; AK029079; BAC26282.1; -; mRNA.
DR EMBL; BC111105; AAI11106.1; -; mRNA.
DR EMBL; BC125244; AAI25245.1; -; mRNA.
DR CCDS; CCDS27528.1; -.
DR RefSeq; NP_065265.1; NM_020519.1.
DR AlphaFoldDB; Q9Z0K7; -.
DR SMR; Q9Z0K7; -.
DR IntAct; Q9Z0K7; 1.
DR STRING; 10090.ENSMUSP00000141013; -.
DR iPTMnet; Q9Z0K7; -.
DR PhosphoSitePlus; Q9Z0K7; -.
DR PaxDb; Q9Z0K7; -.
DR PRIDE; Q9Z0K7; -.
DR ProteomicsDB; 261196; -.
DR Antibodypedia; 27784; 162 antibodies from 21 providers.
DR DNASU; 57277; -.
DR Ensembl; ENSMUST00000190433; ENSMUSP00000141013; ENSMUSG00000022596.
DR GeneID; 57277; -.
DR KEGG; mmu:57277; -.
DR UCSC; uc007wft.1; mouse.
DR CTD; 57152; -.
DR MGI; MGI:1930923; Slurp1.
DR VEuPathDB; HostDB:ENSMUSG00000022596; -.
DR eggNOG; ENOG502TDUY; Eukaryota.
DR GeneTree; ENSGT00940000162933; -.
DR HOGENOM; CLU_141358_2_1_1; -.
DR InParanoid; Q9Z0K7; -.
DR OMA; GEAFRCY; -.
DR OrthoDB; 1592016at2759; -.
DR PhylomeDB; Q9Z0K7; -.
DR TreeFam; TF336080; -.
DR BioGRID-ORCS; 57277; 0 hits in 71 CRISPR screens.
DR PRO; PR:Q9Z0K7; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9Z0K7; protein.
DR Bgee; ENSMUSG00000022596; Expressed in tail skin and 33 other tissues.
DR ExpressionAtlas; Q9Z0K7; baseline and differential.
DR Genevisible; Q9Z0K7; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0030549; F:acetylcholine receptor activator activity; ISO:MGI.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; IDA:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IMP:MGI.
DR GO; GO:0050884; P:neuromuscular process controlling posture; IMP:MGI.
DR GO; GO:0038195; P:urokinase plasminogen activator signaling pathway; ISO:MGI.
DR CDD; cd00117; LU; 1.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR018363; CD59_antigen_CS.
DR InterPro; IPR016054; LY6_UPA_recep-like.
DR InterPro; IPR027103; SLURP1.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR PANTHER; PTHR10036:SF17; PTHR10036:SF17; 1.
DR Pfam; PF00021; UPAR_LY6; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS00983; LY6_UPAR; 1.
PE 1: Evidence at protein level;
KW Cytokine; Disulfide bond; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..110
FT /note="Secreted Ly-6/uPAR-related protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036168"
FT DOMAIN 24..73
FT /note="UPAR/Ly6"
FT DISULFID 25..50
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58, ECO:0000250|UniProtKB:P55000,
FT ECO:0000255"
FT DISULFID 28..37
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58, ECO:0000250|UniProtKB:P55000,
FT ECO:0000255"
FT DISULFID 43..73
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58, ECO:0000250|UniProtKB:P55000,
FT ECO:0000255"
FT DISULFID 77..93
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58, ECO:0000250|UniProtKB:P55000,
FT ECO:0000255"
FT DISULFID 94..99
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58, ECO:0000250|UniProtKB:P55000,
FT ECO:0000255"
SQ SEQUENCE 110 AA; 12016 MW; AAB69CF6C5FE5BFC CRC64;
MTLRWAMWLL LLAAWSMGYG EAFRCYTCEQ PTAINSCKNI AQCKMEDTAC KTVLETVEAA
FPFNHSPMVT RSCSSSCLAT DPDGIGVAHP VFCCFRDLCN SGFPGFVAGL
