CIP4_MOUSE
ID CIP4_MOUSE Reviewed; 603 AA.
AC Q8CJ53; Q8BTR8; Q8R433; Q99LI0;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Cdc42-interacting protein 4;
DE AltName: Full=Thyroid receptor-interacting protein 10;
DE Short=TR-interacting protein 10;
DE Short=TRIP-10;
GN Name=Trip10; Synonyms=Cip4;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Heart;
RX PubMed=12054674; DOI=10.1016/s0006-291x(02)00398-4;
RA Wang L., Rudert W.A., Grishin A., Dombrosky-Ferlan P., Sullivan K.,
RA Deng X., Whitcomb D., Corey S.J.;
RT "Identification and genetic analysis of human and mouse activated Cdc42
RT interacting protein-4 isoforms.";
RL Biochem. Biophys. Res. Commun. 293:1426-1430(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CDC42
RP AND RHOQ, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ILE-454.
RC TISSUE=Adipocyte;
RX PubMed=12242347; DOI=10.1073/pnas.202495599;
RA Chang L., Adams R.D., Saltiel A.R.;
RT "The TC10-interacting protein CIP4/2 is required for insulin-stimulated
RT Glut4 translocation in 3T3L1 adipocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12835-12840(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [5]
RP PROTEIN SEQUENCE OF 98-104, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=16735024; DOI=10.1016/j.bbrc.2006.05.073;
RA Archila S., King M.A., Carlson G.M., Rice N.A.;
RT "The cytoskeletal organizing protein Cdc42-interacting protein 4 associates
RT with phosphorylase kinase in skeletal muscle.";
RL Biochem. Biophys. Res. Commun. 345:1592-1599(2006).
RN [7]
RP FUNCTION, INTERACTION WITH DNM2 AND WASL, AND SUBCELLULAR LOCATION.
RX PubMed=16418535; DOI=10.1083/jcb.200508091;
RA Tsujita K., Suetsugu S., Sasaki N., Furutani M., Oikawa T., Takenawa T.;
RT "Coordination between the actin cytoskeleton and membrane deformation by a
RT novel membrane tubulation domain of PCH proteins is involved in
RT endocytosis.";
RL J. Cell Biol. 172:269-279(2006).
RN [8]
RP INTERACTION WITH GAPVD1.
RX PubMed=17189207; DOI=10.1016/j.cmet.2006.12.006;
RA Lodhi I.J., Chiang S.-H., Chang L., Vollenweider D., Watson R.T., Inoue M.,
RA Pessin J.E., Saltiel A.R.;
RT "Gapex-5, a Rab31 guanine nucleotide exchange factor that regulates Glut4
RT trafficking in adipocytes.";
RL Cell Metab. 5:59-72(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen, and
RC Testis;
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).
CC -!- FUNCTION: Required to coordinate membrane tubulation with
CC reorganization of the actin cytoskeleton during endocytosis. Binds to
CC lipids such as phosphatidylinositol 4,5-bisphosphate and
CC phosphatidylserine and promotes membrane invagination and the formation
CC of tubules. Also promotes CDC42-induced actin polymerization by
CC recruiting WASL/N-WASP which in turn activates the Arp2/3 complex.
CC Actin polymerization may promote the fission of membrane tubules to
CC form endocytic vesicles. Required for the formation of podosomes,
CC actin-rich adhesion structures specific to monocyte-derived cells. May
CC be required for the lysosomal retention of FASLG/FASL (By similarity).
CC Required for translocation of GLUT4 to the plasma membrane in response
CC to insulin signaling. {ECO:0000250, ECO:0000269|PubMed:12242347,
CC ECO:0000269|PubMed:16418535}.
CC -!- SUBUNIT: Homodimerizes, the dimers can polymerize end-to-end to form
CC filamentous structures (By similarity). Interacts with AKAP9, ARHGAP17,
CC DAAM1, DIAPH1, DIAPH2, DNM1, FASLG/FASL, GAPVD1, LYN, microtubules,
CC PDE6G, SRC and WAS/WASP. Interacts with the ligand binding domain of
CC the thyroid receptor (TR) in the presence of thyroid hormone. May
CC interact with CTNNB1 and HD/HTT (By similarity). Interacts specifically
CC with GTP-bound CDC42 and RHOQ. Interacts with DNM2 and WASL.
CC {ECO:0000250, ECO:0000269|PubMed:12242347, ECO:0000269|PubMed:16418535,
CC ECO:0000269|PubMed:17189207}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
CC Lysosome. Golgi apparatus {ECO:0000250}. Cell membrane. Cell
CC projection, phagocytic cup {ECO:0000250}. Note=Localizes to cortical
CC regions coincident with F-actin, to lysosomes and to sites of
CC phagocytosis in macrophages. Also localizes to the Golgi, and this
CC requires AKAP9 (By similarity). Translocates to the plasma membrane in
CC response to insulin stimulation, and this may require active RHOQ.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Cip4/2;
CC IsoId=Q8CJ53-1; Sequence=Displayed;
CC Name=2; Synonyms=H;
CC IsoId=Q8CJ53-2; Sequence=VSP_021723;
CC Name=3;
CC IsoId=Q8CJ53-3; Sequence=VSP_021722;
CC Name=4;
CC IsoId=Q8CJ53-4; Sequence=VSP_021722, VSP_021723;
CC -!- DOMAIN: The F-BAR domain binds the phospholipid membrane with its
CC concave surface. The end-to-end polymerization of dimers of these
CC domains provides a curved surface that fits best membranes with around
CC 600 A diameter, and may drive tubulation (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Tyrosine phosphorylated. Also phosphorylated by PKA (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FNBP1 family. {ECO:0000305}.
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DR EMBL; AY081142; AAL89589.1; -; mRNA.
DR EMBL; AF502565; AAN38709.1; -; mRNA.
DR EMBL; AK088909; BAC40648.1; -; mRNA.
DR EMBL; AK149902; BAE29155.1; -; mRNA.
DR EMBL; BC003249; AAH03249.1; -; mRNA.
DR CCDS; CCDS28930.1; -. [Q8CJ53-3]
DR CCDS; CCDS89129.1; -. [Q8CJ53-1]
DR CCDS; CCDS89130.1; -. [Q8CJ53-2]
DR CCDS; CCDS89131.1; -. [Q8CJ53-4]
DR RefSeq; NP_001229318.1; NM_001242389.1. [Q8CJ53-1]
DR RefSeq; NP_001229319.1; NM_001242390.1. [Q8CJ53-2]
DR RefSeq; NP_001229320.1; NM_001242391.1. [Q8CJ53-4]
DR RefSeq; NP_598886.1; NM_134125.4. [Q8CJ53-3]
DR AlphaFoldDB; Q8CJ53; -.
DR SMR; Q8CJ53; -.
DR BioGRID; 223098; 6.
DR STRING; 10090.ENSMUSP00000019631; -.
DR iPTMnet; Q8CJ53; -.
DR PhosphoSitePlus; Q8CJ53; -.
DR EPD; Q8CJ53; -.
DR jPOST; Q8CJ53; -.
DR MaxQB; Q8CJ53; -.
DR PeptideAtlas; Q8CJ53; -.
DR PRIDE; Q8CJ53; -.
DR ProteomicsDB; 283559; -. [Q8CJ53-1]
DR ProteomicsDB; 283560; -. [Q8CJ53-2]
DR ProteomicsDB; 283561; -. [Q8CJ53-3]
DR ProteomicsDB; 283562; -. [Q8CJ53-4]
DR Antibodypedia; 11922; 269 antibodies from 33 providers.
DR DNASU; 106628; -.
DR Ensembl; ENSMUST00000019631; ENSMUSP00000019631; ENSMUSG00000019487. [Q8CJ53-4]
DR Ensembl; ENSMUST00000224152; ENSMUSP00000153081; ENSMUSG00000019487. [Q8CJ53-1]
DR Ensembl; ENSMUST00000224885; ENSMUSP00000153576; ENSMUSG00000019487. [Q8CJ53-2]
DR Ensembl; ENSMUST00000224947; ENSMUSP00000153467; ENSMUSG00000019487. [Q8CJ53-3]
DR GeneID; 106628; -.
DR KEGG; mmu:106628; -.
DR UCSC; uc008dej.2; mouse. [Q8CJ53-3]
DR UCSC; uc008dek.2; mouse. [Q8CJ53-1]
DR UCSC; uc008del.2; mouse. [Q8CJ53-2]
DR UCSC; uc008dem.2; mouse. [Q8CJ53-4]
DR CTD; 9322; -.
DR MGI; MGI:2146901; Trip10.
DR VEuPathDB; HostDB:ENSMUSG00000019487; -.
DR GeneTree; ENSGT00950000183047; -.
DR HOGENOM; CLU_023320_1_0_1; -.
DR InParanoid; Q8CJ53; -.
DR OMA; QERKTHF; -.
DR OrthoDB; 348563at2759; -.
DR PhylomeDB; Q8CJ53; -.
DR TreeFam; TF351162; -.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR BioGRID-ORCS; 106628; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Trip10; mouse.
DR PRO; PR:Q8CJ53; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8CJ53; protein.
DR Bgee; ENSMUSG00000019487; Expressed in interventricular septum and 218 other tissues.
DR ExpressionAtlas; Q8CJ53; baseline and differential.
DR Genevisible; Q8CJ53; MM.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; TAS:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISO:MGI.
DR GO; GO:0042538; P:hyperosmotic salinity response; ISO:MGI.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; ISO:MGI.
DR GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR028498; CIP4.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR15735:SF17; PTHR15735:SF17; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS51860; REM_1; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Coiled coil;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Endocytosis;
KW Golgi apparatus; Lipid-binding; Lysosome; Membrane; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1..603
FT /note="Cdc42-interacting protein 4"
FT /id="PRO_0000261439"
FT DOMAIN 1..264
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 393..470
FT /note="REM-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 542..603
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..117
FT /note="Required for podosome formation and interaction with
FT AKAP9 and microtubules"
FT /evidence="ECO:0000250"
FT REGION 1..117
FT /note="Required for translocation to the plasma membrane in
FT response to insulin"
FT REGION 293..603
FT /note="Interaction with PDE6G"
FT /evidence="ECO:0000250"
FT REGION 293..539
FT /note="Interaction with CDC42"
FT /evidence="ECO:0000250"
FT REGION 295..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..603
FT /note="Required for interaction with FASLG and localization
FT to lysosomes"
FT /evidence="ECO:0000250"
FT REGION 477..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..543
FT /note="Interaction with DNM2 and WASL"
FT /evidence="ECO:0000269|PubMed:16418535"
FT REGION 532..603
FT /note="Interaction with DNM1 and WASL"
FT /evidence="ECO:0000250"
FT REGION 540..603
FT /note="Required for podosome formation"
FT /evidence="ECO:0000250"
FT REGION 546..603
FT /note="Interaction with WAS"
FT /evidence="ECO:0000250"
FT REGION 548..603
FT /note="Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2"
FT /evidence="ECO:0000250"
FT COILED 67..259
FT /evidence="ECO:0000250"
FT COILED 388..481
FT /evidence="ECO:0000250"
FT COMPBIAS 498..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 166
FT /note="Mediates end-to-end attachment of dimers"
FT /evidence="ECO:0000250"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15642"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15642"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15642"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15642"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15642"
FT VAR_SEQ 329..384
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_021722"
FT VAR_SEQ 515
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12054674,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_021723"
FT MUTAGEN 454
FT /note="I->S: Impairs interaction with CDC42 and RHOQ and
FT reduces insulin-stimulated translocation to the plasma
FT membrane."
FT /evidence="ECO:0000269|PubMed:12242347"
FT CONFLICT 321
FT /note="W -> C (in Ref. 2; AAN38709)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 603 AA; 68489 MW; DDA6271D5FD515AC CRC64;
MDWGTELWDQ FEVLERHTQW GLDLLDKYVK FVKERAEVEQ AYAKQLRSLV KKYLPKRPTK
DDPEVKFSQQ QSFVQLLQEV NDFAGQRELV AESLGIRVCL ELAKYSQEMK QERKMHFQEG
RRAQQQLENG FKQLENSKRK FERDCREAEK AAHTAERLDQ DINATKADVE KAKQQAHLRN
HMAEESKNEY AAQLQRFNRD QAHFYFSQMP QIFDKLQDMD ERRATRLGAG YGLLSEAELQ
VVPIIGKCLE GMKVAAESVD AKNDSQVLIE LHKSGFARPG DLEFEDFSQV INRVPSDSSL
GTPDGRPELR AASSRSRAKR WPFGKKNKPR PPSLSLLGGH LPSTLSDGPS SPRSGRDPLA
ILSEISKSVK PRLASFRSFR GGRGTVATED FSHLPPEQQR KRLQQQLEER NRELQKEEDQ
REALKKMKDV YEKTPQMGDP ASLEPRIAET LGNIERLKLE VQKYEAWLAE AESRVLSNRG
DSLSRHARPP DPPTTAPPDS SSSSTNSGSQ DNKESSSEEP PSEGQDTPIY TEFDEDFEEP
ASPIGQCVAI YHFEGSSEGT VSMSEGEDLS LMEEDKGDGW TRVRRKQGAE GYVPTSYLRV
TLN
