GCP4_HUMAN
ID GCP4_HUMAN Reviewed; 667 AA.
AC Q9UGJ1; B3KNK6; Q969X3; Q9NVF0;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Gamma-tubulin complex component 4;
DE Short=GCP-4;
DE Short=hGCP4;
DE AltName: Full=Gamma-ring complex protein 76 kDa;
DE Short=h76p;
DE Short=hGrip76;
GN Name=TUBGCP4; Synonyms=76P, GCP4;
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 1), AND PROTEIN SEQUENCE OF 1-20.
RC TISSUE=Neuroblastoma;
RX PubMed=10562286; DOI=10.1083/jcb.147.4.857;
RA Fava F., Raynaud-Messina B., Leung-Tack J., Mazzolini L., Li M.,
RA Guillemot J.-C., Cachot D., Tollon Y., Ferrara P., Wright M.;
RT "Human 76p: a new protein member of the gamma-tubulin associated protein
RT family.";
RL J. Cell Biol. 147:857-868(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
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=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 [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] (ISOFORM 2).
RC TISSUE=Lung;
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 NINL.
RX PubMed=12852856; DOI=10.1016/s1534-5807(03)00193-x;
RA Casenghi M., Meraldi P., Weinhart U., Duncan P.I., Korner R., Nigg E.A.;
RT "Polo-like kinase 1 regulates Nlp, a centrosome protein involved in
RT microtubule nucleation.";
RL Dev. Cell 5:113-125(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP INVOLVEMENT IN MCCRP3.
RX PubMed=25817018; DOI=10.1016/j.ajhg.2015.02.011;
RA Scheidecker S., Etard C., Haren L., Stoetzel C., Hull S., Arno G.,
RA Plagnol V., Drunat S., Passemard S., Toutain A., Obringer C., Koob M.,
RA Geoffroy V., Marion V., Strahle U., Ostergaard P., Verloes A., Merdes A.,
RA Moore A.T., Dollfus H.;
RT "Mutations in TUBGCP4 alter microtubule organization via the gamma-tubulin
RT ring complex in autosomal-recessive microcephaly with chorioretinopathy.";
RL Am. J. Hum. Genet. 96:666-674(2015).
RN [9]
RP INTERACTION WITH ATF5.
RX PubMed=26213385; DOI=10.1016/j.cell.2015.06.055;
RA Madarampalli B., Yuan Y., Liu D., Lengel K., Xu Y., Li G., Yang J., Liu X.,
RA Lu Z., Liu D.X.;
RT "ATF5 Connects the Pericentriolar Materials to the Proximal End of the
RT Mother Centriole.";
RL Cell 162:580-592(2015).
CC -!- FUNCTION: Gamma-tubulin complex is necessary for microtubule nucleation
CC at the centrosome.
CC -!- SUBUNIT: Gamma-tubulin complex is composed of gamma-tubulin, TUBGCP2,
CC TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6. Interacts with NINL. Interacts
CC with ATF5; the ATF5:PCNT:polyglutamylated tubulin (PGT) tripartite
CC unites the mother centriole and the pericentriolar material (PCM) in
CC the centrosome (PubMed:26213385). {ECO:0000269|PubMed:12852856,
CC ECO:0000269|PubMed:26213385}.
CC -!- INTERACTION:
CC Q9UGJ1; Q8IVS8: GLYCTK; NbExp=3; IntAct=EBI-1052544, EBI-748515;
CC Q9UGJ1; Q8N653: LZTR1; NbExp=4; IntAct=EBI-1052544, EBI-2350056;
CC Q9UGJ1; Q9NTX7: RNF146; NbExp=3; IntAct=EBI-1052544, EBI-722397;
CC Q9UGJ1-2; P48643: CCT5; NbExp=3; IntAct=EBI-10964469, EBI-355710;
CC Q9UGJ1-2; Q9BRP7: FDXACB1; NbExp=3; IntAct=EBI-10964469, EBI-10297077;
CC Q9UGJ1-2; P22607: FGFR3; NbExp=3; IntAct=EBI-10964469, EBI-348399;
CC Q9UGJ1-2; P01112: HRAS; NbExp=3; IntAct=EBI-10964469, EBI-350145;
CC Q9UGJ1-2; P42858: HTT; NbExp=6; IntAct=EBI-10964469, EBI-466029;
CC Q9UGJ1-2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-10964469, EBI-10975473;
CC Q9UGJ1-2; P19013: KRT4; NbExp=3; IntAct=EBI-10964469, EBI-2371606;
CC Q9UGJ1-2; P04259: KRT6B; NbExp=3; IntAct=EBI-10964469, EBI-740907;
CC Q9UGJ1-2; P07196: NEFL; NbExp=3; IntAct=EBI-10964469, EBI-475646;
CC Q9UGJ1-2; P46020-2: PHKA1; NbExp=3; IntAct=EBI-10964469, EBI-11135904;
CC Q9UGJ1-2; P41219: PRPH; NbExp=3; IntAct=EBI-10964469, EBI-752074;
CC Q9UGJ1-2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-10964469, EBI-396669;
CC Q9UGJ1-2; P23258: TUBG1; NbExp=2; IntAct=EBI-10964469, EBI-302589;
CC Q9UGJ1-2; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-10964469, EBI-741480;
CC Q9UGJ1-2; O76024: WFS1; NbExp=3; IntAct=EBI-10964469, EBI-720609;
CC Q9UGJ1-2; Q9Y649; NbExp=3; IntAct=EBI-10964469, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UGJ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UGJ1-2; Sequence=VSP_040085;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- DISEASE: Microcephaly and chorioretinopathy, autosomal recessive, 3
CC (MCCRP3) [MIM:616335]: A disorder characterized by congenital
CC microcephaly and chorioretinal dysplasia associated with poor vision
CC and nystagmus. Variable ocular anomalies include microphthalmia,
CC retinal folding, retinal detachment, optic nerve hypoplasia, absence of
CC retinal vessels, round areas of chorioretinal atrophy, and attenuated
CC electroretinogram. Most patients have mild developmental delay and mild
CC learning difficulties. {ECO:0000269|PubMed:25817018}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TUBGCP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91802.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ249677; CAB62539.1; -; mRNA.
DR EMBL; AK001639; BAA91802.1; ALT_INIT; mRNA.
DR EMBL; AK027703; BAG51368.1; -; mRNA.
DR EMBL; AC018924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471125; EAW92603.1; -; Genomic_DNA.
DR EMBL; BC009870; AAH09870.1; -; mRNA.
DR EMBL; BC012801; AAH12801.1; -; mRNA.
DR CCDS; CCDS42030.1; -. [Q9UGJ1-2]
DR CCDS; CCDS66745.1; -. [Q9UGJ1-1]
DR RefSeq; NP_001273343.1; NM_001286414.2. [Q9UGJ1-1]
DR RefSeq; NP_055259.2; NM_014444.4. [Q9UGJ1-2]
DR RefSeq; XP_011519757.1; XM_011521455.2.
DR PDB; 3RIP; X-ray; 2.30 A; A=1-667.
DR PDB; 6V69; EM; 4.20 A; I=1-667.
DR PDB; 6V6S; EM; 4.30 A; I/K=1-667.
DR PDB; 7AS4; EM; 4.13 A; I/K=1-667.
DR PDB; 7QJ0; EM; 5.32 A; I/K=1-667.
DR PDB; 7QJ1; EM; 7.00 A; I/K=1-667.
DR PDB; 7QJ2; EM; 8.60 A; I/K=1-667.
DR PDB; 7QJ3; EM; 7.60 A; I/K=1-667.
DR PDB; 7QJ4; EM; 9.00 A; I/K=1-667.
DR PDB; 7QJ5; EM; 8.70 A; I/K=1-667.
DR PDB; 7QJ6; EM; 7.80 A; I/K=1-667.
DR PDB; 7QJ7; EM; 8.70 A; I/K=1-667.
DR PDB; 7QJ8; EM; 8.70 A; I/K=1-667.
DR PDB; 7QJ9; EM; 8.10 A; I/K=1-667.
DR PDB; 7QJA; EM; 9.20 A; I/K=1-667.
DR PDB; 7QJB; EM; 9.20 A; I/K=1-667.
DR PDB; 7QJC; EM; 16.10 A; I/K=1-667.
DR PDB; 7QJD; EM; 7.10 A; I/K=1-667.
DR PDB; 7QJE; EM; 7.80 A; I/K=1-667.
DR PDBsum; 3RIP; -.
DR PDBsum; 6V69; -.
DR PDBsum; 6V6S; -.
DR PDBsum; 7AS4; -.
DR PDBsum; 7QJ0; -.
DR PDBsum; 7QJ1; -.
DR PDBsum; 7QJ2; -.
DR PDBsum; 7QJ3; -.
DR PDBsum; 7QJ4; -.
DR PDBsum; 7QJ5; -.
DR PDBsum; 7QJ6; -.
DR PDBsum; 7QJ7; -.
DR PDBsum; 7QJ8; -.
DR PDBsum; 7QJ9; -.
DR PDBsum; 7QJA; -.
DR PDBsum; 7QJB; -.
DR PDBsum; 7QJC; -.
DR PDBsum; 7QJD; -.
DR PDBsum; 7QJE; -.
DR AlphaFoldDB; Q9UGJ1; -.
DR SMR; Q9UGJ1; -.
DR BioGRID; 118078; 166.
DR CORUM; Q9UGJ1; -.
DR DIP; DIP-50536N; -.
DR IntAct; Q9UGJ1; 90.
DR MINT; Q9UGJ1; -.
DR STRING; 9606.ENSP00000260383; -.
DR GlyGen; Q9UGJ1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UGJ1; -.
DR MetOSite; Q9UGJ1; -.
DR PhosphoSitePlus; Q9UGJ1; -.
DR BioMuta; TUBGCP4; -.
DR DMDM; 22095730; -.
DR EPD; Q9UGJ1; -.
DR jPOST; Q9UGJ1; -.
DR MassIVE; Q9UGJ1; -.
DR MaxQB; Q9UGJ1; -.
DR PaxDb; Q9UGJ1; -.
DR PeptideAtlas; Q9UGJ1; -.
DR PRIDE; Q9UGJ1; -.
DR ProteomicsDB; 84225; -. [Q9UGJ1-1]
DR ProteomicsDB; 84226; -. [Q9UGJ1-2]
DR Antibodypedia; 23879; 226 antibodies from 28 providers.
DR DNASU; 27229; -.
DR Ensembl; ENST00000260383.11; ENSP00000260383.7; ENSG00000137822.13. [Q9UGJ1-1]
DR Ensembl; ENST00000564079.6; ENSP00000456648.2; ENSG00000137822.13. [Q9UGJ1-2]
DR GeneID; 27229; -.
DR KEGG; hsa:27229; -.
DR MANE-Select; ENST00000564079.6; ENSP00000456648.2; NM_014444.5; NP_055259.2. [Q9UGJ1-2]
DR UCSC; uc001zrn.5; human. [Q9UGJ1-1]
DR CTD; 27229; -.
DR DisGeNET; 27229; -.
DR GeneCards; TUBGCP4; -.
DR HGNC; HGNC:16691; TUBGCP4.
DR HPA; ENSG00000137822; Low tissue specificity.
DR MalaCards; TUBGCP4; -.
DR MIM; 609610; gene.
DR MIM; 616335; phenotype.
DR neXtProt; NX_Q9UGJ1; -.
DR OpenTargets; ENSG00000137822; -.
DR Orphanet; 2518; Autosomal recessive chorioretinopathy-microcephaly syndrome.
DR PharmGKB; PA162407404; -.
DR VEuPathDB; HostDB:ENSG00000137822; -.
DR eggNOG; KOG2065; Eukaryota.
DR GeneTree; ENSGT00940000156677; -.
DR HOGENOM; CLU_012029_0_0_1; -.
DR InParanoid; Q9UGJ1; -.
DR OMA; WAAVMHQ; -.
DR OrthoDB; 1137416at2759; -.
DR PhylomeDB; Q9UGJ1; -.
DR TreeFam; TF324188; -.
DR PathwayCommons; Q9UGJ1; -.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR SignaLink; Q9UGJ1; -.
DR SIGNOR; Q9UGJ1; -.
DR BioGRID-ORCS; 27229; 779 hits in 1089 CRISPR screens.
DR ChiTaRS; TUBGCP4; human.
DR EvolutionaryTrace; Q9UGJ1; -.
DR GeneWiki; TUBGCP4; -.
DR GenomeRNAi; 27229; -.
DR Pharos; Q9UGJ1; Tbio.
DR PRO; PR:Q9UGJ1; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9UGJ1; protein.
DR Bgee; ENSG00000137822; Expressed in sperm and 173 other tissues.
DR ExpressionAtlas; Q9UGJ1; baseline and differential.
DR Genevisible; Q9UGJ1; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000923; C:equatorial microtubule organizing center; IBA:GO_Central.
DR GO; GO:0000930; C:gamma-tubulin complex; IBA:GO_Central.
DR GO; GO:0000931; C:gamma-tubulin large complex; NAS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; TAS:ProtInc.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IEA:InterPro.
DR GO; GO:0043015; F:gamma-tubulin binding; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; NAS:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0065003; P:protein-containing complex assembly; NAS:ProtInc.
DR GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
DR Gene3D; 1.20.120.1900; -; 1.
DR InterPro; IPR007259; GCP.
DR InterPro; IPR040457; GCP_C.
DR InterPro; IPR042241; GCP_C_sf.
DR InterPro; IPR041470; GCP_N.
DR PANTHER; PTHR19302; PTHR19302; 1.
DR Pfam; PF04130; GCP_C_terminal; 1.
DR Pfam; PF17681; GCP_N_terminal; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Intellectual disability; Microtubule;
KW Primary microcephaly; Reference proteome.
FT CHAIN 1..667
FT /note="Gamma-tubulin complex component 4"
FT /id="PRO_0000078124"
FT REGION 425..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 427
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040085"
FT HELIX 2..9
FT /evidence="ECO:0007829|PDB:3RIP"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:3RIP"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:3RIP"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 36..61
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 98..113
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 127..146
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 151..162
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 166..193
FT /evidence="ECO:0007829|PDB:3RIP"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:3RIP"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 270..284
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 303..315
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 322..347
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 350..360
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 366..380
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 388..402
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 411..413
FT /evidence="ECO:0007829|PDB:3RIP"
FT STRAND 414..418
FT /evidence="ECO:0007829|PDB:3RIP"
FT TURN 449..452
FT /evidence="ECO:0007829|PDB:3RIP"
FT STRAND 453..457
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 469..499
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 509..535
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 537..549
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 554..574
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 576..597
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 606..635
FT /evidence="ECO:0007829|PDB:3RIP"
FT HELIX 640..654
FT /evidence="ECO:0007829|PDB:3RIP"
SQ SEQUENCE 667 AA; 76089 MW; 2030EEDF290F5FAC CRC64;
MIHELLLALS GYPGSIFTWN KRSGLQVSQD FPFLHPSETS VLNRLCRLGT DYIRFTEFIE
QYTGHVQQQD HHPSQQGQGG LHGIYLRAFC TGLDSVLQPY RQALLDLEQE FLGDPHLSIS
HVNYFLDQFQ LLFPSVMVVV EQIKSQKIHG CQILETVYKH SCGGLPPVRS ALEKILAVCH
GVMYKQLSAW MLHGLLLDQH EEFFIKQGPS SGNVSAQPEE DEEDLGIGGL TGKQLRELQD
LRLIEEENML APSLKQFSLR VEILPSYIPV RVAEKILFVG ESVQMFENQN VNLTRKGSIL
KNQEDTFAAE LHRLKQQPLF SLVDFEQVVD RIRSTVAEHL WKLMVEESDL LGQLKIIKDF
YLLGRGELFQ AFIDTAQHML KTPPTAVTEH DVNVAFQQSA HKVLLDDDNL LPLLHLTIEY
HGKEHKADAT QAREGPSRET SPREAPASGW AALGLSYKVQ WPLHILFTPA VLEKYNVVFK
YLLSVRRVQA ELQHCWALQM QRKHLKSNQT DAIKWRLRNH MAFLVDNLQY YLQVDVLESQ
FSQLLHQINS TRDFESIRLA HDHFLSNLLA QSFILLKPVF HCLNEILDLC HSFCSLVSQN
LGPLDERGAA QLSILVKGFS RQSSLLFKIL SSVRNHQINS DLAQLLLRLD YNKYYTQAGG
TLGSFGM
