ATRN_HUMAN
ID ATRN_HUMAN Reviewed; 1429 AA.
AC O75882; A8KAE5; O60295; O95414; Q3MIT3; Q5TDA2; Q5TDA4; Q5VYW3; Q9NTQ3;
AC Q9NTQ4; Q9NU01; Q9NZ57; Q9NZ58; Q9UC75; Q9UDF5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 206.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 the
RT 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 except
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., 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., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., 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 project:
RT 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. Isolation,
RT 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; 513-521;
RP 538-547; 705-722; 735-755; 818-829; 851-860; 1145-1152; 1203-1213;
RP 1243-1246 AND 1255-1272 (ISOFORM 2), FUNCTION, AND 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. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT 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; ASN-416;
RP ASN-428; ASN-575; ASN-623; ASN-1043; ASN-1198; ASN-1250 AND 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., Moore R.J.,
RA 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 multiple
RT 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., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT 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 that
CC regulate energy homeostasis and hair color. Low-affinity receptor for
CC agouti (By similarity). Has a critical role in normal myelination in
CC the central nervous system (By similarity). {ECO:0000250,
CC 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 -!- TISSUE SPECIFICITY: Isoform 2 is detected in plasma (at protein level).
CC Expressed and secreted by activated T-lymphocytes. Expressed at low to
CC moderate levels in peripheral blood leukocytes, spleen, lymph node,
CC tonsil, bone marrow and fetal liver. At very low levels found in
CC thymus. Isoform 2 is the major 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 isoform
CC 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) thought to
CC have dipeptidase activity but it was shown later to lack that activity.
CC {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";
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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 AlphaFoldDB; O75882; -.
DR SMR; O75882; -.
DR BioGRID; 114033; 103.
DR IntAct; O75882; 10.
DR MINT; O75882; -.
DR STRING; 9606.ENSP00000262919; -.
DR GlyConnect; 679; 50 N-Linked glycans (15 sites).
DR GlyGen; O75882; 27 sites, 66 N-linked glycans (15 sites), 1 O-linked glycan (1 site).
DR iPTMnet; O75882; -.
DR PhosphoSitePlus; O75882; -.
DR SwissPalm; O75882; -.
DR BioMuta; ATRN; -.
DR CPTAC; CPTAC-664; -.
DR CPTAC; non-CPTAC-1089; -.
DR EPD; O75882; -.
DR jPOST; O75882; -.
DR MassIVE; O75882; -.
DR MaxQB; O75882; -.
DR PaxDb; O75882; -.
DR PeptideAtlas; O75882; -.
DR PRIDE; O75882; -.
DR ProteomicsDB; 50238; -. [O75882-1]
DR ProteomicsDB; 50239; -. [O75882-2]
DR ProteomicsDB; 50240; -. [O75882-3]
DR Antibodypedia; 2265; 260 antibodies from 31 providers.
DR DNASU; 8455; -.
DR Ensembl; ENST00000262919.10; ENSP00000262919.5; ENSG00000088812.18. [O75882-1]
DR Ensembl; ENST00000446916.2; ENSP00000416587.2; ENSG00000088812.18. [O75882-2]
DR GeneID; 8455; -.
DR KEGG; hsa:8455; -.
DR MANE-Select; ENST00000262919.10; ENSP00000262919.5; NM_139321.3; NP_647537.1.
DR UCSC; uc002wil.3; human. [O75882-1]
DR CTD; 8455; -.
DR DisGeNET; 8455; -.
DR GeneCards; ATRN; -.
DR HGNC; HGNC:885; ATRN.
DR HPA; ENSG00000088812; Low tissue specificity.
DR MIM; 603130; gene.
DR neXtProt; NX_O75882; -.
DR OpenTargets; ENSG00000088812; -.
DR PharmGKB; PA25178; -.
DR VEuPathDB; HostDB:ENSG00000088812; -.
DR eggNOG; KOG1388; Eukaryota.
DR GeneTree; ENSGT00940000157346; -.
DR HOGENOM; CLU_003930_0_0_1; -.
DR InParanoid; O75882; -.
DR OMA; EACNIAA; -.
DR OrthoDB; 49565at2759; -.
DR PhylomeDB; O75882; -.
DR TreeFam; TF321873; -.
DR PathwayCommons; O75882; -.
DR SignaLink; O75882; -.
DR SIGNOR; O75882; -.
DR BioGRID-ORCS; 8455; 29 hits in 1077 CRISPR screens.
DR ChiTaRS; ATRN; human.
DR GeneWiki; ATRN; -.
DR GenomeRNAi; 8455; -.
DR Pharos; O75882; Tbio.
DR PRO; PR:O75882; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O75882; protein.
DR Bgee; ENSG00000088812; Expressed in duodenum and 214 other tissues.
DR Genevisible; O75882; HS.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
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 GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd03597; CLECT_attractin_like; 1.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00055; EGF_Lam; 3.
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; 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; LE_dom.
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; Direct protein sequencing;
KW Disulfide bond; EGF-like domain; Glycoprotein; Inflammatory response;
KW Kelch repeat; Laminin EGF-like domain; Lectin; Membrane; Receptor;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..83
FT /evidence="ECO:0000305|PubMed:17261078"
FT /id="PRO_0000394771"
FT CHAIN 84..1429
FT /note="Attractin"
FT /id="PRO_0000007483"
FT TOPO_DOM 84..1279
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1280..1300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1301..1429
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 101..129
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 132..248
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT REPEAT 352..402
FT /note="Kelch 1"
FT REPEAT 404..451
FT /note="Kelch 2"
FT REPEAT 461..508
FT /note="Kelch 3"
FT REPEAT 513..564
FT /note="Kelch 4"
FT REPEAT 566..624
FT /note="Kelch 5"
FT REPEAT 625..671
FT /note="Kelch 6"
FT DOMAIN 703..748
FT /note="PSI 1"
FT DOMAIN 755..794
FT /note="PSI 2"
FT DOMAIN 795..919
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 932..983
FT /note="PSI 3"
FT DOMAIN 986..1061
FT /note="PSI 4"
FT DOMAIN 1063..1108
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1109..1157
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:16335952"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 575
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 623
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 731
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:19139490"
FT CARBOHYD 863
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 914
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 923
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 986
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1043
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 1054
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1073
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:19139490"
FT CARBOHYD 1082
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 1206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 1259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT DISULFID 101..111
FT /evidence="ECO:0000250"
FT DISULFID 105..118
FT /evidence="ECO:0000250"
FT DISULFID 120..129
FT /evidence="ECO:0000250"
FT DISULFID 250..260
FT /evidence="ECO:0000250"
FT DISULFID 254..271
FT /evidence="ECO:0000250"
FT DISULFID 273..282
FT /evidence="ECO:0000250"
FT DISULFID 816..918
FT /evidence="ECO:0000250"
FT DISULFID 1063..1071
FT /evidence="ECO:0000250"
FT DISULFID 1065..1077
FT /evidence="ECO:0000250"
FT DISULFID 1080..1089
FT /evidence="ECO:0000250"
FT DISULFID 1092..1106
FT /evidence="ECO:0000250"
FT DISULFID 1127..1137
FT /evidence="ECO:0000250"
FT DISULFID 1140..1155
FT /evidence="ECO:0000250"
FT VAR_SEQ 31..104
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_001372"
FT VAR_SEQ 1268..1429
FT /note="IAFSQHSNFMDLVQFFVTFFSCFLSLLLVAAVVWKIKQSCWASRRREQLLRE
FT MQQMASRPFASVNVALETDEEPPDLIGGSIKTVPKPIALEPCFGNKAAVLSVFVRLPRG
FT LGGIPPPGQSGLAVASALVDISQQMPIVYKEKSGAVRNRKQQPPAQPGTCI -> VQTE
FT Q (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_001375"
FT VARIANT 303
FT /note="D -> A (in dbSNP:rs6107308)"
FT /id="VAR_048967"
FT VARIANT 426
FT /note="I -> T (in dbSNP:rs17782078)"
FT /id="VAR_048968"
FT VARIANT 1152
FT /note="R -> K (in dbSNP:rs3886999)"
FT /id="VAR_048969"
FT VARIANT 1226
FT /note="V -> I (in dbSNP:rs12329487)"
FT /id="VAR_048970"
FT CONFLICT 69
FT /note="S -> P (in Ref. 2; AAD03057)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="D -> E (in Ref. 2; AAD03057)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="S -> P (in Ref. 2; AAD03057)"
FT /evidence="ECO:0000305"
FT CONFLICT 620
FT /note="V -> A (in Ref. 3; BAF85699)"
FT /evidence="ECO:0000305"
FT CONFLICT 704
FT /note="C -> G (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1172
FT /note="E -> K (in Ref. 1; AAF72881/AAF72882)"
FT /evidence="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
