CHIO_HUMAN
ID CHIO_HUMAN Reviewed; 468 AA.
AC P52757; A4D1A2; B3VCF1; B3VCF2; B3VCF3; B3VCF7; B3VCG1; C9J7B0; E9PGE0;
AC F8QPL9; Q2M203; Q75MM2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Beta-chimaerin;
DE AltName: Full=Beta-chimerin;
DE AltName: Full=Rho GTPase-activating protein 3;
GN Name=CHN2; Synonyms=ARHGAP3, BCH;
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 BETA-2).
RC TISSUE=Cerebellum;
RX PubMed=8175705; DOI=10.1016/s0021-9258(18)99959-x;
RA Leung T., How B.-E., Manser E., Lim L.;
RT "Cerebellar beta 2-chimaerin, a GTPase-activating protein for p21 ras-
RT related rac is specifically expressed in granule cells and has a unique N-
RT terminal SH2 domain.";
RL J. Biol. Chem. 269:12888-12892(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-2).
RC TISSUE=Fetal brain;
RX PubMed=7614486;
RA Yuan S., Miller D.W., Barnett G.H., Hahn J.F., Williams B.R.G.;
RT "Identification and characterization of human beta 2-chimaerin: association
RT with malignant transformation in astrocytoma.";
RL Cancer Res. 55:3456-3461(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5; 6; 7 AND 8).
RA Barrio-Real L., Caloca M.J., Gonzalez-Sarmiento R.;
RT "Identification of new alternative splicing isoforms of beta chimaerin.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-3).
RA Zubeldia-Brenner L., Leskow F.C.;
RT "beta3-chimaerin, a novel Rac-GAP.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS BETA-2; 3 AND 4), AND
RP VARIANT ARG-204.
RC TISSUE=Caudate nucleus, Cerebellum, and Ileal mucosa;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-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 [10]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 7-466 IN COMPLEX WITH
RP PHORBOL-ESTER, AND ACTIVITY REGULATION.
RX PubMed=15507211; DOI=10.1016/j.cell.2004.10.012;
RA Canagarajah B., Leskow F.C., Ho J.Y., Mischak H., Saidi L.F.,
RA Kazanietz M.G., Hurley J.H.;
RT "Structural mechanism for lipid activation of the Rac-specific GAP, beta2-
RT chimaerin.";
RL Cell 119:407-418(2004).
CC -!- FUNCTION: GTPase-activating protein for p21-rac. Insufficient
CC expression of beta-2 chimaerin is expected to lead to higher Rac
CC activity and could therefore play a role in the progression from low-
CC grade to high-grade tumors.
CC -!- ACTIVITY REGULATION: In the inactive state, the N terminus protrudes
CC into the active site of the Rho-GAP domain, sterically blocking Rac
CC binding. Phospholipid binding to the Phorbol-ester/DAG-type zinc-
CC finger/C1 domain triggers the cooperative dissociation of these
CC interactions, allowing the N-terminus to move out of the active site
CC and thereby activating the enzyme. {ECO:0000269|PubMed:15507211}.
CC -!- INTERACTION:
CC P52757; Q8NFD2: ANKK1; NbExp=3; IntAct=EBI-714925, EBI-13280688;
CC P52757; P16333: NCK1; NbExp=3; IntAct=EBI-714925, EBI-389883;
CC P52757; O43639: NCK2; NbExp=6; IntAct=EBI-714925, EBI-713635;
CC P52757; P63000: RAC1; NbExp=4; IntAct=EBI-714925, EBI-413628;
CC P52757; Q96LD8: SENP8; NbExp=3; IntAct=EBI-714925, EBI-1041210;
CC P52757; Q8N9I8: SHF; NbExp=3; IntAct=EBI-714925, EBI-14328833;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=Beta-2;
CC IsoId=P52757-1; Sequence=Displayed;
CC Name=Beta-1;
CC IsoId=P52757-2; Sequence=Not described;
CC Name=3;
CC IsoId=P52757-3; Sequence=VSP_046271, VSP_046272;
CC Name=4; Synonyms=B1-CHNdel ex7p;
CC IsoId=P52757-4; Sequence=VSP_047600, VSP_047601;
CC Name=5; Synonyms=B1-CHNdel ex9;
CC IsoId=P52757-5; Sequence=VSP_046271, VSP_046272, VSP_047602;
CC Name=6; Synonyms=B1-CHNdel ex7p,11;
CC IsoId=P52757-6; Sequence=VSP_047600, VSP_047601, VSP_047603;
CC Name=7;
CC IsoId=P52757-7; Sequence=VSP_046271, VSP_046272, VSP_047603;
CC Name=8;
CC IsoId=P52757-8; Sequence=VSP_053323;
CC Name=Beta-3;
CC IsoId=P52757-9; Sequence=VSP_053679;
CC -!- TISSUE SPECIFICITY: Highest levels in the brain and pancreas. Also
CC expressed in the heart, placenta, and weakly in the kidney and liver.
CC Expression is much reduced in the malignant gliomas, compared to normal
CC brain or low-grade astrocytomas.
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; L29126; AAA19191.1; -; mRNA.
DR EMBL; U07223; AAA16836.1; -; mRNA.
DR EMBL; U28926; AAA86528.1; -; mRNA.
DR EMBL; EU732752; ACF04989.1; -; mRNA.
DR EMBL; EU732753; ACF04990.1; -; mRNA.
DR EMBL; EU732754; ACF04991.1; -; mRNA.
DR EMBL; EU732758; ACF04995.1; -; mRNA.
DR EMBL; EU732762; ACF04999.1; -; mRNA.
DR EMBL; GQ924106; ADK47390.1; -; mRNA.
DR EMBL; AK026415; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK313021; BAG35856.1; -; mRNA.
DR EMBL; AK316030; BAH14401.1; -; mRNA.
DR EMBL; AC004417; AAC06177.1; -; Genomic_DNA.
DR EMBL; AC004593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007255; AAS07498.1; -; Genomic_DNA.
DR EMBL; CH236948; EAL24205.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93919.1; -; Genomic_DNA.
DR EMBL; BC112155; AAI12156.1; -; mRNA.
DR CCDS; CCDS47566.1; -. [P52757-3]
DR CCDS; CCDS5420.1; -. [P52757-1]
DR CCDS; CCDS78219.1; -. [P52757-5]
DR PIR; A53764; A53764.
DR RefSeq; NP_001035025.1; NM_001039936.2. [P52757-3]
DR RefSeq; NP_001279998.1; NM_001293069.1. [P52757-9]
DR RefSeq; NP_001279999.1; NM_001293070.1.
DR RefSeq; NP_001280000.1; NM_001293071.1.
DR RefSeq; NP_001280002.1; NM_001293073.1. [P52757-4]
DR RefSeq; NP_001280004.1; NM_001293075.1. [P52757-6]
DR RefSeq; NP_001280005.1; NM_001293076.1. [P52757-5]
DR RefSeq; NP_001280006.1; NM_001293077.1.
DR RefSeq; NP_001280007.1; NM_001293078.1.
DR RefSeq; NP_001280008.1; NM_001293079.1.
DR RefSeq; NP_001280009.1; NM_001293080.1. [P52757-7]
DR RefSeq; NP_004058.1; NM_004067.3. [P52757-1]
DR PDB; 1XA6; X-ray; 3.20 A; A=7-468.
DR PDBsum; 1XA6; -.
DR AlphaFoldDB; P52757; -.
DR SMR; P52757; -.
DR BioGRID; 107548; 23.
DR IntAct; P52757; 18.
DR MINT; P52757; -.
DR STRING; 9606.ENSP00000222792; -.
DR BindingDB; P52757; -.
DR ChEMBL; CHEMBL4504; -.
DR iPTMnet; P52757; -.
DR PhosphoSitePlus; P52757; -.
DR BioMuta; CHN2; -.
DR DMDM; 2506455; -.
DR jPOST; P52757; -.
DR MassIVE; P52757; -.
DR MaxQB; P52757; -.
DR PaxDb; P52757; -.
DR PeptideAtlas; P52757; -.
DR PRIDE; P52757; -.
DR ProteomicsDB; 20301; -.
DR ProteomicsDB; 3840; -.
DR ProteomicsDB; 3841; -.
DR ProteomicsDB; 3842; -.
DR ProteomicsDB; 3843; -.
DR ProteomicsDB; 56529; -. [P52757-1]
DR Antibodypedia; 12544; 252 antibodies from 31 providers.
DR DNASU; 1124; -.
DR Ensembl; ENST00000222792.11; ENSP00000222792.7; ENSG00000106069.24. [P52757-1]
DR Ensembl; ENST00000412711.6; ENSP00000486515.1; ENSG00000106069.24. [P52757-3]
DR Ensembl; ENST00000421775.6; ENSP00000394284.2; ENSG00000106069.24. [P52757-5]
DR GeneID; 1124; -.
DR KEGG; hsa:1124; -.
DR MANE-Select; ENST00000222792.11; ENSP00000222792.7; NM_004067.4; NP_004058.1.
DR UCSC; uc003szz.4; human. [P52757-1]
DR CTD; 1124; -.
DR DisGeNET; 1124; -.
DR GeneCards; CHN2; -.
DR HGNC; HGNC:1944; CHN2.
DR HPA; ENSG00000106069; Tissue enhanced (brain, intestine).
DR MIM; 602857; gene.
DR neXtProt; NX_P52757; -.
DR OpenTargets; ENSG00000106069; -.
DR PharmGKB; PA26474; -.
DR VEuPathDB; HostDB:ENSG00000106069; -.
DR eggNOG; KOG1453; Eukaryota.
DR GeneTree; ENSGT01030000234635; -.
DR HOGENOM; CLU_015883_0_0_1; -.
DR InParanoid; P52757; -.
DR OMA; HCKTIFA; -.
DR OrthoDB; 1300981at2759; -.
DR PhylomeDB; P52757; -.
DR TreeFam; TF342052; -.
DR PathwayCommons; P52757; -.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR SignaLink; P52757; -.
DR SIGNOR; P52757; -.
DR BioGRID-ORCS; 1124; 10 hits in 1068 CRISPR screens.
DR ChiTaRS; CHN2; human.
DR EvolutionaryTrace; P52757; -.
DR GeneWiki; Chimerin_2; -.
DR GenomeRNAi; 1124; -.
DR Pharos; P52757; Tbio.
DR PRO; PR:P52757; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P52757; protein.
DR Bgee; ENSG00000106069; Expressed in cerebellum and 98 other tissues.
DR ExpressionAtlas; P52757; baseline and differential.
DR Genevisible; P52757; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00029; C1; 1.
DR CDD; cd04372; RhoGAP_chimaerin; 1.
DR CDD; cd10352; SH2_a2chimerin_b2chimerin; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035840; Chimaerin_SH2.
DR InterPro; IPR017356; CHN1/CHN2.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR037860; RhoGAP_chimaerin.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00017; SH2; 1.
DR PIRSF; PIRSF038015; N-chimaerin; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; GTPase activation; Membrane;
KW Metal-binding; Reference proteome; SH2 domain; Zinc; Zinc-finger.
FT CHAIN 1..468
FT /note="Beta-chimaerin"
FT /id="PRO_0000056697"
FT DOMAIN 59..127
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 277..468
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 214..264
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..56
FT /note="MAASSNSSLSGSSVSSDAEEYQPPIWKSYLYQLQQEAPRPKRIICPREVENR
FT PKYY -> MFSEELWLENEKKCAVVRKSKQGRKRQELLAVAFGVKVGVKGGFLWPPLKL
FT FACSQ (in isoform 3, isoform 5 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_046271"
FT VAR_SEQ 1..36
FT /note="MAASSNSSLSGSSVSSDAEEYQPPIWKSYLYQLQQE -> MFSEELWLENEK
FT KCAVVRKSKQGRKRQELLAVAFGV (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_047600"
FT VAR_SEQ 1..15
FT /note="MAASSNSSLSGSSVS -> MTQTHRAKSASSCPNLLVPETWPHQVSASHAGR
FT SKQPQGGILKINEEHRRGAIQDLLASPGFTFGKRVVFDSHCLKRQHTFADGLHSSCT
FT (in isoform Beta-3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_053679"
FT VAR_SEQ 37..217
FT /note="Missing (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_047601"
FT VAR_SEQ 49..192
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_053323"
FT VAR_SEQ 57..192
FT /note="Missing (in isoform 3, isoform 5 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_046272"
FT VAR_SEQ 247..304
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_047602"
FT VAR_SEQ 331..377
FT /note="DGEKADISANVYPDINIITGALKLYFRDLPIPVITYDTYSKFIDAAK -> E
FT (in isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_047603"
FT VARIANT 204
FT /note="H -> R (in dbSNP:rs3750103)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_022118"
FT VARIANT 438
FT /note="P -> S (in dbSNP:rs34971642)"
FT /id="VAR_049136"
FT CONFLICT 1..6
FT /note="MAASSN -> MRLL (in Ref. 1; AAA16836/AAA19191)"
FT /evidence="ECO:0000305"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:1XA6"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:1XA6"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:1XA6"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1XA6"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1XA6"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:1XA6"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:1XA6"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:1XA6"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1XA6"
FT HELIX 125..138
FT /evidence="ECO:0007829|PDB:1XA6"
FT HELIX 141..146
FT /evidence="ECO:0007829|PDB:1XA6"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:1XA6"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:1XA6"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:1XA6"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:1XA6"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:1XA6"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:1XA6"
FT TURN 266..269
FT /evidence="ECO:0007829|PDB:1XA6"
FT HELIX 279..286
FT /evidence="ECO:0007829|PDB:1XA6"
FT HELIX 292..303
FT /evidence="ECO:0007829|PDB:1XA6"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:1XA6"
FT TURN 309..313
FT /evidence="ECO:0007829|PDB:1XA6"
FT HELIX 318..328
FT /evidence="ECO:0007829|PDB:1XA6"
FT TURN 331..334
FT /evidence="ECO:0007829|PDB:1XA6"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:1XA6"
FT HELIX 346..358
FT /evidence="ECO:0007829|PDB:1XA6"
FT HELIX 369..373
FT /evidence="ECO:0007829|PDB:1XA6"
FT TURN 374..377
FT /evidence="ECO:0007829|PDB:1XA6"
FT HELIX 381..392
FT /evidence="ECO:0007829|PDB:1XA6"
FT HELIX 397..405
FT /evidence="ECO:0007829|PDB:1XA6"
FT TURN 406..410
FT /evidence="ECO:0007829|PDB:1XA6"
FT HELIX 411..414
FT /evidence="ECO:0007829|PDB:1XA6"
FT TURN 415..419
FT /evidence="ECO:0007829|PDB:1XA6"
FT HELIX 424..431
FT /evidence="ECO:0007829|PDB:1XA6"
FT TURN 432..434
FT /evidence="ECO:0007829|PDB:1XA6"
FT HELIX 445..448
FT /evidence="ECO:0007829|PDB:1XA6"
FT HELIX 450..462
FT /evidence="ECO:0007829|PDB:1XA6"
FT HELIX 464..467
FT /evidence="ECO:0007829|PDB:1XA6"
SQ SEQUENCE 468 AA; 53924 MW; 63254958E0B5804C CRC64;
MAASSNSSLS GSSVSSDAEE YQPPIWKSYL YQLQQEAPRP KRIICPREVE NRPKYYGREF
HGIISREQAD ELLGGVEGAY ILRESQRQPG CYTLALRFGN QTLNYRLFHD GKHFVGEKRF
ESIHDLVTDG LITLYIETKA AEYISKMTTN PIYEHIGYAT LLREKVSRRL SRSKNEPRKT
NVTHEEHTAV EKISSLVRRA ALTHNDNHFN YEKTHNFKVH TFRGPHWCEY CANFMWGLIA
QGVRCSDCGL NVHKQCSKHV PNDCQPDLKR IKKVYCCDLT TLVKAHNTQR PMVVDICIRE
IEARGLKSEG LYRVSGFTEH IEDVKMAFDR DGEKADISAN VYPDINIITG ALKLYFRDLP
IPVITYDTYS KFIDAAKISN ADERLEAVHE VLMLLPPAHY ETLRYLMIHL KKVTMNEKDN
FMNAENLGIV FGPTLMRPPE DSTLTTLHDM RYQKLIVQIL IENEDVLF
