ID ARAID_HUMAN Reviewed; 229 AA. AC Q6UW56; A8C1S2; A8K779; Q96FF6; Q96RT2; Q9Y2R7; Q9Y5L7; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 2. DT 29-MAY-2024, entry version 153. DE RecName: Full=All-trans retinoic acid-induced differentiation factor; DE AltName: Full=Apoptosis-related protein 3; DE Short=APR-3; DE AltName: Full=p18; DE Flags: Precursor; GN Name=ATRAID {ECO:0000312|HGNC:HGNC:24090}; Synonyms=APR3, C2orf28; GN ORFNames=HSPC013, UNQ214/PRO240; 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] (ISOFORM 1), AND VARIANT SER-209. RC TISSUE=Kidney; RA Mori K., Ogawa Y., Tashiro K., Ozaki S., Mukoyama M., Tanaka I., Nakao K.; RT "Molecular cloning of a novel protein with four putative transmembrane RT domains."; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=10948432; DOI=10.2144/00292st06; RA Zhu F., Yan W., Zhao Z.L., Chai Y.B., Lu F., Wang Q., Peng W.D., Yang A.G., RA Wang C.J.; RT "Improved PCR-based subtractive hybridization strategy for cloning RT differentially expressed genes."; RL BioTechniques 29:310-313(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Yang Y.C., Chen S.Y., Chang M.S.; RT "Cloning and characterization of p18."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Skeletal muscle; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Neuroblastoma; RA Li W.B., Gruber C., Jessee J., Polayes D.; RT "Full-length cDNA libraries and normalization."; RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [9] 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 [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, Placenta, and Uterus; 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 [11] RP PROTEIN SEQUENCE OF 31-45. RX PubMed=15340161; DOI=10.1110/ps.04682504; RA Zhang Z., Henzel W.J.; RT "Signal peptide prediction based on analysis of experimentally verified RT cleavage sites."; RL Protein Sci. 13:2819-2824(2004). RN [12] RP INDUCTION, SUBCELLULAR LOCATION, AND POSSIBLE FUNCTION. RX PubMed=17524364; DOI=10.1016/j.bbrc.2007.05.049; RA Yu F., Yang G., Zhao Z., Ji L., Cao Y., Bai L., Lu F., Fu H., Huang B., RA Li H., Zhang J., Yao L., Lu Z.; RT "Apoptosis related protein 3, an ATRA-upregulated membrane protein arrests RT the cell cycle at G1/S phase by decreasing the expression of cyclin D1."; RL Biochem. Biophys. Res. Commun. 358:1041-1046(2007). RN [13] RP ALTERNATIVE PROMOTER USAGE. RX PubMed=17387583; DOI=10.1007/s11010-007-9440-7; RA Yang G., Yu F., Fu H., Lu F., Huang B., Bai L., Zhao Z., Yao L., Lu Z.; RT "Identification of the distinct promoters for the two transcripts of RT apoptosis related protein 3 and their transcriptional regulation by NFAT RT and NFkappaB."; RL Mol. Cell. Biochem. 302:187-194(2007). RN [14] RP FUNCTION IN OSTEOBLAST DIFFERENTIATION, INTERACTION WITH NELL1, AND RP SUBCELLULAR LOCATION. RX PubMed=21723284; DOI=10.1016/j.febslet.2011.06.024; RA Zou X., Shen J., Chen F., Ting K., Zheng Z., Pang S., Zara J.N., RA Adams J.S., Soo C., Zhang X.; RT "NELL-1 binds to APR3 affecting human osteoblast proliferation and RT differentiation."; RL FEBS Lett. 585:2410-2418(2011). RN [15] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SLC37A3. RX PubMed=29745899; DOI=10.7554/elife.36620; RA Yu Z., Surface L.E., Park C.Y., Horlbeck M.A., Wyant G.A., Abu-Remaileh M., RA Peterson T.R., Sabatini D.M., Weissman J.S., O'Shea E.K.; RT "Identification of a transporter complex responsible for the cytosolic RT entry of nitrogen-containing bisphosphonates."; RL Elife 7:0-0(2018). CC -!- FUNCTION: Promotes osteoblast cell differentiation and terminal CC mineralization. Plays a role in inducing the cell cycle arrest via CC inhibiting CCND1 expression in all-trans-retinoic acid (ATRA) signal CC pathway. In osteoclasts, forms a transporter complex with ATRAID for CC nitrogen-containing-bisphophonates (N-BPs) required for releasing N-BP CC molecules that have trafficked to lysosomes through fluid-phase CC endocytosis into the cytosol (PubMed:29745899). CC {ECO:0000269|PubMed:21723284, ECO:0000269|PubMed:29745899}. CC -!- SUBUNIT: Interacts with NELL1; the interaction promotes osteoblastic CC differentiation and mineralization. Interacts with SLC37A3; the CC interaction is direct and both proteins are mutually dependent for CC their stability (PubMed:29745899). {ECO:0000269|PubMed:21723284, CC ECO:0000269|PubMed:29745899}. CC -!- INTERACTION: CC Q6UW56; Q92832: NELL1; NbExp=4; IntAct=EBI-723802, EBI-947754; CC Q6UW56; Q9Y5X1: SNX9; NbExp=2; IntAct=EBI-723802, EBI-77848; CC Q6UW56-2; Q00013: MPP1; NbExp=3; IntAct=EBI-12830308, EBI-711788; CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:21723284}. CC Cell membrane {ECO:0000269|PubMed:17524364}; Single-pass membrane CC protein {ECO:0000269|PubMed:17524364}. Lysosome membrane CC {ECO:0000269|PubMed:29745899}; Multi-pass membrane protein CC {ECO:0000255}. Note=Colocalizes with NELL1 on the nuclear envelope and CC the perinuclear region (PubMed:21723284). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q6UW56-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6UW56-2; Sequence=VSP_014108; CC Name=3; CC IsoId=Q6UW56-3; Sequence=VSP_037521; CC -!- TISSUE SPECIFICITY: Weakly expressed in hematopoietic cell lines. CC {ECO:0000269|PubMed:11042152}. CC -!- INDUCTION: Up-regulated by all-trans-retinoic acid (ATRA) in several CC tumor cell lines. {ECO:0000269|PubMed:17524364}. CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing of isoform CC 1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative promoter usage. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD27770.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAD31317.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAD31317.2; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAH02846.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH11006.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH35850.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAX93173.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; 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; AB009017; BAF80618.1; -; mRNA. DR EMBL; AF144055; AAD31317.2; ALT_SEQ; mRNA. DR EMBL; AF275744; AAK69412.1; -; mRNA. DR EMBL; AF077037; AAD27770.1; ALT_FRAME; mRNA. DR EMBL; AY358968; AAQ89327.1; -; mRNA. DR EMBL; AK291894; BAF84583.1; -; mRNA. DR EMBL; CR600041; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AC013403; AAX93173.1; ALT_SEQ; Genomic_DNA. DR EMBL; CH471053; EAX00617.1; -; Genomic_DNA. DR EMBL; BC002846; AAH02846.2; ALT_INIT; mRNA. DR EMBL; BC011006; AAH11006.3; ALT_INIT; mRNA. DR EMBL; BC021237; AAH21237.1; -; mRNA. DR EMBL; BC035850; AAH35850.1; ALT_INIT; mRNA. DR CCDS; CCDS46243.1; -. [Q6UW56-2] DR CCDS; CCDS62877.1; -. [Q6UW56-1] DR RefSeq; NP_001164266.1; NM_001170795.1. [Q6UW56-1] DR RefSeq; NP_057169.2; NM_016085.4. [Q6UW56-2] DR RefSeq; NP_542159.3; NM_080592.3. DR AlphaFoldDB; Q6UW56; -. DR BioGRID; 119507; 10. DR IntAct; Q6UW56; 8. DR MINT; Q6UW56; -. DR STRING; 9606.ENSP00000484228; -. DR TCDB; 9.B.87.5.1; the selenoprotein p receptor (selp-receptor) family. DR GlyConnect; 1000; 4 N-Linked glycans (2 sites). DR GlyCosmos; Q6UW56; 4 sites, 4 glycans. DR GlyGen; Q6UW56; 6 sites, 4 N-linked glycans (2 sites), 1 O-linked glycan (2 sites). DR iPTMnet; Q6UW56; -. DR PhosphoSitePlus; Q6UW56; -. DR SwissPalm; Q6UW56; -. DR BioMuta; ATRAID; -. DR DMDM; 239938597; -. DR EPD; Q6UW56; -. DR jPOST; Q6UW56; -. DR MassIVE; Q6UW56; -. DR MaxQB; Q6UW56; -. DR PaxDb; 9606-ENSP00000484228; -. DR PeptideAtlas; Q6UW56; -. DR ProteomicsDB; 67447; -. [Q6UW56-1] DR ProteomicsDB; 67448; -. [Q6UW56-2] DR ProteomicsDB; 67449; -. [Q6UW56-3] DR Pumba; Q6UW56; -. DR Antibodypedia; 28263; 132 antibodies from 24 providers. DR DNASU; 51374; -. DR Ensembl; ENST00000380171.9; ENSP00000369518.4; ENSG00000138085.18. [Q6UW56-1] DR Ensembl; ENST00000405489.7; ENSP00000384033.3; ENSG00000138085.18. [Q6UW56-2] DR GeneID; 51374; -. DR KEGG; hsa:51374; -. DR MANE-Select; ENST00000380171.9; ENSP00000369518.4; NM_001170795.4; NP_001164266.1. DR UCSC; uc002rjf.5; human. [Q6UW56-1] DR AGR; HGNC:24090; -. DR CTD; 51374; -. DR DisGeNET; 51374; -. DR GeneCards; ATRAID; -. DR HGNC; HGNC:24090; ATRAID. DR HPA; ENSG00000138085; Low tissue specificity. DR MIM; 619682; gene. DR neXtProt; NX_Q6UW56; -. DR OpenTargets; ENSG00000138085; -. DR PharmGKB; PA134964154; -. DR VEuPathDB; HostDB:ENSG00000138085; -. DR eggNOG; ENOG502S1YR; Eukaryota. DR GeneTree; ENSGT00390000017252; -. DR HOGENOM; CLU_086391_0_0_1; -. DR InParanoid; Q6UW56; -. DR OMA; KMAPHGP; -. DR OrthoDB; 5361987at2759; -. DR PhylomeDB; Q6UW56; -. DR TreeFam; TF335766; -. DR PathwayCommons; Q6UW56; -. DR SignaLink; Q6UW56; -. DR BioGRID-ORCS; 51374; 9 hits in 1159 CRISPR screens. DR ChiTaRS; ATRAID; human. DR GeneWiki; C2orf28; -. DR GenomeRNAi; 51374; -. DR Pharos; Q6UW56; Tbio. DR PRO; PR:Q6UW56; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q6UW56; Protein. DR Bgee; ENSG00000138085; Expressed in type B pancreatic cell and 201 other cell types or tissues. DR ExpressionAtlas; Q6UW56; baseline and differential. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0033689; P:negative regulation of osteoblast proliferation; IDA:UniProtKB. DR GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:UniProtKB. DR GO; GO:0030501; P:positive regulation of bone mineralization; IDA:UniProtKB. DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:UniProtKB. DR GO; GO:0010468; P:regulation of gene expression; IDA:UniProtKB. DR GO; GO:0006855; P:xenobiotic transmembrane transport; IDA:UniProtKB. DR InterPro; IPR042350; ATRAID. DR InterPro; IPR000742; EGF-like_dom. DR PANTHER; PTHR15926; ALL-TRANS RETINOIC ACID-INDUCED DIFFERENTIATION FACTOR; 1. DR PANTHER; PTHR15926:SF1; ALL-TRANS RETINOIC ACID-INDUCED DIFFERENTIATION FACTOR; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 1. PE 1: Evidence at protein level; KW Alternative promoter usage; Alternative splicing; Cell membrane; KW Differentiation; Direct protein sequencing; Disulfide bond; KW EGF-like domain; Glycoprotein; Lysosome; Membrane; Nucleus; KW Reference proteome; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..30 FT /evidence="ECO:0000269|PubMed:15340161" FT CHAIN 31..229 FT /note="All-trans retinoic acid-induced differentiation FT factor" FT /id="PRO_0000020752" FT TOPO_DOM 31..199 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 200..220 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 221..229 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 152..193 FT /note="EGF-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT CARBOHYD 44 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 79 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 157 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 168 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 156..171 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 165..181 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DISULFID 183..192 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT VAR_SEQ 1..58 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10948432, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334, FT ECO:0000303|Ref.3" FT /id="VSP_014108" FT VAR_SEQ 1 FT /note="M -> MKTSAELHEQEKPPSSPRATGPGRLGHARGRGPDALRGGAAGPGRAS FT SGAPRERKM (in isoform 3)" FT /evidence="ECO:0000303|Ref.7" FT /id="VSP_037521" FT VARIANT 209 FT /note="A -> S (in dbSNP:rs7437)" FT /evidence="ECO:0000269|Ref.1" FT /id="VAR_057991" FT CONFLICT 5 FT /note="D -> G (in Ref. 1; BAF80618, 4; AAD27770, 5; FT AAQ89327 and 10; AAH02846/AAH11006/AAH35850)" FT /evidence="ECO:0000305" FT CONFLICT 33 FT /note="E -> EP (in Ref. 3; AAK69412)" FT /evidence="ECO:0000305" FT CONFLICT 219 FT /note="W -> S (in Ref. 1; BAF80618)" FT /evidence="ECO:0000305" FT CONFLICT 221 FT /note="T -> A (in Ref. 3; AAK69412)" FT /evidence="ECO:0000305" SQ SEQUENCE 229 AA; 24747 MW; CF051C5E886BCFF1 CRC64; MAPHDPGSLT TLVPWAAALL LALGVERALA LPEICTQCPG SVQNLSKVAF YCKTTRELML HARCCLNQKG TILGLDLQNC SLEDPGPNFH QAHTTVIIDL QANPLKGDLA NTFRGFTQLQ TLILPQHVNC PGGINAWNTI TSYIDNQICQ GQKNLCNNTG DPEMCPENGS CVPDGPGLLQ CVCADGFHGY KCMRQGSFSL LMFFGILGAT TLSVSILLWA TQRRKAKTS //