PDLI2_HUMAN
ID PDLI2_HUMAN Reviewed; 352 AA.
AC Q96JY6; D3DSR5; J3KNH4; Q7Z584; Q86WM8; Q8WZ29; Q9H4L9; Q9H7I2;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=PDZ and LIM domain protein 2;
DE AltName: Full=PDZ-LIM protein mystique;
GN Name=PDLIM2; ORFNames=PP6345;
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 2).
RA Lau Y.M., Kotaka M., Chan A.H., Lee S.M.Y., Au C.C., Chim S.S.C.,
RA Kok L.D.S., Ng E.K.O., Siu S.S., Yiu S.W.H., Fung K.P., Waye M.M.Y.,
RA Tsui S.K.W., Lee C.Y.;
RT "Mystique, a PDZ-LIM protein with one carboxyl terminal LIM domain.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Hypothalamus;
RA Guo J.H., Zan Q., Yu L.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Shan Y.X., Yu L., Huang C.Q.;
RT "Cloning a novel protein containing PDZ and LIM domains.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Spleen;
RX PubMed=11214971; DOI=10.1093/dnares/7.6.357;
RA Hattori A., Okumura K., Nagase T., Kikuno R., Hirosawa M., Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen.";
RL DNA Res. 7:357-366(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, and Spleen;
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 GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Placenta;
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 FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-80; CYS-313 AND
RP CYS-316.
RX PubMed=15659642; DOI=10.1091/mbc.e04-12-1052;
RA Loughran G., Healy N., Kiely P.A., Huigsloot M., Kedersha N.L.,
RA O'connor R.;
RT "Mystique is a new IGF-I regulated PDZ-LIM domain protein that promotes
RT cell attachment and migration and suppresses anchorage independent
RT growth.";
RL Mol. Biol. Cell 16:1811-1822(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; THR-126; SER-129;
RP SER-137; SER-161 AND SER-197, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-82.
RG Structural genomics consortium (SGC);
RT "Structure of the PDZ domain of human PDLIM2 bound to a C-terminal
RT extension from human beta-tropomyosin.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Probable adapter protein located at the actin cytoskeleton
CC that promotes cell attachment. Necessary for the migratory capacity of
CC epithelial cells. Overexpression enhances cell adhesion to collagen and
CC fibronectin and suppresses anchorage independent growth. May contribute
CC to tumor cell migratory capacity. {ECO:0000269|PubMed:15659642}.
CC -!- SUBUNIT: Interacts with alpha-actinins ACTN1 and ACTN4, FLNA and MYH9
CC (By similarity). Interacts (via LIM zinc-binding domain) with MKRN2 (By
CC similarity). {ECO:0000250|UniProtKB:Q6AYD6,
CC ECO:0000250|UniProtKB:Q8R1G6}.
CC -!- INTERACTION:
CC Q96JY6; Q96AP0: ACD; NbExp=2; IntAct=EBI-9057264, EBI-717666;
CC Q96JY6; Q8IW36-1: ZNF695; NbExp=3; IntAct=EBI-9057264, EBI-18985109;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15659642}. Nucleus
CC {ECO:0000269|PubMed:15659642}. Note=May be partially nuclear.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton.
CC Note=Colocalizes with beta-1 integrin (ITGB1) and alpha-actinin but not
CC with paxillin (PXN).
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Mystique 2;
CC IsoId=Q96JY6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96JY6-2; Sequence=VSP_014058, VSP_014059;
CC Name=3; Synonyms=Mystique 1;
CC IsoId=Q96JY6-3; Sequence=VSP_014061;
CC Name=4; Synonyms=Mystique 3;
CC IsoId=Q96JY6-4; Sequence=VSP_014060;
CC Name=5;
CC IsoId=Q96JY6-5; Sequence=VSP_047113;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG16633.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAL55747.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAL65265.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB15788.1; 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; AY007729; AAG16633.1; ALT_FRAME; mRNA.
DR EMBL; AY070438; AAL65265.1; ALT_FRAME; mRNA.
DR EMBL; AY217349; AAO45102.1; -; mRNA.
DR EMBL; AF289563; AAL55747.1; ALT_FRAME; mRNA.
DR EMBL; AK024498; BAB15788.1; ALT_INIT; mRNA.
DR EMBL; AK027800; BAB55378.1; -; mRNA.
DR EMBL; AC037459; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471080; EAW63667.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63669.1; -; Genomic_DNA.
DR EMBL; BC021556; AAH21556.1; -; mRNA.
DR EMBL; BC071774; AAH71774.1; -; mRNA.
DR CCDS; CCDS34860.1; -. [Q96JY6-3]
DR CCDS; CCDS34861.1; -. [Q96JY6-4]
DR CCDS; CCDS6032.2; -. [Q96JY6-5]
DR RefSeq; NP_067643.3; NM_021630.5. [Q96JY6-5]
DR RefSeq; NP_789847.1; NM_176871.3. [Q96JY6-3]
DR RefSeq; NP_932159.1; NM_198042.3. [Q96JY6-4]
DR PDB; 2PA1; X-ray; 1.70 A; A=1-82.
DR PDB; 3PDV; X-ray; 2.20 A; A=1-83.
DR PDBsum; 2PA1; -.
DR PDBsum; 3PDV; -.
DR AlphaFoldDB; Q96JY6; -.
DR SMR; Q96JY6; -.
DR BioGRID; 122122; 22.
DR IntAct; Q96JY6; 13.
DR MINT; Q96JY6; -.
DR STRING; 9606.ENSP00000312634; -.
DR GlyGen; Q96JY6; 8 sites, 2 O-linked glycans (8 sites).
DR iPTMnet; Q96JY6; -.
DR PhosphoSitePlus; Q96JY6; -.
DR BioMuta; PDLIM2; -.
DR DMDM; 67461069; -.
DR EPD; Q96JY6; -.
DR jPOST; Q96JY6; -.
DR MassIVE; Q96JY6; -.
DR MaxQB; Q96JY6; -.
DR PaxDb; Q96JY6; -.
DR PeptideAtlas; Q96JY6; -.
DR PRIDE; Q96JY6; -.
DR ProteomicsDB; 77017; -. [Q96JY6-1]
DR ProteomicsDB; 77018; -. [Q96JY6-2]
DR ProteomicsDB; 77019; -. [Q96JY6-3]
DR ProteomicsDB; 77020; -. [Q96JY6-4]
DR Antibodypedia; 999; 265 antibodies from 27 providers.
DR DNASU; 64236; -.
DR Ensembl; ENST00000265810.8; ENSP00000265810.4; ENSG00000120913.24. [Q96JY6-3]
DR Ensembl; ENST00000308354.11; ENSP00000312634.7; ENSG00000120913.24. [Q96JY6-5]
DR Ensembl; ENST00000339162.11; ENSP00000342035.8; ENSG00000120913.24. [Q96JY6-5]
DR Ensembl; ENST00000397760.8; ENSP00000380867.4; ENSG00000120913.24. [Q96JY6-1]
DR Ensembl; ENST00000397761.6; ENSP00000380868.2; ENSG00000120913.24. [Q96JY6-1]
DR Ensembl; ENST00000409141.5; ENSP00000386868.1; ENSG00000120913.24. [Q96JY6-4]
DR Ensembl; ENST00000409417.5; ENSP00000387084.1; ENSG00000120913.24. [Q96JY6-1]
DR GeneID; 64236; -.
DR KEGG; hsa:64236; -.
DR MANE-Select; ENST00000409417.6; ENSP00000387084.1; NM_001368120.1; NP_001355049.1.
DR UCSC; uc003xby.5; human. [Q96JY6-1]
DR CTD; 64236; -.
DR DisGeNET; 64236; -.
DR GeneCards; PDLIM2; -.
DR HGNC; HGNC:13992; PDLIM2.
DR HPA; ENSG00000120913; Low tissue specificity.
DR MIM; 609722; gene.
DR neXtProt; NX_Q96JY6; -.
DR OpenTargets; ENSG00000120913; -.
DR PharmGKB; PA33159; -.
DR VEuPathDB; HostDB:ENSG00000120913; -.
DR eggNOG; KOG1703; Eukaryota.
DR GeneTree; ENSGT00940000160418; -.
DR InParanoid; Q96JY6; -.
DR OMA; HAVRIQE; -.
DR OrthoDB; 840552at2759; -.
DR PhylomeDB; Q96JY6; -.
DR TreeFam; TF106408; -.
DR PathwayCommons; Q96JY6; -.
DR SignaLink; Q96JY6; -.
DR BioGRID-ORCS; 64236; 12 hits in 1071 CRISPR screens.
DR ChiTaRS; PDLIM2; human.
DR EvolutionaryTrace; Q96JY6; -.
DR GeneWiki; PDLIM2; -.
DR GenomeRNAi; 64236; -.
DR Pharos; Q96JY6; Tbio.
DR PRO; PR:Q96JY6; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q96JY6; protein.
DR Bgee; ENSG00000120913; Expressed in spleen and 198 other tissues.
DR ExpressionAtlas; Q96JY6; baseline and differential.
DR Genevisible; Q96JY6; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0031005; F:filamin binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051371; F:muscle alpha-actinin binding; IBA:GO_Central.
DR GO; GO:0032036; F:myosin heavy chain binding; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0061061; P:muscle structure development; IBA:GO_Central.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR031847; DUF4749.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF15936; DUF4749; 1.
DR Pfam; PF00412; LIM; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00132; LIM; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton; LIM domain;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..352
FT /note="PDZ and LIM domain protein 2"
FT /id="PRO_0000075862"
FT DOMAIN 1..84
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 284..344
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 67..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 126
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1G6"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1G6"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1G6"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1G6"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYD6"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYD6"
FT VAR_SEQ 1
FT /note="M -> MRGGRARPAWESFMGLPPRSSAKWGAGQSLDRLCCAPGSRGLAGAPG
FT RMRAPPAGRSQPAGGPGDSLPHPPGGLGPGGSAWARRAEAAASRARGGGRGGPGITWAE
FT AGPGAPGGLSPESGRRQRERWRLPAFPPSRAWAPSRTGERQPGERAHLRLSARPALPGA
FT GLLSAPLSARNPGLVRGPAPWSLASAGAPPRAALSPAGALLLQPPARRVLCPRSEGGSR
FT TGRAGPSGWAPPRGARSAESTDRLKGM (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_047113"
FT VAR_SEQ 154..224
FT /note="SFQSLACSPGLPAADRLSYSGRPGSRQAGLGRAGDSAVLVLPPSPGPRSSRP
FT SMDSEGGSLLLDEDSEVFK -> RRPRPRWRLGGAGAAAFPGPSFLQAQHGLGRGKPPP
FT GRGLGSLQDAAGKSRGTGGPPTVQLLSALAGSPGG (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_014058"
FT VAR_SEQ 225..352
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_014059"
FT VAR_SEQ 256..352
FT /note="GTPAFLPSSLSPQSSLPASRALATPPKLHTCEKCSTSIANQAVRIQEGRYRH
FT PGCYTCADCGLNLKMRGHFWVGDELYCEKHARQRYSAPATLSSRA -> TRLCASRRAG
FT TATPAATPVPTVG (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_014060"
FT VAR_SEQ 328..352
FT /note="VGDELYCEKHARQRYSAPATLSSRA -> EDACAMEGMRLSLEALEGMVEGA
FT KRRDRRKTRRPIQPSW (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11214971,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_014061"
FT MUTAGEN 80
FT /note="L->K: Abolishes cell adhesion to collagen and
FT ability to suppress anchorage independent growth."
FT /evidence="ECO:0000269|PubMed:15659642"
FT MUTAGEN 313
FT /note="C->S: Abolishes ability to suppress anchorage
FT independent growth but not cell adhesion to collagen; when
FT associated with S-316."
FT /evidence="ECO:0000269|PubMed:15659642"
FT MUTAGEN 316
FT /note="C->S: Abolishes ability to suppress anchorage
FT independent growth but not cell adhesion to collagen; when
FT associated with S-313."
FT /evidence="ECO:0000269|PubMed:15659642"
FT CONFLICT 91
FT /note="T -> N (in Ref. 1; AAG16633)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="S -> F (in Ref. 1; AAG16633)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="A -> R (in Ref. 4; AAL55747)"
FT /evidence="ECO:0000305"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:2PA1"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:2PA1"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:2PA1"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:2PA1"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:2PA1"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:2PA1"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:2PA1"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:2PA1"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:2PA1"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:2PA1"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:2PA1"
SQ SEQUENCE 352 AA; 37459 MW; E36EC66C61C5E9DB CRC64;
MALTVDVAGP APWGFRITGG RDFHTPIMVT KVAERGKAKD ADLRPGDIIV AINGESAEGM
LHAEAQSKIR QSPSPLRLQL DRSQATSPGQ TNGDSSLEVL ATRFQGSVRT YTESQSSLRS
SYSSPTSLSP RAGSPFSPPP SSSSLTGEAA ISRSFQSLAC SPGLPAADRL SYSGRPGSRQ
AGLGRAGDSA VLVLPPSPGP RSSRPSMDSE GGSLLLDEDS EVFKMLQENR EGRAAPRQSS
SFRLLQEALE AEERGGTPAF LPSSLSPQSS LPASRALATP PKLHTCEKCS TSIANQAVRI
QEGRYRHPGC YTCADCGLNL KMRGHFWVGD ELYCEKHARQ RYSAPATLSS RA
