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SLUR2_HUMAN
ID   SLUR2_HUMAN             Reviewed;          97 AA.
AC   P0DP57; D3DWI7; G3XAC2; Q86SR0; Q9BZG9;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2017, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Secreted Ly-6/uPAR domain-containing protein 2 {ECO:0000305};
DE   AltName: Full=Secreted LY6/PLAUR domain-containing protein 2 {ECO:0000312|HGNC:HGNC:25549};
DE   AltName: Full=Secreted Ly-6/uPAR-related protein 2 {ECO:0000303|PubMed:12573258};
DE            Short=SLURP-2 {ECO:0000303|PubMed:12573258};
DE   Flags: Precursor;
GN   Name=SLURP2 {ECO:0000312|HGNC:HGNC:25549};
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], AND TISSUE SPECIFICITY.
RC   TISSUE=Skin;
RX   PubMed=12573258; DOI=10.1016/s0888-7543(02)00025-3;
RA   Tsuji H., Okamoto K., Matsuzaka Y., Iizuka H., Tamiya G., Inoko H.;
RT   "SLURP-2, a novel member of the human Ly-6 superfamily that is up-regulated
RT   in psoriasis vulgaris.";
RL   Genomics 81:26-33(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=16575903; DOI=10.1002/jcp.20661;
RA   Arredondo J., Chernyavsky A.I., Jolkovsky D.L., Webber R.J., Grando S.A.;
RT   "SLURP-2: a novel cholinergic signaling peptide in human mucocutaneous
RT   epithelium.";
RL   J. Cell. Physiol. 208:238-245(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   INDUCTION.
RX   PubMed=26033490; DOI=10.1016/j.intimp.2015.05.030;
RA   Moriwaki Y., Takada K., Tsuji S., Kawashima K., Misawa H.;
RT   "Transcriptional regulation of SLURP2, a psoriasis-associated gene, is
RT   under control of IL-22 in the skin: A special reference to the nested gene
RT   LYNX1.";
RL   Int. Immunopharmacol. 29:71-75(2015).
RN   [7]
RP   STRUCTURE BY NMR OF 23-97, DISULFIDE BONDS, FUNCTION, AND INTERACTION WITH
RP   CHRNA3; CHRNA4; CHRNA5; CHRNA7; CHRNB2; CHRNB4; CHRM1 AND CHRM3.
RX   PubMed=27485575; DOI=10.1038/srep30698;
RA   Lyukmanova E.N., Shulepko M.A., Shenkarev Z.O., Bychkov M.L.,
RA   Paramonov A.S., Chugunov A.O., Kulbatskii D.S., Arvaniti M., Dolejsi E.,
RA   Schaer T., Arseniev A.S., Efremov R.G., Thomsen M.S., Dolezal V.,
RA   Bertrand D., Dolgikh D.A., Kirpichnikov M.P.;
RT   "Secreted isoform of human Lynx1 (SLURP-2): spatial structure and
RT   pharmacology of interactions with different types of acetylcholine
RT   receptors.";
RL   Sci. Rep. 6:30698-30698(2016).
CC   -!- FUNCTION: Binds and may modulate the functional properties of nicotinic
CC       and muscarinic acetylcholine receptors. May regulate keratinocytes
CC       proliferation, differentiation and apoptosis. In vitro moderately
CC       inhibits ACh-evoked currents of alpha-3:beta-2-containing nAChRs and
CC       strongly these of alpha-4:beta-2-containing nAChRs, modulates alpha-7-
CC       containing nAChRs, and inhibits nicotine-induced signaling probably
CC       implicating alpha-3:beta-4-containing nAChRs. Proposed to act on alpha-
CC       3:beta-2 and alpha-7 nAChRs in an orthosteric, and on mAChRs, such as
CC       CHRM1 and CHRM3, in an allosteric manner. {ECO:0000269|PubMed:16575903,
CC       ECO:0000269|PubMed:27485575}.
CC   -!- SUBUNIT: Interacts with CHRNA3, CHRNA4, CHRNA5, CHRNA7, CHRNB2 and
CC       CHRNB4. Interacts with CHRM1 and CHRM3 probably in an allosteric manner
CC       (PubMed:27485575). {ECO:0000269|PubMed:27485575}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16575903}.
CC   -!- TISSUE SPECIFICITY: Expressed at highest levels in cervix and
CC       esophagus, followed by adult and fetal skin. Expressed at lower levels
CC       in brain, lung, stomach, small intestine, colon, rectum, uterus, and
CC       thymus. Not detected in spleen nor bone marrow. Up-regulated 3-fold in
CC       psoriatic lesional skin (PubMed:12573258). In the epidermis,
CC       predominantly produced by keratinocytes of the suprabasal epidermal
CC       compartment (at protein level) (PubMed:16575903). In attached gingiva,
CC       produced at highest levels by basal cells located in the lowermost
CC       epithelial layers (at protein level) (PubMed:16575903). Detected in
CC       serum (at protein level) (PubMed:16575903).
CC       {ECO:0000269|PubMed:12573258, ECO:0000269|PubMed:16575903}.
CC   -!- INDUCTION: Up-regulation by IL22/interleukin-22 is suppressed by
CC       IFNG/Interferon gamma (at protein level).
CC       {ECO:0000269|PubMed:26033490}.
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DR   EMBL; AB081838; BAC56859.1; -; mRNA.
DR   EMBL; AY587277; AAT00512.1; -; mRNA.
DR   EMBL; AY358417; AAQ88783.1; -; mRNA.
DR   EMBL; AC083841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471162; EAW82306.1; -; Genomic_DNA.
DR   CCDS; CCDS34952.1; -.
DR   RefSeq; NP_803253.1; NM_177458.1.
DR   PDB; 2N99; NMR; -; A=23-97.
DR   PDBsum; 2N99; -.
DR   AlphaFoldDB; P0DP57; -.
DR   SMR; P0DP57; -.
DR   IntAct; P0DP57; 1.
DR   BioMuta; SLURP2; -.
DR   jPOST; P0DP57; -.
DR   MassIVE; P0DP57; -.
DR   PeptideAtlas; P0DP57; -.
DR   PRIDE; P0DP57; -.
DR   DNASU; 432355; -.
DR   Ensembl; ENST00000317543.12; ENSP00000319846.7; ENSG00000283992.2.
DR   GeneID; 432355; -.
DR   KEGG; hsa:432355; -.
DR   MANE-Select; ENST00000317543.12; ENSP00000319846.7; NM_177458.3; NP_803253.1.
DR   CTD; 432355; -.
DR   DisGeNET; 432355; -.
DR   GeneCards; SLURP2; -.
DR   HGNC; HGNC:25549; SLURP2.
DR   HPA; ENSG00000283992; Group enriched (esophagus, skin, vagina).
DR   MIM; 606110; gene.
DR   neXtProt; NX_P0DP57; -.
DR   VEuPathDB; HostDB:ENSG00000283992; -.
DR   GeneTree; ENSGT00940000164325; -.
DR   OMA; LMCHQCK; -.
DR   OrthoDB; 1593386at2759; -.
DR   PathwayCommons; P0DP57; -.
DR   SignaLink; P0DP57; -.
DR   GenomeRNAi; 66004; -.
DR   Pharos; P0DP57; Tbio.
DR   PRO; PR:P0DP57; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; P0DP57; protein.
DR   Bgee; ENSG00000283992; Expressed in lower esophagus mucosa and 82 other tissues.
DR   ExpressionAtlas; P0DP57; baseline and differential.
DR   Genevisible; Q9BZG9; HS.
DR   GO; GO:0031225; C:anchored component of membrane; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0033130; F:acetylcholine receptor binding; IDA:UniProtKB.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IBA:GO_Central.
DR   GO; GO:0030548; F:acetylcholine receptor regulator activity; IDA:UniProtKB.
DR   GO; GO:0095500; P:acetylcholine receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0099601; P:regulation of neurotransmitter receptor activity; IDA:UniProtKB.
DR   CDD; cd00117; LU; 1.
DR   Gene3D; 2.10.60.10; -; 1.
DR   InterPro; IPR016054; LY6_UPA_recep-like.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   Pfam; PF00021; UPAR_LY6; 1.
DR   SUPFAM; SSF57302; SSF57302; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..97
FT                   /note="Secreted Ly-6/uPAR domain-containing protein 2"
FT                   /id="PRO_0000440646"
FT   DOMAIN          25..95
FT                   /note="UPAR/Ly6"
FT                   /evidence="ECO:0000255"
FT   DISULFID        25..47
FT                   /evidence="ECO:0000269|PubMed:27485575,
FT                   ECO:0007744|PDB:2N99"
FT   DISULFID        28..34
FT                   /evidence="ECO:0000269|PubMed:27485575,
FT                   ECO:0007744|PDB:2N99"
FT   DISULFID        40..68
FT                   /evidence="ECO:0000269|PubMed:27485575,
FT                   ECO:0007744|PDB:2N99"
FT   DISULFID        72..88
FT                   /evidence="ECO:0000269|PubMed:27485575,
FT                   ECO:0007744|PDB:2N99"
FT   DISULFID        89..94
FT                   /evidence="ECO:0000269|PubMed:27485575,
FT                   ECO:0007744|PDB:2N99"
FT   STRAND          24..26
FT                   /evidence="ECO:0007829|PDB:2N99"
FT   TURN            31..33
FT                   /evidence="ECO:0007829|PDB:2N99"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:2N99"
FT   STRAND          46..52
FT                   /evidence="ECO:0007829|PDB:2N99"
FT   STRAND          63..71
FT                   /evidence="ECO:0007829|PDB:2N99"
FT   HELIX           76..78
FT                   /evidence="ECO:0007829|PDB:2N99"
FT   STRAND          81..83
FT                   /evidence="ECO:0007829|PDB:2N99"
FT   STRAND          85..91
FT                   /evidence="ECO:0007829|PDB:2N99"
FT   TURN            92..95
FT                   /evidence="ECO:0007829|PDB:2N99"
SQ   SEQUENCE   97 AA;  10160 MW;  81719A103EC3001A CRC64;
     MQLGTGLLLA AVLSLQLAAA EAIWCHQCTG FGGCSHGSRC LRDSTHCVTT ATRVLSNTED
     LPLVTKMCHI GCPDIPSLGL GPYVSIACCQ TSLCNHD
 
 
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