EPHA1_MOUSE
ID EPHA1_MOUSE Reviewed; 977 AA.
AC Q60750; Q8CED9; Q9ESJ2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Ephrin type-A receptor 1;
DE Short=mEpha1;
DE EC=2.7.10.1;
DE AltName: Full=Embryonic stem cell kinase;
DE AltName: Full=Tyrosine-protein kinase receptor ESK;
DE Flags: Precursor;
GN Name=Epha1; Synonyms=Esk;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND EFNA1 LIGAND-BINDING.
RX PubMed=11519828; DOI=10.3109/08977190109029118;
RA Coulthard M.G., Lickliter J.D., Subanesan N., Chen K., Webb G.C.,
RA Lowry A.J., Koblar S., Bottema C.D., Boyd A.W.;
RT "Characterization of the Epha1 receptor tyrosine kinase: expression in
RT epithelial tissues.";
RL Growth Factors 18:303-317(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 281-814.
RC STRAIN=129/Sv;
RX PubMed=8552593; DOI=10.1073/pnas.93.1.145;
RA Lickliter J.D., Smith F.M., Olsson J.E., Mackwell K.L., Boyd A.W.;
RT "Embryonic stem cells express multiple Eph-subfamily receptor tyrosine
RT kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:145-150(1996).
RN [4]
RP DISRUPTION PHENOTYPE, FUNCTION IN APOPTOSIS, AND TISSUE SPECIFICITY.
RX PubMed=18802966; DOI=10.1002/dvg.20434;
RA Duffy S.L., Coulthard M.G., Spanevello M.D., Herath N.I., Yeadon T.M.,
RA McCarron J.K., Carter J.C., Tonks I.D., Kay G.F., Phillips G.E., Boyd A.W.;
RT "Generation and characterization of EphA1 receptor tyrosine kinase reporter
RT knockout mice.";
RL Genesis 46:553-561(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=27446912; DOI=10.3389/fcell.2016.00058;
RA Alonso-Martin S., Rochat A., Mademtzoglou D., Morais J., de Reynies A.,
RA Aurade F., Chang T.H., Zammit P.S., Relaix F.;
RT "Gene expression profiling of muscle stem cells identifies novel regulators
RT of postnatal myogenesis.";
RL Front. Cell Dev. Biol. 4:58-58(2016).
RN [7]
RP STRUCTURE BY NMR OF 446-539.
RG RIKEN structural genomics initiative (RSGI);
RT "The solution structure of the second fibronectin type III domain of mouse
RT ephrin type-A receptor 1.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Receptor tyrosine kinase which binds promiscuously membrane-
CC bound ephrin-A family ligands residing on adjacent cells, leading to
CC contact-dependent bidirectional signaling into neighboring cells. The
CC signaling pathway downstream of the receptor is referred to as forward
CC signaling while the signaling pathway downstream of the ephrin ligand
CC is referred to as reverse signaling. Binds with a low affinity EFNA3
CC and EFNA4 and with a high affinity to EFNA1 which most probably
CC constitutes its cognate/functional ligand. Upon activation by EFNA1
CC induces cell attachment to the extracellular matrix inhibiting cell
CC spreading and motility through regulation of ILK and downstream RHOA
CC and RAC. Also plays a role in angiogenesis and regulates cell
CC proliferation. May play a role in apoptosis.
CC {ECO:0000269|PubMed:18802966}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBUNIT: Homodimer. Forms a signaling complex with LCK; PTK2B/PYK2 and
CC PI3-kinase upon activation by EFNA1; regulates T-lymphocytes migration.
CC Interacts (via SAM domain) with ILK (via ANK repeats); stimulated by
CC EFNA1 but independent of the kinase activity of EPHA1. Interacts
CC (kinase activity-dependent) with PTK2/FAK1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in epithelial cells
CC including skin, kidney, liver and thymus (PubMed:11519828,
CC PubMed:18802966). Expressed in myogenic progenitor cells
CC (PubMed:27446912). {ECO:0000269|PubMed:11519828,
CC ECO:0000269|PubMed:18802966, ECO:0000269|PubMed:27446912}.
CC -!- DEVELOPMENTAL STAGE: In myogenic progenitor cells, expressed during the
CC acquisition of muscle stem cell properties, from 18.5 dpc to adulthood.
CC {ECO:0000269|PubMed:27446912}.
CC -!- PTM: Phosphorylated. Autophosphorylation is stimulated by its ligand
CC EFNA1 (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice display a partially-penetrant uterovaginal
CC and tail development defects. The uterovaginal defect is due to a
CC defect in apoptosis during development. {ECO:0000269|PubMed:18802966}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AF131197; AAG12206.1; -; mRNA.
DR EMBL; AK028478; BAC25971.1; -; mRNA.
DR EMBL; U18084; AAC52384.1; -; mRNA.
DR CCDS; CCDS20067.1; -.
DR RefSeq; NP_076069.2; NM_023580.4.
DR PDB; 1X5A; NMR; -; A=446-539.
DR PDBsum; 1X5A; -.
DR AlphaFoldDB; Q60750; -.
DR BMRB; Q60750; -.
DR SMR; Q60750; -.
DR BioGRID; 199468; 1.
DR IntAct; Q60750; 4.
DR MINT; Q60750; -.
DR STRING; 10090.ENSMUSP00000073099; -.
DR GlyGen; Q60750; 2 sites.
DR iPTMnet; Q60750; -.
DR PhosphoSitePlus; Q60750; -.
DR MaxQB; Q60750; -.
DR PaxDb; Q60750; -.
DR PeptideAtlas; Q60750; -.
DR PRIDE; Q60750; -.
DR ProteomicsDB; 277884; -.
DR Antibodypedia; 32658; 629 antibodies from 39 providers.
DR DNASU; 13835; -.
DR Ensembl; ENSMUST00000073387; ENSMUSP00000073099; ENSMUSG00000029859.
DR GeneID; 13835; -.
DR KEGG; mmu:13835; -.
DR UCSC; uc009brc.1; mouse.
DR CTD; 2041; -.
DR MGI; MGI:107381; Epha1.
DR VEuPathDB; HostDB:ENSMUSG00000029859; -.
DR eggNOG; KOG0196; Eukaryota.
DR GeneTree; ENSGT00940000160920; -.
DR HOGENOM; CLU_000288_141_0_1; -.
DR InParanoid; Q60750; -.
DR OMA; YQRCPEA; -.
DR OrthoDB; 933071at2759; -.
DR PhylomeDB; Q60750; -.
DR TreeFam; TF315363; -.
DR Reactome; R-MMU-2682334; EPH-Ephrin signaling.
DR Reactome; R-MMU-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
DR BioGRID-ORCS; 13835; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Epha1; mouse.
DR EvolutionaryTrace; Q60750; -.
DR PRO; PR:Q60750; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q60750; protein.
DR Bgee; ENSMUSG00000029859; Expressed in lip and 95 other tissues.
DR ExpressionAtlas; Q60750; baseline and differential.
DR Genevisible; Q60750; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005003; F:ephrin receptor activity; IDA:ARUK-UCL.
DR GO; GO:0001968; F:fibronectin binding; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0005005; F:transmembrane-ephrin receptor activity; ISS:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISS:UniProtKB.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd10479; EphR_LBD_A1; 1.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR027936; Eph_TM.
DR InterPro; IPR034251; EphA1_rcpt_lig-bd.
DR InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
DR InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
DR Pfam; PF14575; EphA2_TM; 1.
DR Pfam; PF01404; Ephrin_lbd; 1.
DR Pfam; PF07699; Ephrin_rec_like; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00615; EPH_lbd; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS51550; EPH_LBD; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
DR PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Angiogenesis; ATP-binding; Cell adhesion; Cell membrane;
KW Glycoprotein; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..977
FT /note="Ephrin type-A receptor 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000016799"
FT TOPO_DOM 27..548
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 549..569
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 570..977
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..210
FT /note="Eph LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00883"
FT DOMAIN 333..446
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 448..539
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 625..885
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 914..977
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT MOTIF 975..977
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT ACT_SITE 750
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 631..639
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 657
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 600
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000255"
FT MOD_RES 606
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000255"
FT MOD_RES 782
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 907
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21709"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21709"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 163
FT /note="G -> D (in Ref. 1; AAG12206)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="S -> P (in Ref. 3; AAC52384)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="L -> R (in Ref. 3; AAC52384)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="T -> A (in Ref. 3; AAC52384)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="D -> G (in Ref. 3; AAC52384)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="F -> Y (in Ref. 3; AAC52384)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="K -> R (in Ref. 3; AAC52384)"
FT /evidence="ECO:0000305"
FT CONFLICT 720
FT /note="D -> G (in Ref. 3; AAC52384)"
FT /evidence="ECO:0000305"
FT CONFLICT 769
FT /note="F -> L (in Ref. 3; AAC52384)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="E -> G (in Ref. 3; AAC52384)"
FT /evidence="ECO:0000305"
FT CONFLICT 817
FT /note="M -> T (in Ref. 1; AAG12206)"
FT /evidence="ECO:0000305"
FT STRAND 456..460
FT /evidence="ECO:0007829|PDB:1X5A"
FT STRAND 463..467
FT /evidence="ECO:0007829|PDB:1X5A"
FT STRAND 481..487
FT /evidence="ECO:0007829|PDB:1X5A"
FT STRAND 492..506
FT /evidence="ECO:0007829|PDB:1X5A"
FT STRAND 512..520
FT /evidence="ECO:0007829|PDB:1X5A"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:1X5A"
FT STRAND 532..535
FT /evidence="ECO:0007829|PDB:1X5A"
SQ SEQUENCE 977 AA; 108578 MW; AB78D6E6C8B2E7F4 CRC64;
MERRWPLGLA LLLLLLCAPL PPGARAEEVT LMDTSTAQGE LGWLLDPPET GWSEVQQMLN
GTPLYMYQDC PIQEGGDTDH WLRSNWIYRG EEASRIYVEL QFTVRDCKSF PGGAGPLGCK
ETFNLFYMES DQDVGIQLRR PLFQKVTTVA ADQSFTIRDL ASGSVKLNVE RCSLGHLTRR
GLYLAFHNPG SCVALVSVRV FYQRCAETVH GLAHFPDTLP GPGGLVEVAG TCLSHAQISL
GSSGTPRMHC SPDGEWLVPV GQCQCEPGYE ESSGNVGCTA CPTGFYRVDM NTLRCLKCPQ
HSIAESEGST ICTCENGHYR APGEGPQVAC TRPPSAPQNL SFSTSGTQLS LRWEPPRDTG
GRHDIRYSVE CLQCRGIAQD GGPCQPCGKG VHFSPAASGL TTSTVQVQGL EPYANYTFTV
KSQNRVSGLD SSSPSSASLS INMGHAESLS GLSLKLVKKE PRQLELTWAG SRPRNPGGNL
SYELHVLNQD EEWHQMVLEP RVLLTKLQPD TTYIVRVRTL TPLGPGPFSP DHEFRTSPPV
SRSLTGGEIV AVIFGLLLGI ALLIGIYVFR SRRGQRQRQQ RQRERTTNVD REDKLWLKPY
VDLQAYEDPA QGALDFAQEL DPAWLIVDTV IGEGEFGEVY RGALRLPSQD CKTVAIKTLK
DTSPDGYWWN FLREATIMGQ FNHPHILRLE GVITKRKPIM IITEFMENGA LDAFLKERED
QLAPGQLVAM LLGIASGMNC LSGHNYVHRD LAARNILVNQ NLCCKVSDFG LTRLLDDFDG
TYETQGGKIP IRWTAPEAIA HRIFTTASDV WSFGIVMWEV LSFGDKPYGE MSNQEVMKSI
EDGYRLPPPV DCPAPLYELM KNCWAYDRAR RPHFLQLQAH LEQLLTDPHS LRTIANFDPR
VTLRLPSLSG SDGIPYRSVS EWLESIRMKR YILHFRSAGL DTMECVLELT AEDLTQMGIT
LPGHQKRILC SIQGFKD
