GSKIP_HUMAN
ID GSKIP_HUMAN Reviewed; 139 AA.
AC Q9P0R6; B3KSZ0; Q9BST1; Q9NWK0;
DT 09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 09-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=GSK3B-interacting protein {ECO:0000312|HGNC:HGNC:20343};
DE Short=GSKIP {ECO:0000303|PubMed:16981698};
DE AltName: Full=GSK3beta interaction protein {ECO:0000312|HGNC:HGNC:20343};
GN Name=GSKIP {ECO:0000303|PubMed:16981698, ECO:0000312|HGNC:HGNC:20343};
GN Synonyms=C14orf129 {ECO:0000312|HGNC:HGNC:20343}; ORFNames=HSPC210;
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 [LARGE SCALE MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala, and Colon;
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 GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP INTERACTION WITH GSK3B, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-109;
RP THR-113; SER-115 AND LEU-130, TISSUE SPECIFICITY, FUNCTION, AND REGION.
RX PubMed=16981698; DOI=10.1021/bi061147r;
RA Chou H.-Y., Howng S.-L., Cheng T.-S., Hsiao Y.-L., Lieu A.-S., Loh J.-K.,
RA Hwang S.-L., Lin C.-C., Hsu C.-M., Wang C., Lee C.-I., Lu P.-J.,
RA Chou C.-K., Huang C.-Y., Hong Y.-R.;
RT "GSKIP is homologous to the axin GSK3beta interaction domain and functions
RT as a negative regulator of GSK3beta.";
RL Biochemistry 45:11379-11389(2006).
RN [7]
RP FUNCTION.
RX PubMed=19830702; DOI=10.1002/jcb.22362;
RA Lin C.C., Chou C.H., Howng S.L., Hsu C.Y., Hwang C.C., Wang C., Hsu C.M.,
RA Hong Y.R.;
RT "GSKIP, an inhibitor of GSK3beta, mediates the N-cadherin/beta-catenin pool
RT in the differentiation of SH-SY5Y cells.";
RL J. Cell. Biochem. 108:1325-1336(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PRKAR2A; PRKAR2B AND
RP GSK3B, AND SUBCELLULAR LOCATION.
RX PubMed=20007971; DOI=10.1074/jbc.m109.047944;
RA Hundsrucker C., Skroblin P., Christian F., Zenn H.M., Popara V., Joshi M.,
RA Eichhorst J., Wiesner B., Herberg F.W., Reif B., Rosenthal W.,
RA Klussmann E.;
RT "Glycogen synthase kinase 3beta interaction protein functions as an A-
RT kinase anchoring protein.";
RL J. Biol. Chem. 285:5507-5521(2010).
RN [9]
RP INTERACTION WITH PRKAR2B AND GSK3B, MUTAGENESIS OF 41-VAL--LEU-45 AND
RP LEU-130, FUNCTION, AND REGION.
RX PubMed=25920809; DOI=10.1016/j.bbamcr.2015.04.013;
RA Loh J.K., Lin C.C., Yang M.C., Chou C.H., Chen W.S., Hong M.C., Cho C.L.,
RA Hsu C.M., Cheng J.T., Chou A.K., Chang C.H., Tseng C.N., Wang C.H.,
RA Lieu A.S., Howng S.L., Hong Y.R.;
RT "GSKIP- and GSK3-mediated anchoring strengthens cAMP/PKA/Drp1 axis
RT signaling in the regulation of mitochondrial elongation.";
RL Biochim. Biophys. Acta 1853:1796-1807(2015).
RN [10]
RP FUNCTION, MUTAGENESIS OF ASN-42 AND LEU-130, AND INTERACTION WITH PRKAR2A
RP AND GSK3B.
RX PubMed=27484798; DOI=10.1074/jbc.m116.738047;
RA Dema A., Schroeter M.F., Perets E., Skroblin P., Moutty M.C., Deak V.A.,
RA Birchmeier W., Klussmann E.;
RT "The A-Kinase Anchoring Protein (AKAP) Glycogen Synthase Kinase 3beta
RT Interaction Protein (GSKIP) Regulates beta-Catenin through Its Interactions
RT with Both Protein Kinase A (PKA) and GSK3beta.";
RL J. Biol. Chem. 291:19618-19630(2016).
RN [11]
RP STRUCTURE BY NMR.
RG Northeast structural genomics consortium (NESG);
RT "NMR structure of the human C14orf129 gene product, HSPC210. Northeast
RT structural genomics target HR969.";
RL Submitted (JAN-2005) to the PDB data bank.
CC -!- FUNCTION: A-kinase anchoring protein for GSK3B and PKA that regulates
CC or facilitates their kinase activity towards their targets
CC (PubMed:27484798, PubMed:25920809, PubMed:16981698). The ternary
CC complex enhances Wnt-induced signaling by facilitating the GSK3B- and
CC PKA-induced phosphorylation of beta-catenin leading to beta-catenin
CC degradation and stabilization respectively (PubMed:27484798,
CC PubMed:16981698). Upon cAMP activation, the ternary complex contributes
CC to neuroprotection against oxidative stress-induced apoptosis by
CC facilitating the PKA-induced phosphorylation of DML1 and PKA-induced
CC inactivation of GSK3B (PubMed:25920809). During neurite outgrowth
CC promotes neuron proliferation; while increases beta-catenin-induced
CC transcriptional activity through GSK3B kinase activity inhibition,
CC reduces N-cadherin level to promote cell cycle progression
CC (PubMed:19830702). {ECO:0000269|PubMed:16981698,
CC ECO:0000269|PubMed:19830702, ECO:0000269|PubMed:25920809,
CC ECO:0000269|PubMed:27484798}.
CC -!- SUBUNIT: Forms a complex composed of PRKAR2A or PRKAR2B, GSK3B and
CC GSKIP through GSKIP interaction; facilitates PKA-induced
CC phosphorylation of GSK3B leading to GSK3B inactivation; recruits DNM1L
CC through GSK3B for PKA-mediated phosphorylation of DNM1L; promotes beta-
CC catenin degradation through GSK3B-induced phosphorylation of beta-
CC catenin; stabilizes beta-catenin and enhances Wnt-induced signaling
CC through PKA-induced phosphorylation of beta-catenin (PubMed:20007971,
CC PubMed:25920809, PubMed:27484798). Interacts with GSK3B; induces GSK3B-
CC mediated phosphorylation of GSKIP and inhibits GSK3B kinase activity
CC (PubMed:16981698, PubMed:25920809). {ECO:0000269|PubMed:16981698,
CC ECO:0000269|PubMed:20007971, ECO:0000269|PubMed:25920809,
CC ECO:0000269|PubMed:27484798}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16981698,
CC ECO:0000269|PubMed:20007971}. Nucleus {ECO:0000269|PubMed:20007971}.
CC -!- TISSUE SPECIFICITY: Detected in heart, brain, placenta, liver, skeletal
CC muscle, kidney, testis, lung and pancreas.
CC {ECO:0000269|PubMed:16981698}.
CC -!- PTM: Phosphorylated by GSK3B. {ECO:0000269|PubMed:16981698}.
CC -!- SIMILARITY: Belongs to the GSKIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF36130.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF151044; AAF36130.1; ALT_FRAME; mRNA.
DR EMBL; AK000796; BAA91380.1; -; mRNA.
DR EMBL; AK094654; BAG52902.1; -; mRNA.
DR EMBL; AL359240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81634.1; -; Genomic_DNA.
DR EMBL; BC004818; AAH04818.1; -; mRNA.
DR CCDS; CCDS32153.1; -.
DR RefSeq; NP_001258833.1; NM_001271904.1.
DR RefSeq; NP_001258834.1; NM_001271905.1.
DR RefSeq; NP_001258835.1; NM_001271906.1.
DR RefSeq; NP_057556.2; NM_016472.4.
DR RefSeq; XP_016876854.1; XM_017021365.1.
DR PDB; 1SGO; NMR; -; A=1-139.
DR PDBsum; 1SGO; -.
DR AlphaFoldDB; Q9P0R6; -.
DR BMRB; Q9P0R6; -.
DR SMR; Q9P0R6; -.
DR BioGRID; 119589; 19.
DR CORUM; Q9P0R6; -.
DR IntAct; Q9P0R6; 5.
DR MINT; Q9P0R6; -.
DR STRING; 9606.ENSP00000451188; -.
DR BioMuta; GSKIP; -.
DR DMDM; 34582343; -.
DR EPD; Q9P0R6; -.
DR jPOST; Q9P0R6; -.
DR MassIVE; Q9P0R6; -.
DR MaxQB; Q9P0R6; -.
DR PaxDb; Q9P0R6; -.
DR PeptideAtlas; Q9P0R6; -.
DR PRIDE; Q9P0R6; -.
DR ProteomicsDB; 83591; -.
DR Antibodypedia; 27335; 86 antibodies from 18 providers.
DR DNASU; 51527; -.
DR Ensembl; ENST00000438650.5; ENSP00000412315.1; ENSG00000100744.15.
DR Ensembl; ENST00000554182.5; ENSP00000451384.1; ENSG00000100744.15.
DR Ensembl; ENST00000555181.6; ENSP00000450420.1; ENSG00000100744.15.
DR Ensembl; ENST00000556095.5; ENSP00000451188.1; ENSG00000100744.15.
DR GeneID; 51527; -.
DR KEGG; hsa:51527; -.
DR MANE-Select; ENST00000555181.6; ENSP00000450420.1; NM_016472.5; NP_057556.2.
DR UCSC; uc001yfj.6; human.
DR CTD; 51527; -.
DR DisGeNET; 51527; -.
DR GeneCards; GSKIP; -.
DR HGNC; HGNC:20343; GSKIP.
DR HPA; ENSG00000100744; Low tissue specificity.
DR MIM; 616605; gene.
DR neXtProt; NX_Q9P0R6; -.
DR OpenTargets; ENSG00000100744; -.
DR PharmGKB; PA134987554; -.
DR VEuPathDB; HostDB:ENSG00000100744; -.
DR eggNOG; KOG3965; Eukaryota.
DR GeneTree; ENSGT00390000009517; -.
DR HOGENOM; CLU_143747_0_0_1; -.
DR InParanoid; Q9P0R6; -.
DR OMA; FAVTEMH; -.
DR OrthoDB; 1508955at2759; -.
DR PhylomeDB; Q9P0R6; -.
DR TreeFam; TF313906; -.
DR PathwayCommons; Q9P0R6; -.
DR SignaLink; Q9P0R6; -.
DR BioGRID-ORCS; 51527; 16 hits in 1081 CRISPR screens.
DR EvolutionaryTrace; Q9P0R6; -.
DR GenomeRNAi; 51527; -.
DR Pharos; Q9P0R6; Tbio.
DR PRO; PR:Q9P0R6; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9P0R6; protein.
DR Bgee; ENSG00000100744; Expressed in secondary oocyte and 186 other tissues.
DR ExpressionAtlas; Q9P0R6; baseline and differential.
DR Genevisible; Q9P0R6; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019207; F:kinase regulator activity; IBA:GO_Central.
DR GO; GO:0051018; F:protein kinase A binding; IPI:UniProtKB.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0030111; P:regulation of Wnt signaling pathway; IMP:UniProtKB.
DR Gene3D; 3.30.2280.10; -; 1.
DR InterPro; IPR037395; GSKIP.
DR InterPro; IPR007967; GSKIP_dom.
DR InterPro; IPR023231; GSKIP_dom_sf.
DR PANTHER; PTHR12490; PTHR12490; 1.
DR Pfam; PF05303; DUF727; 1.
DR SUPFAM; SSF103107; SSF103107; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..139
FT /note="GSK3B-interacting protein"
FT /id="PRO_0000220951"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..45
FT /note="Required for PRKAR2A interaction; contributes to a
FT protective effect against H(2)O(2)-induced apoptosis"
FT /evidence="ECO:0000269|PubMed:25920809"
FT REGION 115..139
FT /note="Interaction with GSK3B and acts as GSK3B inhibitor"
FT /evidence="ECO:0000269|PubMed:16981698"
FT SITE 130
FT /note="Required for GSK3B interaction; contributes to a
FT protective effect against H(2)O(2)-induced apoptosis"
FT /evidence="ECO:0000269|PubMed:16981698,
FT ECO:0000269|PubMed:25920809, ECO:0000269|PubMed:27484798"
FT MUTAGEN 41..45
FT /note="VNDVL->PNDVP: Abolishes interaction with PRKAR2A and
FT PRKAR2B. Abolishes acquired resistance against oxidative
FT stress-induced apoptosis under activated cAMP signaling.
FT Decreases PKA-mediated DNM1L phosphorylation."
FT /evidence="ECO:0000269|PubMed:25920809"
FT MUTAGEN 42
FT /note="N->I: Abolishes interaction with PRKAR2A. Prevents
FT the Wnt-induced transcription. Does not alter the
FT phosphorylation of CTNNB1 in the presence of Wnt."
FT /evidence="ECO:0000269|PubMed:27484798"
FT MUTAGEN 109
FT /note="S->A: No effect on GSK3B-mediated phosphorylation.
FT Reduces to 30 % GSK3B-mediated phosphorylation; when
FT associated with A-113. Reduces to 30 % GSK3B-mediated
FT phosphorylation; when associated with A-113 and A-115."
FT /evidence="ECO:0000269|PubMed:16981698"
FT MUTAGEN 113
FT /note="T->A: No effect on GSK3B-mediated phosphorylation.
FT Reduces to 30 % GSK3B-mediated phosphorylation; when
FT associated with A-109.Reduces to 30 % GSK3B-mediated
FT phosphorylation; when associated with A-113 and A-115."
FT /evidence="ECO:0000269|PubMed:16981698"
FT MUTAGEN 115
FT /note="S->A: No effect on GSK3B-mediated phosphorylation.
FT Reduces to 30 % GSK3B-mediated phosphorylation; when
FT associated with A-109.Reduces to 30 % GSK3B-mediated
FT phosphorylation; when associated with A109 and A-113."
FT /evidence="ECO:0000269|PubMed:16981698"
FT MUTAGEN 130
FT /note="L->P: Loss of interaction with GSK3B. Abolishes
FT GSK3B-mediated phosphorylation. Prevents beta-catenin
FT accumulation in the cytoplasm and nucleus. Prevents the
FT Wnt-induced transcription. Decreases PKA-mediated
FT phosphorylation of GSK3B. Abolishes acquired resistance
FT against oxidative stress-induced apoptosis under activated
FT cAMP signaling. Decreases PKA-mediated DNM1L
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:16981698,
FT ECO:0000269|PubMed:25920809, ECO:0000269|PubMed:27484798"
FT CONFLICT 46
FT /note="F -> S (in Ref. 2; BAA91380)"
FT /evidence="ECO:0000305"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:1SGO"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:1SGO"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:1SGO"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:1SGO"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:1SGO"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:1SGO"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:1SGO"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:1SGO"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:1SGO"
FT HELIX 116..135
FT /evidence="ECO:0007829|PDB:1SGO"
SQ SEQUENCE 139 AA; 15648 MW; A2D8BAF4B458B316 CRC64;
METDCNPMEL SSMSGFEEGS ELNGFEGTDM KDMRLEAEAV VNDVLFAVNN MFVSKSLRCA
DDVAYINVET KERNRYCLEL TEAGLKVVGY AFDQVDDHLQ TPYHETVYSL LDTLSPAYRE
AFGNALLQRL EALKRDGQS
