ID AEBP1_HUMAN Reviewed; 1158 AA. AC Q8IUX7; Q14113; Q59ER7; Q6ZSC7; Q7KZ79; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 02-OCT-2024, entry version 176. DE RecName: Full=Adipocyte enhancer-binding protein 1; DE Short=AE-binding protein 1; DE AltName: Full=Aortic carboxypeptidase-like protein; DE Flags: Precursor; GN Name=AEBP1; Synonyms=ACLP; 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). RC TISSUE=Aortic smooth muscle; RX PubMed=9624159; DOI=10.1074/jbc.273.25.15654; RA Layne M.D., Endege W.O., Jain M.K., Yet S.-F., Hsieh C.-M., Chin M.T., RA Perrella M.A., Blanar M.A., Haber E., Lee M.-E.; RT "Aortic carboxypeptidase-like protein, a novel protein with discoidin and RT carboxypeptidase-like domains, is up-regulated during vascular smooth RT muscle cell differentiation."; RL J. Biol. Chem. 273:15654-15660(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-1133. RC TISSUE=Aortic endothelium; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 314-1158 (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Cancellous bone; RX PubMed=8920928; DOI=10.1006/bbrc.1996.1675; RA Ohno I., Hashimoto J., Shimizu K., Takaoka K., Ochi T., Matsubara K., RA Okubo K.; RT "A cDNA cloning of human AEBP1 from primary cultured osteoblasts and its RT expression in a differentiating osteoblastic cell line."; RL Biochem. Biophys. Res. Commun. 228:411-414(1996). RN [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-528 AND ASN-922. 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 [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [10] RP INVOLVEMENT IN EDSCLL2. RX PubMed=27023906; DOI=10.1007/s00439-016-1660-z; RA Alazami A.M., Al-Qattan S.M., Faqeih E., Alhashem A., Alshammari M., RA Alzahrani F., Al-Dosari M.S., Patel N., Alsagheir A., Binabbas B., RA Alzaidan H., Alsiddiky A., Alharbi N., Alfadhel M., Kentab A., Daza R.M., RA Kircher M., Shendure J., Hashem M., Alshahrani S., Rahbeeni Z., Khalifa O., RA Shaheen R., Alkuraya F.S.; RT "Expanding the clinical and genetic heterogeneity of hereditary disorders RT of connective tissue."; RL Hum. Genet. 135:525-540(2016). RN [11] RP FUNCTION, INTERACTION WITH COLLAGEN, DOMAIN, INVOLVEMENT IN EDSCLL2, AND RP VARIANT EDSCLL2 581-CYS--PHE-1158 DEL. RX PubMed=29606302; DOI=10.1016/j.ajhg.2018.02.018; RA Blackburn P.R., Xu Z., Tumelty K.E., Zhao R.W., Monis W.J., Harris K.G., RA Gass J.M., Cousin M.A., Boczek N.J., Mitkov M.V., Cappel M.A., RA Francomano C.A., Parisi J.E., Klee E.W., Faqeih E., Alkuraya F.S., RA Layne M.D., McDonnell N.B., Atwal P.S.; RT "Bi-allelic alterations in AEBP1 lead to defective collagen assembly and RT connective tissue structure resulting in a variant of Ehlers-Danlos RT syndrome."; RL Am. J. Hum. Genet. 102:696-705(2018). CC -!- FUNCTION: [Isoform 1]: As a positive regulator of collagen CC fibrillogenesis, it is probably involved in the organization and CC remodeling of the extracellular matrix. {ECO:0000269|PubMed:29606302}. CC -!- FUNCTION: [Isoform 2]: May positively regulate MAP-kinase activity in CC adipocytes, leading to enhanced adipocyte proliferation and reduced CC adipocyte differentiation. May also positively regulate NF-kappa-B CC activity in macrophages by promoting the phosphorylation and subsequent CC degradation of I-kappa-B-alpha (NFKBIA), leading to enhanced macrophage CC inflammatory responsiveness. Can act as a transcriptional repressor. CC {ECO:0000250|UniProtKB:Q640N1}. CC -!- SUBUNIT: Isoform 1: Interacts with different types of collagen, CC including collagens I, III, and V (PubMed:29606302). Isoform 2: CC Interacts with GNG5, NFKBIA, MAPK1, MAPK3 and PTEN. Interaction with CC MAPK1 may stimulate DNA-binding. May interact with calmodulin. Binds to CC DNA in vitro. {ECO:0000250|UniProtKB:Q640N1, CC ECO:0000269|PubMed:29606302}. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted CC {ECO:0000250|UniProtKB:Q640N1}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm CC {ECO:0000250|UniProtKB:Q640N1}. Nucleus {ECO:0000250|UniProtKB:Q640N1}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8IUX7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8IUX7-2; Sequence=VSP_033467, VSP_033468, VSP_033469; CC -!- TISSUE SPECIFICITY: Expressed in osteoblast and visceral fat. CC {ECO:0000269|PubMed:8920928}. CC -!- DOMAIN: [Isoform 1]: The F5/8 type C domain binds to different types of CC collagen, including collagens I, III, and V. CC {ECO:0000269|PubMed:29606302}. CC -!- PTM: Phosphorylated by MAPK1 in vitro. {ECO:0000250}. CC -!- DISEASE: Ehlers-Danlos syndrome, classic-like, 2 (EDSCLL2) CC [MIM:618000]: A variant form of Ehlers-Danlos syndrome, a connective CC tissue disorder. EDSCLL2 patients show severe joint and skin laxity, CC osteoporosis affecting the hips and spine, osteoarthritis, soft CC redundant skin that can be acrogeria-like, delayed wound healing with CC abnormal atrophic scarring, and shoulder, hip, knee, and ankle CC dislocations. Additional variable features include gastrointestinal and CC genitourinary manifestations (bowel rupture, gut dysmotility, CC cryptorchidism, and hernias), vascular complications (mitral valve CC prolapse and aortic root dilation), and skeletal anomalies. EDSCLL2 CC inheritance is autosomal recessive. {ECO:0000269|PubMed:27023906, CC ECO:0000269|PubMed:29606302}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}. CC -!- CAUTION: Although related to peptidase M14 family, lacks the active CC site residues and zinc-binding sites, suggesting that it has no CC carboxypeptidase activity. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD92981.1; Type=Erroneous initiation; 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; AF053944; AAC25585.1; -; mRNA. DR EMBL; AK127541; BAC87026.1; -; mRNA. DR EMBL; AB209744; BAD92981.1; ALT_INIT; mRNA. DR EMBL; CH236960; EAL23768.1; -; Genomic_DNA. DR EMBL; CH471128; EAW61119.1; -; Genomic_DNA. DR EMBL; BC038588; AAH38588.1; -; mRNA. DR EMBL; D86479; BAA13094.1; -; mRNA. DR CCDS; CCDS5476.1; -. [Q8IUX7-1] DR PIR; JC5256; JC5256. DR RefSeq; NP_001120.3; NM_001129.4. [Q8IUX7-1] DR AlphaFoldDB; Q8IUX7; -. DR SMR; Q8IUX7; -. DR BioGRID; 106674; 6. DR IntAct; Q8IUX7; 3. DR STRING; 9606.ENSP00000223357; -. DR MEROPS; M14.951; -. DR GlyConnect; 995; 18 N-Linked glycans (3 sites). DR GlyCosmos; Q8IUX7; 15 sites, 22 glycans. DR GlyGen; Q8IUX7; 15 sites, 18 N-linked glycans (3 sites), 4 O-linked glycans (12 sites). DR iPTMnet; Q8IUX7; -. DR PhosphoSitePlus; Q8IUX7; -. DR BioMuta; AEBP1; -. DR DMDM; 74728002; -. DR jPOST; Q8IUX7; -. DR MassIVE; Q8IUX7; -. DR PaxDb; 9606-ENSP00000223357; -. DR PeptideAtlas; Q8IUX7; -. DR ProteomicsDB; 70626; -. [Q8IUX7-1] DR ProteomicsDB; 70627; -. [Q8IUX7-2] DR Antibodypedia; 4099; 207 antibodies from 29 providers. DR DNASU; 165; -. DR Ensembl; ENST00000223357.8; ENSP00000223357.3; ENSG00000106624.11. [Q8IUX7-1] DR Ensembl; ENST00000450684.2; ENSP00000398878.2; ENSG00000106624.11. [Q8IUX7-2] DR GeneID; 165; -. DR KEGG; hsa:165; -. DR MANE-Select; ENST00000223357.8; ENSP00000223357.3; NM_001129.5; NP_001120.3. DR UCSC; uc003tkb.5; human. [Q8IUX7-1] DR AGR; HGNC:303; -. DR CTD; 165; -. DR DisGeNET; 165; -. DR GeneCards; AEBP1; -. DR HGNC; HGNC:303; AEBP1. DR HPA; ENSG00000106624; Low tissue specificity. DR MalaCards; AEBP1; -. DR MIM; 602981; gene. DR MIM; 618000; phenotype. DR neXtProt; NX_Q8IUX7; -. DR OpenTargets; ENSG00000106624; -. DR Orphanet; 536532; Classical-like Ehlers-Danlos syndrome type 2. DR PharmGKB; PA24604; -. DR VEuPathDB; HostDB:ENSG00000106624; -. DR eggNOG; KOG2649; Eukaryota. DR GeneTree; ENSGT00940000158323; -. DR HOGENOM; CLU_006722_0_1_1; -. DR InParanoid; Q8IUX7; -. DR OMA; YIRRQKR; -. DR OrthoDB; 5490979at2759; -. DR PhylomeDB; Q8IUX7; -. DR TreeFam; TF315592; -. DR PathwayCommons; Q8IUX7; -. DR SignaLink; Q8IUX7; -. DR SIGNOR; Q8IUX7; -. DR BioGRID-ORCS; 165; 15 hits in 1158 CRISPR screens. DR ChiTaRS; AEBP1; human. DR GenomeRNAi; 165; -. DR Pharos; Q8IUX7; Tbio. DR PRO; PR:Q8IUX7; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q8IUX7; protein. DR Bgee; ENSG00000106624; Expressed in tendon of biceps brachii and 186 other cell types or tissues. DR ExpressionAtlas; Q8IUX7; baseline and differential. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL. DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR GO; GO:0005518; F:collagen binding; IDA:UniProtKB. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:NTNU_SB. DR GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central. DR GO; GO:0016485; P:protein processing; IBA:GO_Central. DR GO; GO:1904026; P:regulation of collagen fibril organization; IDA:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR CDD; cd00057; FA58C; 1. DR CDD; cd11308; Peptidase_M14NE-CP-C_like; 1. DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 1. DR InterPro; IPR008969; CarboxyPept-like_regulatory. DR InterPro; IPR000421; FA58C. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR000834; Peptidase_M14. DR InterPro; IPR050753; Peptidase_M14_domain. DR PANTHER; PTHR11532:SF48; ADIPOCYTE ENHANCER-BINDING PROTEIN 1; 1. DR PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1. DR Pfam; PF13620; CarboxypepD_reg; 1. DR Pfam; PF00754; F5_F8_type_C; 1. DR Pfam; PF00246; Peptidase_M14; 1. DR PRINTS; PR00765; CRBOXYPTASEA. DR SMART; SM00231; FA58C; 1. DR SMART; SM00631; Zn_pept; 1. DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1. DR SUPFAM; SSF49785; Galactose-binding domain-like; 1. DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1. DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1. DR PROSITE; PS01285; FA58C_1; 1. DR PROSITE; PS01286; FA58C_2; 1. DR PROSITE; PS50022; FA58C_3; 1. DR PROSITE; PS52035; PEPTIDASE_M14; 1. PE 1: Evidence at protein level; KW Alternative splicing; Calmodulin-binding; Cytoplasm; Disease variant; KW DNA-binding; Ehlers-Danlos syndrome; Glycoprotein; Nucleus; KW Proteomics identification; Reference proteome; Repressor; Secreted; Signal; KW Transcription; Transcription regulation. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT CHAIN 26..1158 FT /note="Adipocyte enhancer-binding protein 1" FT /id="PRO_0000333189" FT DOMAIN 383..540 FT /note="F5/8 type C" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081" FT DOMAIN 563..904 FT /note="Peptidase M14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01379" FT REGION 40..387 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 390..555 FT /note="Required for DNA-binding and interaction with FT NFKBIA" FT /evidence="ECO:0000250" FT REGION 421..624 FT /note="Interaction with MAPK1 and MAPK3" FT /evidence="ECO:0000250" FT REGION 555..985 FT /note="Interaction with PTEN" FT /evidence="ECO:0000250" FT REGION 941..1158 FT /note="Required for transcriptional repression" FT /evidence="ECO:0000250" FT REGION 1006..1158 FT /note="Interaction with MAPK1 and MAPK3" FT /evidence="ECO:0000250" FT REGION 1108..1141 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 43..58 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 84..162 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 164..194 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 212..227 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 234..283 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 284..303 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 327..387 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1112..1136 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 528 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 922 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT VAR_SEQ 1..457 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_033467" FT VAR_SEQ 458..495 FT /note="ITQGRDSSIHDDFVTTFFVGFSNDSQTWVMYTNGYEEM -> MRKWWAPCPG FT SWLCSHCLGEGWALRGAGSTALRPASPQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_033468" FT VAR_SEQ 543..544 FT /note="AP -> ARECGGLAGALSGGGVLGWASRHPAKDNPASLAA (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_033469" FT VARIANT 273 FT /note="P -> T (in dbSNP:rs2537188)" FT /id="VAR_043118" FT VARIANT 581..1158 FT /note="Missing (in EDSCLL2)" FT /evidence="ECO:0000269|PubMed:29606302" FT /id="VAR_080664" FT VARIANT 648 FT /note="D -> E (in dbSNP:rs11770649)" FT /id="VAR_043119" FT VARIANT 1001 FT /note="P -> L (in dbSNP:rs4724285)" FT /id="VAR_043120" FT VARIANT 1133 FT /note="K -> E (in dbSNP:rs13928)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_043121" FT VARIANT 1148 FT /note="V -> I (in dbSNP:rs13898)" FT /id="VAR_043122" FT CONFLICT 145 FT /note="K -> E (in Ref. 1; AAC25585)" FT /evidence="ECO:0000305" FT CONFLICT 218 FT /note="R -> Q (in Ref. 1; AAC25585)" FT /evidence="ECO:0000305" FT CONFLICT 569 FT /note="D -> G (in Ref. 2; BAC87026)" FT /evidence="ECO:0000305" FT CONFLICT 715 FT /note="R -> G (in Ref. 2; BAC87026)" FT /evidence="ECO:0000305" FT CONFLICT 884 FT /note="S -> G (in Ref. 2; BAC87026)" FT /evidence="ECO:0000305" FT CONFLICT 1079 FT /note="E -> G (in Ref. 3; BAD92981)" FT /evidence="ECO:0000305" SQ SEQUENCE 1158 AA; 130929 MW; 1D7F4A20451646AE CRC64; MAAVRGAPLL SCLLALLALC PGGRPQTVLT DDEIEEFLEG FLSELEPEPR EDDVEAPPPP EPTPRVRKAQ AGGKPGKRPG TAAEVPPEKT KDKGKKGKKD KGPKVPKESL EGSPRPPKKG KEKPPKATKK PKEKPPKATK KPKEKPPKAT KKPKEKPPKA TKKPPSGKRP PILAPSETLE WPLPPPPSPG PEELPQEGGA PLSNNWQNPG EETHVEAREH QPEPEEETEQ PTLDYNDQIE REDYEDFEYI RRQKQPRPPP SRRRRPERVW PEPPEEKAPA PAPEERIEPP VKPLLPPLPP DYGDGYVIPN YDDMDYYFGP PPPQKPDAER QTDEEKEELK KPKKEDSSPK EETDKWAVEK GKDHKEPRKG EELEEEWTPT EKVKCPPIGM ESHRIEDNQI RASSMLRHGL GAQRGRLNMQ TGATEDDYYD GAWCAEDDAR TQWIEVDTRR TTRFTGVITQ GRDSSIHDDF VTTFFVGFSN DSQTWVMYTN GYEEMTFHGN VDKDTPVLSE LPEPVVARFI RIYPLTWNGS LCMRLEVLGC SVAPVYSYYA QNEVVATDDL DFRHHSYKDM RQLMKVVNEE CPTITRTYSL GKSSRGLKIY AMEISDNPGE HELGEPEFRY TAGIHGNEVL GRELLLLLMQ YLCREYRDGN PRVRSLVQDT RIHLVPSLNP DGYEVAAQMG SEFGNWALGL WTEEGFDIFE DFPDLNSVLW GAEERKWVPY RVPNNNLPIP ERYLSPDATV STEVRAIIAW MEKNPFVLGA NLNGGERLVS YPYDMARTPT QEQLLAAAMA AARGEDEDEV SEAQETPDHA IFRWLAISFA SAHLTLTEPY RGGCQAQDYT GGMGIVNGAK WNPRTGTIND FSYLHTNCLE LSFYLGCDKF PHESELPREW ENNKEALLTF MEQVHRGIKG VVTDEQGIPI ANATISVSGI NHGVKTASGG DYWRILNPGE YRVTAHAEGY TPSAKTCNVD YDIGATQCNF ILARSNWKRI REIMAMNGNR PIPHIDPSRP MTPQQRRLQQ RRLQHRLRLR AQMRLRRLNA TTTLGPHTVP PTLPPAPATT LSTTIEPWGL IPPTTAGWEE SETETYTEVV TEFGTEVEPE FGTKVEPEFE TQLEPEFETQ LEPEFEEEEE EEKEEEIATG QAFPFTTVET YTVNFGDF //