C2C2L_HUMAN
ID C2C2L_HUMAN Reviewed; 706 AA.
AC O14523; Q86UT7; Q86V04; Q8N522; Q8TBN4; Q96G10;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Phospholipid transfer protein C2CD2L {ECO:0000305};
DE AltName: Full=C2 domain-containing protein 2-like {ECO:0000312|HGNC:HGNC:29000};
DE Short=C2CD2-like;
DE AltName: Full=Transmembrane protein 24 {ECO:0000303|PubMed:28209843};
GN Name=C2CD2L {ECO:0000312|HGNC:HGNC:29000};
GN Synonyms=KIAA0285 {ECO:0000303|PubMed:9179496},
GN TMEM24 {ECO:0000303|PubMed:28209843}; ORFNames=DLNB23 {ECO:0000303|Ref.1};
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 Kubo T., Arai Y., Ohira M., Gamou T., Maeno G., Sakiyama T., Toyoda A.,
RA Hattori M., Sakaki Y., Nakagawara A., Ohki M.;
RT "Identification of a 500-kb region of common allelic loss in chromosome
RT 11q23 in non-MYCN amplified type of neuroblastoma.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 381-706 (ISOFORM 2).
RC TISSUE=Blood, Brain, and Pancreas;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 49-706 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9179496; DOI=10.1093/dnares/4.1.53;
RA Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N.,
RA Nomura N.;
RT "Construction and characterization of human brain cDNA libraries suitable
RT for analysis of cDNA clones encoding relatively large proteins.";
RL DNA Res. 4:53-59(1997).
RN [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-417 AND SER-464, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-623, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; SER-374; SER-411;
RP THR-417; THR-428; SER-464; SER-468; SER-470; SER-623; SER-638; SER-660;
RP SER-662 AND SER-674, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 76-260, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, AND PHOSPHORYLATION.
RX PubMed=28209843; DOI=10.1126/science.aah6171;
RA Lees J.A., Messa M., Sun E.W., Wheeler H., Torta F., Wenk M.R.,
RA De Camilli P., Reinisch K.M.;
RT "Lipid transport by TMEM24 at ER-plasma membrane contacts regulates
RT pulsatile insulin secretion.";
RL Science 355:0-0(2017).
CC -!- FUNCTION: Lipid-binding protein that transports phosphatidylinositol,
CC the precursor of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2),
CC from its site of synthesis in the endoplasmic reticulum to the cell
CC membrane (PubMed:28209843). It thereby maintains the pool of cell
CC membrane phosphoinositides, which are degraded during phospholipase C
CC (PLC) signaling (PubMed:28209843). Plays a key role in the coordination
CC of Ca(2+) and phosphoinositide signaling: localizes to sites of contact
CC between the endoplasmic reticulum and the cell membrane, where it
CC tethers the two bilayers (PubMed:28209843). In response to elevation of
CC cytosolic Ca(2+), it is phosphorylated at its C-terminus and
CC dissociates from the cell membrane, abolishing phosphatidylinositol
CC transport to the cell membrane (PubMed:28209843). Positively regulates
CC insulin secretion in response to glucose: phosphatidylinositol transfer
CC to the cell membrane allows replenishment of PI(4,5)P2 pools and
CC calcium channel opening, priming a new population of insulin granules
CC (PubMed:28209843). {ECO:0000269|PubMed:28209843}.
CC -!- SUBUNIT: Homodimer (PubMed:28209843). {ECO:0000269|PubMed:28209843}.
CC -!- INTERACTION:
CC O14523; Q86WK6: AMIGO1; NbExp=3; IntAct=EBI-12822627, EBI-19125216;
CC O14523; Q13520: AQP6; NbExp=3; IntAct=EBI-12822627, EBI-13059134;
CC O14523; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-12822627, EBI-11343438;
CC O14523; Q13323: BIK; NbExp=3; IntAct=EBI-12822627, EBI-700794;
CC O14523; P11912: CD79A; NbExp=3; IntAct=EBI-12822627, EBI-7797864;
CC O14523; Q9H9P2: CHODL; NbExp=3; IntAct=EBI-12822627, EBI-17447707;
CC O14523; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-12822627, EBI-1045797;
CC O14523; P58418: CLRN1; NbExp=3; IntAct=EBI-12822627, EBI-17274839;
CC O14523; P49682: CXCR3; NbExp=3; IntAct=EBI-12822627, EBI-12836456;
CC O14523; Q15125: EBP; NbExp=3; IntAct=EBI-12822627, EBI-3915253;
CC O14523; Q9NYP7: ELOVL5; NbExp=3; IntAct=EBI-12822627, EBI-11037623;
CC O14523; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-12822627, EBI-781551;
CC O14523; P48165: GJA8; NbExp=3; IntAct=EBI-12822627, EBI-17458373;
CC O14523; P08034: GJB1; NbExp=3; IntAct=EBI-12822627, EBI-17565645;
CC O14523; P31937: HIBADH; NbExp=3; IntAct=EBI-12822627, EBI-11427100;
CC O14523; P26951: IL3RA; NbExp=3; IntAct=EBI-12822627, EBI-1757512;
CC O14523; O95214: LEPROTL1; NbExp=3; IntAct=EBI-12822627, EBI-750776;
CC O14523; Q6N075: MFSD5; NbExp=3; IntAct=EBI-12822627, EBI-3920969;
CC O14523; P15941-11: MUC1; NbExp=3; IntAct=EBI-12822627, EBI-17263240;
CC O14523; P35372-10: OPRM1; NbExp=3; IntAct=EBI-12822627, EBI-12807478;
CC O14523; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-12822627, EBI-716063;
CC O14523; Q9BRK0: REEP2; NbExp=3; IntAct=EBI-12822627, EBI-11337973;
CC O14523; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-12822627, EBI-7545592;
CC O14523; O00560: SDCBP; NbExp=3; IntAct=EBI-12822627, EBI-727004;
CC O14523; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-12822627, EBI-18159983;
CC O14523; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-12822627, EBI-17595455;
CC O14523; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-12822627, EBI-8638294;
CC O14523; Q7Z7N9: TMEM179B; NbExp=3; IntAct=EBI-12822627, EBI-11724423;
CC O14523; Q9NWD8: TMEM248; NbExp=3; IntAct=EBI-12822627, EBI-10314986;
CC O14523; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-12822627, EBI-2548832;
CC O14523; Q6PEY1: TMEM88; NbExp=3; IntAct=EBI-12822627, EBI-17198826;
CC O14523; Q9P0T7: TMEM9; NbExp=3; IntAct=EBI-12822627, EBI-723976;
CC O14523; O15393-2: TMPRSS2; NbExp=3; IntAct=EBI-12822627, EBI-12345267;
CC O14523; Q9Y320: TMX2; NbExp=3; IntAct=EBI-12822627, EBI-6447886;
CC O14523; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-12822627, EBI-12837904;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:28209843}; Single-pass membrane protein
CC {ECO:0000269|PubMed:28209843}. Cell membrane
CC {ECO:0000269|PubMed:28209843}; Peripheral membrane protein
CC {ECO:0000269|PubMed:28209843}. Note=Localizes to sites of contact
CC between the endoplasmic reticulum and the cell membrane
CC (PubMed:28209843). Embedded into the endoplasmic reticulum membrane via
CC its N-terminal transmembrane domain and associates with cell membrane
CC via its C-terminus (PubMed:28209843). In response to elevation of
CC cytosolic Ca(2+), it is phosphorylated at its C-terminus and
CC dissociates from the cell membrane and localizes to the reticular
CC endoplasmic reticulum (PubMed:28209843). Reassociates with cell
CC membrane upon dephosphorylation (PubMed:28209843).
CC {ECO:0000269|PubMed:28209843}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O14523-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14523-2; Sequence=VSP_021158;
CC -!- DOMAIN: The SMP-LBD domain is a lipid transport module, which binds
CC glycerolipids with a preference for phosphatidylinositol (PI).
CC {ECO:0000269|PubMed:28209843}.
CC -!- PTM: Phosphorylation at the C-terminus acidifies the protein and leads
CC to disassociation from the acidic cell membrane. Reassociates with the
CC cell membrane upon dephosphorylation. {ECO:0000269|PubMed:28209843}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH10071.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH21254.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB094094; BAC76048.1; -; mRNA.
DR EMBL; BC010071; AAH10071.2; ALT_INIT; mRNA.
DR EMBL; BC021254; AAH21254.2; ALT_INIT; mRNA.
DR EMBL; BC022219; AAH22219.1; -; mRNA.
DR EMBL; BC033083; AAH33083.1; -; mRNA.
DR EMBL; BC052246; AAH52246.1; -; mRNA.
DR EMBL; AB006623; BAA22954.2; -; mRNA.
DR CCDS; CCDS8413.1; -. [O14523-2]
DR RefSeq; NP_001277403.1; NM_001290474.1. [O14523-1]
DR RefSeq; NP_055622.3; NM_014807.4. [O14523-2]
DR PDB; 5TOD; X-ray; 2.96 A; A/B/C/D/E/F=76-260.
DR PDBsum; 5TOD; -.
DR AlphaFoldDB; O14523; -.
DR SMR; O14523; -.
DR BioGRID; 115188; 105.
DR IntAct; O14523; 58.
DR MINT; O14523; -.
DR STRING; 9606.ENSP00000338885; -.
DR TCDB; 8.A.78.1.1; the insulin secretion-regulating lipid transporter tmem24 (tmem24) family.
DR GlyGen; O14523; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; O14523; -.
DR PhosphoSitePlus; O14523; -.
DR SwissPalm; O14523; -.
DR BioMuta; C2CD2L; -.
DR EPD; O14523; -.
DR jPOST; O14523; -.
DR MassIVE; O14523; -.
DR MaxQB; O14523; -.
DR PaxDb; O14523; -.
DR PeptideAtlas; O14523; -.
DR PRIDE; O14523; -.
DR ProteomicsDB; 48067; -. [O14523-1]
DR ProteomicsDB; 48068; -. [O14523-2]
DR Antibodypedia; 32613; 61 antibodies from 17 providers.
DR DNASU; 9854; -.
DR Ensembl; ENST00000336702.7; ENSP00000338885.3; ENSG00000172375.14. [O14523-2]
DR Ensembl; ENST00000648610.2; ENSP00000497391.1; ENSG00000172375.14. [O14523-1]
DR GeneID; 9854; -.
DR KEGG; hsa:9854; -.
DR MANE-Select; ENST00000648610.2; ENSP00000497391.1; NM_001290474.2; NP_001277403.1.
DR UCSC; uc001pvn.4; human. [O14523-1]
DR CTD; 9854; -.
DR GeneCards; C2CD2L; -.
DR HGNC; HGNC:29000; C2CD2L.
DR HPA; ENSG00000172375; Low tissue specificity.
DR MIM; 617582; gene.
DR neXtProt; NX_O14523; -.
DR OpenTargets; ENSG00000172375; -.
DR PharmGKB; PA162379049; -.
DR VEuPathDB; HostDB:ENSG00000172375; -.
DR eggNOG; ENOG502QRBG; Eukaryota.
DR GeneTree; ENSGT00530000063764; -.
DR HOGENOM; CLU_024872_1_0_1; -.
DR InParanoid; O14523; -.
DR OMA; ISHVTCT; -.
DR OrthoDB; 307984at2759; -.
DR PhylomeDB; O14523; -.
DR TreeFam; TF331604; -.
DR PathwayCommons; O14523; -.
DR SignaLink; O14523; -.
DR BioGRID-ORCS; 9854; 9 hits in 1082 CRISPR screens.
DR GenomeRNAi; 9854; -.
DR Pharos; O14523; Tbio.
DR PRO; PR:O14523; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O14523; protein.
DR Bgee; ENSG00000172375; Expressed in right frontal lobe and 159 other tissues.
DR ExpressionAtlas; O14523; baseline and differential.
DR Genevisible; O14523; HS.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140268; C:endoplasmic reticulum-plasma membrane contact site; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0043559; F:insulin binding; IEA:Ensembl.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; IDA:UniProtKB.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:UniProtKB.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR039934; C2CD2/C2CD2L.
DR InterPro; IPR040885; SMP_C2CD2L.
DR PANTHER; PTHR21119; PTHR21119; 1.
DR Pfam; PF18696; SMP_C2CD2L; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Endoplasmic reticulum;
KW Lipid transport; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..706
FT /note="Phospholipid transfer protein C2CD2L"
FT /id="PRO_0000072596"
FT TOPO_DOM 1..9
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:28209843"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..706
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:28209843"
FT DOMAIN 76..260
FT /note="SMP-LBD"
FT /evidence="ECO:0000269|PubMed:28209843,
FT ECO:0007744|PDB:5TOD"
FT DOMAIN 268..389
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 409..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..706
FT /note="Association with the cell membrane"
FT /evidence="ECO:0000269|PubMed:28209843"
FT REGION 449..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80X80"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 417
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 419
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q80X80"
FT MOD_RES 428
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80X80"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80X80"
FT MOD_RES 621
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q80X80"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 497
FT /note="R -> PG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_021158"
FT VARIANT 413
FT /note="R -> W (in dbSNP:rs2239896)"
FT /id="VAR_028797"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:5TOD"
FT HELIX 96..114
FT /evidence="ECO:0007829|PDB:5TOD"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:5TOD"
FT STRAND 133..145
FT /evidence="ECO:0007829|PDB:5TOD"
FT STRAND 147..171
FT /evidence="ECO:0007829|PDB:5TOD"
FT STRAND 174..198
FT /evidence="ECO:0007829|PDB:5TOD"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:5TOD"
FT STRAND 202..211
FT /evidence="ECO:0007829|PDB:5TOD"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:5TOD"
FT HELIX 235..248
FT /evidence="ECO:0007829|PDB:5TOD"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:5TOD"
SQ SEQUENCE 706 AA; 76181 MW; 9301A8BDF6D4D5B6 CRC64;
MDPGWGQRDV GWAALLILFA ASLLTVFAWL LQYARGLWLA RARGDRGPGP ALAGEPAGSL
RELGVWRSLL RLRATRAGAA EEPGVRGLLA SLFAFKSFRE NWQRAWVRAL NEQACRNGSS
IQIAFEEVPQ LPPRASISHV TCVDQSEHTM VLRCQLSAEE VRFPVSVTQQ SPAAVSMETY
HVTLTLPPTQ LEVNLEEIPG EGLLISWAFT DRPDLSLTVL PKLQARERGE EQVELSTIEE
LIKDAIVSTQ PAMMVNLRAC SAPGGLVPSE KPPMMPQAQP AIPRPNRLFL RQLRASHLGN
ELEGTEELCC VAELDNPMQQ KWTKPARAGS EVEWTEDLAL DLGPQSRELT LKVLRSSSCG
DTELLGQATL PVGSPSRPLS RRQLCPLTPG PGKALGPAAT MAVELHYEEG SPRNLGTPTS
STPRPSITPT KKIELDRTIM PDGTIVTTVT TVQSRPRIDG KLDSPSRSPS KVEVTEKTTT
VLSESSGPSN TSHSSSRDSH LSNGLDPVAE TAIRQLTEPS GRVAKKTPTK RSTLIISGVS
KVPIAQDELA LSLGYAASLE ASVQDDAGTS GGPSSPPSDP PAMSPGPLDA LSSPTSVQEA
DETTRSDISE RPSVDDIESE TGSTGALETR SLKDHKVSFL RSGTKLIFRR RPRQKEAGLS
QSHDDLSNAT ATPSVRKKAG SFSRRLIKRF SFKSKPKANG NPSPQL
