CCPG1_HUMAN
ID CCPG1_HUMAN Reviewed; 757 AA.
AC Q9ULG6; A0PJH3; A8K9T0; O14712; Q05DG4; Q5U5S7; Q8IYV8; Q9BY53; Q9HA17;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Cell cycle progression protein 1;
DE AltName: Full=Cell cycle progression restoration protein 8;
GN Name=CCPG1; Synonyms=CCP8, CPR8, KIAA1254;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Liver;
RA Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.;
RT "A novel gene expressed in human liver non-tumor tissues.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
RC TISSUE=Mammary gland, and Trachea;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP VAL-161; LEU-436; GLU-627 AND ILE-646.
RC TISSUE=Brain, Lymph, Placenta, and Skin;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 379-757 (ISOFORM 4), FUNCTION, AND VARIANTS
RP VAL-477 AND ASP-517.
RX PubMed=9383053; DOI=10.1093/genetics/147.3.1063;
RA Edwards M.C., Liegeois N., Horecka J., DePinho R.A., Sprague G.F. Jr.,
RA Tyers M., Elledge S.J.;
RT "Human CPR (cell cycle progression restoration) genes impart a Far-
RT phenotype on yeast cells.";
RL Genetics 147:1063-1076(1997).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION BY
RP 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Acts as an assembly platform for Rho protein signaling
CC complexes. Limits guanine nucleotide exchange activity of MCF2L toward
CC RHOA, which results in an inhibition of both its transcriptional
CC activation ability and its transforming activity. Does not inhibit
CC activity of MCF2L toward CDC42, or activity of MCF2 toward either RHOA
CC or CDC42 (By similarity). May be involved in cell cycle regulation.
CC {ECO:0000250, ECO:0000269|PubMed:9383053}.
CC -!- SUBUNIT: Interacts with MCF2L. May interact with MCF2, ARHGEF1, BCR,
CC VAV1 and FGD1, but not with TIAM1. Interacts with GTP-bound CDC42 and
CC SRC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9ULG6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULG6-2; Sequence=VSP_029311, VSP_029312;
CC Name=3;
CC IsoId=Q9ULG6-3; Sequence=VSP_029313, VSP_029316;
CC Name=4;
CC IsoId=Q9ULG6-4; Sequence=VSP_029314, VSP_029315;
CC Name=5;
CC IsoId=Q9ULG6-5; Sequence=VSP_029316;
CC -!- SIMILARITY: Belongs to the CCPG1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB69314.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH15203.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH29398.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA86568.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 4]:
CC Sequence=AAB69314.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAK14914.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB033080; BAA86568.2; ALT_INIT; mRNA.
DR EMBL; AF212228; AAK14914.1; ALT_FRAME; mRNA.
DR EMBL; AK022459; BAB14042.1; -; mRNA.
DR EMBL; AK292795; BAF85484.1; -; mRNA.
DR EMBL; AC013355; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC018926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471082; EAW77481.1; -; Genomic_DNA.
DR EMBL; BC015203; AAH15203.1; ALT_SEQ; mRNA.
DR EMBL; BC029398; AAH29398.1; ALT_SEQ; mRNA.
DR EMBL; BC034914; AAH34914.1; -; mRNA.
DR EMBL; BC039871; AAH39871.1; -; mRNA.
DR EMBL; AF011794; AAB69314.1; ALT_SEQ; mRNA.
DR CCDS; CCDS42039.1; -. [Q9ULG6-1]
DR CCDS; CCDS55966.1; -. [Q9ULG6-5]
DR CCDS; CCDS55967.1; -. [Q9ULG6-3]
DR RefSeq; NP_001191379.1; NM_001204450.1. [Q9ULG6-5]
DR RefSeq; NP_001191380.1; NM_001204451.1. [Q9ULG6-3]
DR RefSeq; NP_004739.3; NM_004748.4. [Q9ULG6-1]
DR RefSeq; NP_065790.2; NM_020739.3. [Q9ULG6-1]
DR PDB; 7D0E; X-ray; 1.40 A; B=101-113.
DR PDBsum; 7D0E; -.
DR AlphaFoldDB; Q9ULG6; -.
DR SMR; Q9ULG6; -.
DR BioGRID; 114665; 83.
DR IntAct; Q9ULG6; 35.
DR MINT; Q9ULG6; -.
DR STRING; 9606.ENSP00000403400; -.
DR GlyGen; Q9ULG6; 1 site.
DR iPTMnet; Q9ULG6; -.
DR PhosphoSitePlus; Q9ULG6; -.
DR BioMuta; CCPG1; -.
DR DMDM; 160380597; -.
DR EPD; Q9ULG6; -.
DR jPOST; Q9ULG6; -.
DR MassIVE; Q9ULG6; -.
DR MaxQB; Q9ULG6; -.
DR PaxDb; Q9ULG6; -.
DR PeptideAtlas; Q9ULG6; -.
DR PRIDE; Q9ULG6; -.
DR ProteomicsDB; 1897; -.
DR ProteomicsDB; 85016; -. [Q9ULG6-1]
DR ProteomicsDB; 85017; -. [Q9ULG6-2]
DR ProteomicsDB; 85018; -. [Q9ULG6-3]
DR ProteomicsDB; 85019; -. [Q9ULG6-4]
DR Antibodypedia; 57643; 66 antibodies from 19 providers.
DR DNASU; 9236; -.
DR Ensembl; ENST00000310958.10; ENSP00000311656.6; ENSG00000260916.8. [Q9ULG6-1]
DR Ensembl; ENST00000425574.7; ENSP00000415128.3; ENSG00000260916.8. [Q9ULG6-3]
DR Ensembl; ENST00000442196.8; ENSP00000403400.3; ENSG00000260916.8. [Q9ULG6-5]
DR Ensembl; ENST00000569205.5; ENSP00000454456.1; ENSG00000260916.8. [Q9ULG6-1]
DR GeneID; 9236; -.
DR KEGG; hsa:9236; -.
DR MANE-Select; ENST00000442196.8; ENSP00000403400.3; NM_001204450.2; NP_001191379.1. [Q9ULG6-5]
DR UCSC; uc002acv.3; human. [Q9ULG6-1]
DR CTD; 9236; -.
DR DisGeNET; 9236; -.
DR GeneCards; CCPG1; -.
DR HGNC; HGNC:24227; CCPG1.
DR HPA; ENSG00000260916; Low tissue specificity.
DR MalaCards; CCPG1; -.
DR MIM; 611326; gene.
DR neXtProt; NX_Q9ULG6; -.
DR OpenTargets; ENSG00000260916; -.
DR PharmGKB; PA134967250; -.
DR VEuPathDB; HostDB:ENSG00000260916; -.
DR eggNOG; ENOG502QWDZ; Eukaryota.
DR GeneTree; ENSGT00940000160497; -.
DR HOGENOM; CLU_018722_0_0_1; -.
DR InParanoid; Q9ULG6; -.
DR OMA; LDAFHHW; -.
DR OrthoDB; 667993at2759; -.
DR PhylomeDB; Q9ULG6; -.
DR TreeFam; TF333202; -.
DR PathwayCommons; Q9ULG6; -.
DR SignaLink; Q9ULG6; -.
DR BioGRID-ORCS; 9236; 9 hits in 1082 CRISPR screens.
DR GenomeRNAi; 9236; -.
DR Pharos; Q9ULG6; Tbio.
DR PRO; PR:Q9ULG6; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9ULG6; protein.
DR Bgee; ENSG00000260916; Expressed in calcaneal tendon and 143 other tissues.
DR ExpressionAtlas; Q9ULG6; baseline and differential.
DR Genevisible; Q9ULG6; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:2001106; P:regulation of Rho guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR InterPro; IPR033588; CCPG1.
DR PANTHER; PTHR28638:SF2; PTHR28638:SF2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Coiled coil; Membrane;
KW Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..757
FT /note="Cell cycle progression protein 1"
FT /id="PRO_0000310538"
FT TOPO_DOM 1..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..757
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..308
FT /note="Interaction with MCF2L and SRC"
FT /evidence="ECO:0000250"
FT REGION 152..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 248..272
FT /evidence="ECO:0000255"
FT COILED 306..450
FT /evidence="ECO:0000255"
FT COILED 504..530
FT /evidence="ECO:0000255"
FT COMPBIAS 152..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..144
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029311"
FT VAR_SEQ 145..151
FT /note="TFCQPET -> MSTFFLI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029312"
FT VAR_SEQ 312..694
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_029313"
FT VAR_SEQ 582..598
FT /note="HNRGPTMQNDGRKEKPV -> SRPYYAKRWKERKASSL (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:9383053, ECO:0000303|Ref.3"
FT /id="VSP_029314"
FT VAR_SEQ 599..757
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9383053, ECO:0000303|Ref.3"
FT /id="VSP_029315"
FT VAR_SEQ 745..757
FT /note="RSVYIKPCHYSSL -> SRPDKKQRMVNIENSRHRKQEQKHLQPQPYKREGK
FT WHKYGRTNGRQMANLEIELGQLPFDPQY (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_029316"
FT VARIANT 44
FT /note="S -> P (in dbSNP:rs11555304)"
FT /id="VAR_037063"
FT VARIANT 161
FT /note="E -> V (in dbSNP:rs17853336)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_037064"
FT VARIANT 418
FT /note="Y -> H (in dbSNP:rs34958422)"
FT /id="VAR_037065"
FT VARIANT 436
FT /note="R -> L (in dbSNP:rs17857026)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_037066"
FT VARIANT 477
FT /note="A -> V (in dbSNP:rs1063562)"
FT /evidence="ECO:0000269|PubMed:9383053"
FT /id="VAR_037067"
FT VARIANT 517
FT /note="A -> D (in dbSNP:rs1063563)"
FT /evidence="ECO:0000269|PubMed:9383053"
FT /id="VAR_037068"
FT VARIANT 553
FT /note="G -> D (in dbSNP:rs1063565)"
FT /id="VAR_037069"
FT VARIANT 553
FT /note="G -> S (in dbSNP:rs1063564)"
FT /id="VAR_037070"
FT VARIANT 590
FT /note="N -> K (in dbSNP:rs1063566)"
FT /id="VAR_037071"
FT VARIANT 627
FT /note="K -> E (in dbSNP:rs17853335)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_037072"
FT VARIANT 646
FT /note="T -> I (in dbSNP:rs17857027)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_037073"
FT VARIANT 673
FT /note="H -> R (in dbSNP:rs1063567)"
FT /id="VAR_037074"
FT CONFLICT 196
FT /note="A -> G (in Ref. 1; BAA86568)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="E -> G (in Ref. 4; BAB14042)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="E -> G (in Ref. 7; AAH29398 and 8; AAB69314)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="G -> N (in Ref. 8; AAB69314)"
FT /evidence="ECO:0000305"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:7D0E"
SQ SEQUENCE 757 AA; 87340 MW; DDF496D4431A7976 CRC64;
MSENSSDSDS SCGWTVISHE GSDIEMLNSV TPTDSCEPAP ECSSLEQEEL QALQIEQGES
SQNGTVLMEE TAYPALEETS STIEAEEQKI PEDSIYIGTA SDDSDIVTLE PPKLEEIGNQ
EVVIVEEAQS SEDFNMGSSS SSQYTFCQPE TVFSSQPSDD ESSSDETSNQ PSPAFRRRRA
RKKTVSASES EDRLVAEQET EPSKELSKRQ FSSGLNKCVI LALVIAISMG FGHFYGTIQI
QKRQQLVRKI HEDELNDMKD YLSQCQQEQE SFIDYKSLKE NLARCWTLTE AEKMSFETQK
TNLATENQYL RVSLEKEEKA LSSLQEELNK LREQIRILED KGTSTELVKE NQKLKQHLEE
EKQKKHSFLS QRETLLTEAK MLKRELERER LVTTALRGEL QQLSGSQLHG KSDSPNVYTE
KKEIAILRER LTELERKLTF EQQRSDLWER LYVEAKDQNG KQGTDGKKKG GRGSHRAKNK
SKETFLGSVK ETFDAMKNST KEFVRHHKEK IKQAKEAVKE NLKKFSDSVK STFRHFKDTT
KNIFDEKGNK RFGATKEAAE KPRTVFSDYL HPQYKAPTEN HHNRGPTMQN DGRKEKPVHF
KEFRKNTNSK KCSPGHDCRE NSHSFRKACS GVFDCAQQES MSLFNTVVNP IRMDEFRQII
QRYMLKELDT FCHWNELDQF INKFFLNGVF IHDQKLFTDF VNDVKDYLRN MKEYEVDNDG
VFEKLDEYIY RHFFGHTFSP PYGPRSVYIK PCHYSSL
