AEBP1_HUMAN
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 03-AUG-2022, entry version 165.
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};
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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; 3.
DR IntAct; Q8IUX7; 3.
DR STRING; 9606.ENSP00000223357; -.
DR MEROPS; M14.951; -.
DR GlyConnect; 995; 18 N-Linked glycans (3 sites).
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 EPD; Q8IUX7; -.
DR jPOST; Q8IUX7; -.
DR MassIVE; Q8IUX7; -.
DR MaxQB; Q8IUX7; -.
DR PaxDb; Q8IUX7; -.
DR PeptideAtlas; Q8IUX7; -.
DR PRIDE; Q8IUX7; -.
DR ProteomicsDB; 70626; -. [Q8IUX7-1]
DR ProteomicsDB; 70627; -. [Q8IUX7-2]
DR Antibodypedia; 4099; 198 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 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; PHYDDMD; -.
DR OrthoDB; 101221at2759; -.
DR PhylomeDB; Q8IUX7; -.
DR TreeFam; TF315592; -.
DR PathwayCommons; Q8IUX7; -.
DR SignaLink; Q8IUX7; -.
DR SIGNOR; Q8IUX7; -.
DR BioGRID-ORCS; 165; 14 hits in 1077 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 184 other tissues.
DR ExpressionAtlas; Q8IUX7; baseline and differential.
DR Genevisible; Q8IUX7; HS.
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:0004180; F:carboxypeptidase activity; IEA:Ensembl.
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: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:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:1904026; P:regulation of collagen fibril organization; IDA:UniProtKB.
DR CDD; cd00057; FA58C; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000834; Peptidase_M14.
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; SSF49464; 1.
DR SUPFAM; SSF49785; SSF49785; 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.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Cytoplasm; Disease variant;
KW DNA-binding; Ehlers-Danlos syndrome; Glycoprotein; Nucleus;
KW Reference proteome; Repressor; Secreted; Signal; Transcription;
KW 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 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
