ID ATRN_HUMAN Reviewed; 1429 AA. AC O75882; A8KAE5; O60295; O95414; Q3MIT3; Q5TDA2; Q5TDA4; Q5VYW3; AC Q9NTQ3; Q9NTQ4; Q9NU01; Q9NZ57; Q9NZ58; Q9UC75; Q9UDF5; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 2. DT 13-FEB-2019, entry version 187. DE RecName: Full=Attractin; DE AltName: Full=DPPT-L; DE AltName: Full=Mahogany homolog; DE Flags: Precursor; GN Name=ATRN; Synonyms=KIAA0548, MGCA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND TISSUE RP SPECIFICITY. RX PubMed=10811918; DOI=10.1073/pnas.110139897; RA Tang W., Gunn T.M., McLaughlin D.F., Barsh G.S., Schlossman S.F., RA Duke-Cohan J.S.; RT "Secreted and membrane attractin result from alternative splicing of RT the human ATRN gene."; RL Proc. Natl. Acad. Sci. U.S.A. 97:6025-6030(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Duke-Cohan J.S., Gu J., Freeman G.J., Schlossman S.F.; RT "Cloning of cDNA for attractin-2, identical with that of attractin RT except for a GC-rich 222 bp 5' insertion."; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 138-153; 537-548 AND 704-723 (ISOFORMS 1/2/3), RP SUBCELLULAR LOCATION, GLYCOSYLATION, AND SUBUNIT. RC TISSUE=Serum; RX PubMed=7539799; DOI=10.1074/jbc.270.23.14107; RA Duke-Cohan J.S., Morimoto C., Rocker J.A., Schlossman S.F.; RT "A novel form of dipeptidylpeptidase IV found in human serum. RT Isolation, characterization, and comparison with T lymphocyte membrane RT dipeptidylpeptidase IV (CD26)."; RL J. Biol. Chem. 270:14107-14114(1995). RN [7] RP PROTEIN SEQUENCE OF 138-153; 280-285; 355-376; 378-394; 405-411; RP 513-521; 538-547; 705-722; 735-755; 818-829; 851-860; 1145-1152; RP 1203-1213; 1243-1246 AND 1255-1272 (ISOFORM 2), FUNCTION, AND RP SUBCELLULAR LOCATION. RX PubMed=9736737; DOI=10.1073/pnas.95.19.11336; RA Duke-Cohan J.S., Gu J., McLaughlin D.F., Xu Y., Freeman G.J., RA Schlossman S.F.; RT "Attractin (DPPT-L), a member of the CUB family of cell adhesion and RT guidance proteins, is secreted by activated human T lymphocytes and RT modulates immune cell interactions."; RL Proc. Natl. Acad. Sci. U.S.A. 95:11336-11341(1998). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 978-1429 (ISOFORM 1). RC TISSUE=Brain; RX PubMed=9628581; DOI=10.1093/dnares/5.1.31; RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., RA Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. IX. RT The complete sequences of 100 new cDNA clones from brain which can RT code for large proteins in vitro."; RL DNA Res. 5:31-39(1998). RN [9] RP PROTEIN SEQUENCE OF N-TERMINUS, TISSUE SPECIFICITY, GLYCOSYLATION, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=17261078; DOI=10.1515/BC.2007.017; RA Friedrich D., Hoffmann T., Bar J., Wermann M., Manhart S., Heiser U., RA Demuth H.U.; RT "Does human attractin have DP4 activity?"; RL Biol. Chem. 388:155-162(2007). RN [10] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-264; ASN-383 AND ASN-731. RC TISSUE=Plasma; RX PubMed=14760718; DOI=10.1002/pmic.200300556; RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; RT "Screening for N-glycosylated proteins by liquid chromatography mass RT spectrometry."; RL Proteomics 4:454-465(2004). RN [11] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-264; ASN-300; ASN-383; RP ASN-416; ASN-428; ASN-575; ASN-623; ASN-1043; ASN-1198; ASN-1250 AND RP ASN-1259. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [12] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-416. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [13] RP GLYCOSYLATION AT ASN-300; ASN-383; ASN-731 AND ASN-1073. RX PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200; RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.; RT "A strategy for precise and large scale identification of core RT fucosylated glycoproteins."; RL Mol. Cell. Proteomics 8:913-923(2009). CC -!- FUNCTION: Involved in the initial immune cell clustering during CC inflammatory response and may regulate chemotactic activity of CC chemokines. May play a role in melanocortin signaling pathways CC that regulate energy homeostasis and hair color. Low-affinity CC receptor for agouti (By similarity). Has a critical role in normal CC myelination in the central nervous system (By similarity). CC {ECO:0000250, ECO:0000269|PubMed:9736737}. CC -!- SUBUNIT: Monomer and homotrimer. {ECO:0000269|PubMed:7539799}. CC -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane CC {ECO:0000269|PubMed:7539799}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:7539799}. CC -!- SUBCELLULAR LOCATION: Isoform 2: Secreted CC {ECO:0000269|PubMed:7539799, ECO:0000269|PubMed:9736737}. CC -!- SUBCELLULAR LOCATION: Isoform 3: Secreted CC {ECO:0000269|PubMed:7539799}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=Membrane; CC IsoId=O75882-1; Sequence=Displayed; CC Name=2; Synonyms=Secreted; CC IsoId=O75882-2; Sequence=VSP_001375; CC Name=3; CC IsoId=O75882-3; Sequence=VSP_001372, VSP_001375; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Isoform 2 is detected in plasma (at protein CC level). Expressed and secreted by activated T-lymphocytes. CC Expressed at low to moderate levels in peripheral blood CC leukocytes, spleen, lymph node, tonsil, bone marrow and fetal CC liver. At very low levels found in thymus. Isoform 2 is the major CC isoform in peripheral blood leukocytes. CC {ECO:0000269|PubMed:10811918, ECO:0000269|PubMed:17261078}. CC -!- INDUCTION: Activation of peripheral blood leukocytes with CC phytohemagglutinin induces strong expression of the membrane CC isoform followed by the release of the secreted isoform. CC -!- PTM: Heavily glycosylated. {ECO:0000269|PubMed:14760718, CC ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17261078, CC ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, CC ECO:0000269|PubMed:7539799}. CC -!- CAUTION: Was originally (PubMed:7539799 and PubMed:9736737) CC thought to have dipeptidase activity but it was shown later to CC lack that activity. {ECO:0000305|PubMed:17261078}. CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; CC Note=Attractin-2; CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_206"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AF218915; AAF72881.1; -; Genomic_DNA. DR EMBL; AF218889; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218890; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218891; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218892; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218893; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218894; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218895; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218896; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218897; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218898; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218899; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218900; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218901; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218902; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218903; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218904; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218905; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218906; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218907; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218908; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218909; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218911; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218912; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218913; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218914; AAF72881.1; JOINED; Genomic_DNA. DR EMBL; AF218910; AAF72882.1; -; Genomic_DNA. DR EMBL; AF218889; AAF72882.1; JOINED; Genomic_DNA. DR EMBL; AF218890; AAF72882.1; JOINED; Genomic_DNA. DR EMBL; AF218891; AAF72882.1; JOINED; Genomic_DNA. DR EMBL; AF218892; AAF72882.1; JOINED; Genomic_DNA. DR EMBL; AF218893; AAF72882.1; JOINED; Genomic_DNA. DR EMBL; AF218894; AAF72882.1; JOINED; Genomic_DNA. DR EMBL; AF218895; AAF72882.1; JOINED; Genomic_DNA. DR EMBL; AF218896; AAF72882.1; JOINED; Genomic_DNA. DR EMBL; AF218897; AAF72882.1; JOINED; Genomic_DNA. DR EMBL; AF218898; AAF72882.1; JOINED; Genomic_DNA. DR EMBL; AF218899; AAF72882.1; JOINED; Genomic_DNA. DR EMBL; AF218900; AAF72882.1; JOINED; Genomic_DNA. DR EMBL; AF218901; AAF72882.1; JOINED; Genomic_DNA. DR EMBL; AF218902; AAF72882.1; JOINED; Genomic_DNA. DR EMBL; AF218903; AAF72882.1; JOINED; Genomic_DNA. DR EMBL; AF218904; AAF72882.1; JOINED; Genomic_DNA. DR EMBL; AF218905; AAF72882.1; JOINED; Genomic_DNA. DR EMBL; AF218906; AAF72882.1; JOINED; Genomic_DNA. DR EMBL; AF218907; AAF72882.1; JOINED; Genomic_DNA. DR EMBL; AF218908; AAF72882.1; JOINED; Genomic_DNA. DR EMBL; AF218909; AAF72882.1; JOINED; Genomic_DNA. DR EMBL; AF106861; AAD03057.1; -; mRNA. DR EMBL; AK293010; BAF85699.1; -; mRNA. DR EMBL; AL109805; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL132773; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL353193; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC101705; AAI01706.1; -; mRNA. DR EMBL; AB011120; BAA25474.1; -; mRNA. DR CCDS; CCDS13053.1; -. [O75882-1] DR CCDS; CCDS13054.1; -. [O75882-2] DR RefSeq; NP_001193976.1; NM_001207047.2. DR RefSeq; NP_001310261.1; NM_001323332.1. DR RefSeq; NP_647537.1; NM_139321.2. [O75882-1] DR RefSeq; NP_647538.1; NM_139322.3. [O75882-2] DR UniGene; Hs.276252; -. DR ProteinModelPortal; O75882; -. DR SMR; O75882; -. DR BioGrid; 114033; 15. DR IntAct; O75882; 7. DR MINT; O75882; -. DR STRING; 9606.ENSP00000262919; -. DR GlyConnect; 679; -. DR iPTMnet; O75882; -. DR PhosphoSitePlus; O75882; -. DR SwissPalm; O75882; -. DR UniCarbKB; O75882; -. DR BioMuta; ATRN; -. DR EPD; O75882; -. DR jPOST; O75882; -. DR MaxQB; O75882; -. DR PaxDb; O75882; -. DR PeptideAtlas; O75882; -. DR PRIDE; O75882; -. DR ProteomicsDB; 50238; -. DR ProteomicsDB; 50239; -. [O75882-2] DR ProteomicsDB; 50240; -. [O75882-3] DR Ensembl; ENST00000262919; ENSP00000262919; ENSG00000088812. [O75882-1] DR Ensembl; ENST00000446916; ENSP00000416587; ENSG00000088812. [O75882-2] DR GeneID; 8455; -. DR KEGG; hsa:8455; -. DR UCSC; uc002wil.3; human. [O75882-1] DR CTD; 8455; -. DR DisGeNET; 8455; -. DR EuPathDB; HostDB:ENSG00000088812.17; -. DR GeneCards; ATRN; -. DR HGNC; HGNC:885; ATRN. DR HPA; HPA008853; -. DR MIM; 603130; gene. DR neXtProt; NX_O75882; -. DR OpenTargets; ENSG00000088812; -. DR PharmGKB; PA25178; -. DR eggNOG; KOG1388; Eukaryota. DR eggNOG; ENOG410XRW4; LUCA. DR GeneTree; ENSGT00940000157346; -. DR HOVERGEN; HBG004312; -. DR InParanoid; O75882; -. DR OMA; GIRCVWD; -. DR OrthoDB; 49565at2759; -. DR PhylomeDB; O75882; -. DR TreeFam; TF321873; -. DR SIGNOR; O75882; -. DR ChiTaRS; ATRN; human. DR GeneWiki; ATRN; -. DR GenomeRNAi; 8455; -. DR PRO; PR:O75882; -. DR Proteomes; UP000005640; Chromosome 20. DR Bgee; ENSG00000088812; Expressed in 235 organ(s), highest expression level in occipital lobe. DR Genevisible; O75882; HS. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; NAS:ProtInc. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc. DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl. DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW. DR GO; GO:0042552; P:myelination; IEA:Ensembl. DR GO; GO:0043473; P:pigmentation; IEA:Ensembl. DR GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl. DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl. DR CDD; cd03597; CLECT_attractin_like; 1. DR CDD; cd00041; CUB; 1. DR Gene3D; 2.120.10.80; -; 2. DR Gene3D; 2.60.120.290; -; 1. DR Gene3D; 3.10.100.10; -; 1. DR InterPro; IPR034011; Attractin-like_CTLD. DR InterPro; IPR001304; C-type_lectin-like. DR InterPro; IPR016186; C-type_lectin-like/link_sf. DR InterPro; IPR016187; CTDL_fold. DR InterPro; IPR000859; CUB_dom. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller. DR InterPro; IPR015915; Kelch-typ_b-propeller. DR InterPro; IPR006652; Kelch_1. DR InterPro; IPR002049; Laminin_EGF. DR InterPro; IPR002165; Plexin_repeat. DR InterPro; IPR016201; PSI. DR InterPro; IPR035914; Sperma_CUB_dom_sf. DR Pfam; PF00431; CUB; 1. DR Pfam; PF01344; Kelch_1; 2. DR Pfam; PF00059; Lectin_C; 1. DR Pfam; PF01437; PSI; 2. DR SMART; SM00034; CLECT; 1. DR SMART; SM00042; CUB; 1. DR SMART; SM00181; EGF; 2. DR SMART; SM00180; EGF_Lam; 2. DR SMART; SM00423; PSI; 5. DR SUPFAM; SSF49854; SSF49854; 1. DR SUPFAM; SSF50965; SSF50965; 1. DR SUPFAM; SSF56436; SSF56436; 1. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1. DR PROSITE; PS01180; CUB; 1. DR PROSITE; PS00022; EGF_1; 3. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 2. DR PROSITE; PS01248; EGF_LAM_1; 1. DR PROSITE; PS50027; EGF_LAM_2; 3. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Complete proteome; KW Direct protein sequencing; Disulfide bond; EGF-like domain; KW Glycoprotein; Inflammatory response; Kelch repeat; KW Laminin EGF-like domain; Lectin; Membrane; Polymorphism; Receptor; KW Reference proteome; Repeat; Secreted; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 28 {ECO:0000255}. FT PROPEP 29 83 {ECO:0000305|PubMed:17261078}. FT /FTId=PRO_0000394771. FT CHAIN 84 1429 Attractin. FT /FTId=PRO_0000007483. FT TOPO_DOM 84 1279 Extracellular. {ECO:0000255}. FT TRANSMEM 1280 1300 Helical. {ECO:0000255}. FT TOPO_DOM 1301 1429 Cytoplasmic. {ECO:0000255}. FT DOMAIN 101 129 EGF-like. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 132 248 CUB. {ECO:0000255|PROSITE- FT ProRule:PRU00059}. FT REPEAT 352 402 Kelch 1. FT REPEAT 404 451 Kelch 2. FT REPEAT 461 508 Kelch 3. FT REPEAT 513 564 Kelch 4. FT REPEAT 566 624 Kelch 5. FT REPEAT 625 671 Kelch 6. FT DOMAIN 703 748 PSI 1. FT DOMAIN 755 794 PSI 2. FT DOMAIN 795 919 C-type lectin. {ECO:0000255|PROSITE- FT ProRule:PRU00040}. FT DOMAIN 932 983 PSI 3. FT DOMAIN 986 1061 PSI 4. FT DOMAIN 1063 1108 Laminin EGF-like 1. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 1109 1157 Laminin EGF-like 2. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT COMPBIAS 43 77 Leu-rich. FT CARBOHYD 213 213 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 237 237 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 242 242 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 253 253 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 264 264 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:14760718, FT ECO:0000269|PubMed:16335952}. FT CARBOHYD 300 300 N-linked (GlcNAc...) (complex) FT asparagine. {ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19139490}. FT CARBOHYD 325 325 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 362 362 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 383 383 N-linked (GlcNAc...) (complex) FT asparagine. {ECO:0000269|PubMed:14760718, FT ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19139490}. FT CARBOHYD 416 416 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218}. FT CARBOHYD 428 428 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:16335952}. FT CARBOHYD 575 575 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:16335952}. FT CARBOHYD 623 623 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:16335952}. FT CARBOHYD 731 731 N-linked (GlcNAc...) (complex) FT asparagine. {ECO:0000269|PubMed:14760718, FT ECO:0000269|PubMed:19139490}. FT CARBOHYD 863 863 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 914 914 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 923 923 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 986 986 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1043 1043 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:16335952}. FT CARBOHYD 1054 1054 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1073 1073 N-linked (GlcNAc...) (complex) FT asparagine. FT {ECO:0000269|PubMed:19139490}. FT CARBOHYD 1082 1082 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1198 1198 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:16335952}. FT CARBOHYD 1206 1206 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1250 1250 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:16335952}. FT CARBOHYD 1259 1259 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:16335952}. FT DISULFID 101 111 {ECO:0000250}. FT DISULFID 105 118 {ECO:0000250}. FT DISULFID 120 129 {ECO:0000250}. FT DISULFID 250 260 {ECO:0000250}. FT DISULFID 254 271 {ECO:0000250}. FT DISULFID 273 282 {ECO:0000250}. FT DISULFID 816 918 {ECO:0000250}. FT DISULFID 1063 1071 {ECO:0000250}. FT DISULFID 1065 1077 {ECO:0000250}. FT DISULFID 1080 1089 {ECO:0000250}. FT DISULFID 1092 1106 {ECO:0000250}. FT DISULFID 1127 1137 {ECO:0000250}. FT DISULFID 1140 1155 {ECO:0000250}. FT VAR_SEQ 31 104 Missing (in isoform 3). {ECO:0000305}. FT /FTId=VSP_001372. FT VAR_SEQ 1268 1429 IAFSQHSNFMDLVQFFVTFFSCFLSLLLVAAVVWKIKQSCW FT ASRRREQLLREMQQMASRPFASVNVALETDEEPPDLIGGSI FT KTVPKPIALEPCFGNKAAVLSVFVRLPRGLGGIPPPGQSGL FT AVASALVDISQQMPIVYKEKSGAVRNRKQQPPAQPGTCI FT -> VQTEQ (in isoform 2 and isoform 3). FT {ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, FT ECO:0000303|Ref.2}. FT /FTId=VSP_001375. FT VARIANT 303 303 D -> A (in dbSNP:rs6107308). FT /FTId=VAR_048967. FT VARIANT 426 426 I -> T (in dbSNP:rs17782078). FT /FTId=VAR_048968. FT VARIANT 1152 1152 R -> K (in dbSNP:rs3886999). FT /FTId=VAR_048969. FT VARIANT 1226 1226 V -> I (in dbSNP:rs12329487). FT /FTId=VAR_048970. FT CONFLICT 69 69 S -> P (in Ref. 2; AAD03057). FT {ECO:0000305}. FT CONFLICT 267 267 D -> E (in Ref. 2; AAD03057). FT {ECO:0000305}. FT CONFLICT 413 413 S -> P (in Ref. 2; AAD03057). FT {ECO:0000305}. FT CONFLICT 620 620 V -> A (in Ref. 3; BAF85699). FT {ECO:0000305}. FT CONFLICT 704 704 C -> G (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 1172 1172 E -> K (in Ref. 1; AAF72881/AAF72882). FT {ECO:0000305}. SQ SEQUENCE 1429 AA; 158537 MW; 9F206A319B7E3DD8 CRC64; MVAAAAATEA RLRRRTAATA ALAGRSGGPH WDWDVTRAGR PGLGAGLRLP RLLSPPLRPR LLLLLLLLSP PLLLLLLPCE AEAAAAAAAV SGSAAAEAKE CDRPCVNGGR CNPGTGQCVC PAGWVGEQCQ HCGGRFRLTG SSGFVTDGPG NYKYKTKCTW LIEGQPNRIM RLRFNHFATE CSWDHLYVYD GDSIYAPLVA AFSGLIVPER DGNETVPEVV ATSGYALLHF FSDAAYNLTG FNITYSFDMC PNNCSGRGEC KISNSSDTVE CECSENWKGE ACDIPHCTDN CGFPHRGICN SSDVRGCSCF SDWQGPGCSV PVPANQSFWT REEYSNLKLP RASHKAVVNG NIMWVVGGYM FNHSDYNMVL AYDLASREWL PLNRSVNNVV VRYGHSLALY KDKIYMYGGK IDSTGNVTNE LRVFHIHNES WVLLTPKAKE QYAVVGHSAH IVTLKNGRVV MLVIFGHCPL YGYISNVQEY DLDKNTWSIL HTQGALVQGG YGHSSVYDHR TRALYVHGGY KAFSANKYRL ADDLYRYDVD TQMWTILKDS RFFRYLHTAV IVSGTMLVFG GNTHNDTSMS HGAKCFSSDF MAYDIACDRW SVLPRPDLHH DVNRFGHSAV LHNSTMYVFG GFNSLLLSDI LVFTSEQCDA HRSEAACLAA GPGIRCVWNT GSSQCISWAL ATDEQEEKLK SECFSKRTLD HDRCDQHTDC YSCTANTNDC HWCNDHCVPR NHSCSEGQIS IFRYENCPKD NPMYYCNKKT SCRSCALDQN CQWEPRNQEC IALPENICGI GWHLVGNSCL KITTAKENYD NAKLFCRNHN ALLASLTTQK KVEFVLKQLR IMQSSQSMSK LTLTPWVGLR KINVSYWCWE DMSPFTNSLL QWMPSEPSDA GFCGILSEPS TRGLKAATCI NPLNGSVCER PANHSAKQCR TPCALRTACG DCTSGSSECM WCSNMKQCVD SNAYVASFPF GQCMEWYTMS TCPPENCSGY CTCSHCLEQP GCGWCTDPSN TGKGKCIEGS YKGPVKMPSQ APTGNFYPQP LLNSSMCLED SRYNWSFIHC PACQCNGHSK CINQSICEKC ENLTTGKHCE TCISGFYGDP TNGGKCQPCK CNGHASLCNT NTGKCFCTTK GVKGDECQLC EVENRYQGNP LRGTCYYTLL IDYQFTFSLS QEDDRYYTAI NFVATPDEQN RDLDMFINAS KNFNLNITWA ASFSAGTQAG EEMPVVSKTN IKEYKDSFSN EKFDFRNHPN ITFFVYVSNF TWPIKIQIAF SQHSNFMDLV QFFVTFFSCF LSLLLVAAVV WKIKQSCWAS RRREQLLREM QQMASRPFAS VNVALETDEE PPDLIGGSIK TVPKPIALEP CFGNKAAVLS VFVRLPRGLG GIPPPGQSGL AVASALVDIS QQMPIVYKEK SGAVRNRKQQ PPAQPGTCI //