ID KALRN_HUMAN Reviewed; 2986 AA. AC O60229; A8MSI4; C9JQ37; J3QSW6; Q6ZN45; Q8TBQ5; Q9NSZ4; Q9Y2A5; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 31-JUL-2019, sequence version 3. DT 24-JAN-2024, entry version 218. DE RecName: Full=Kalirin {ECO:0000250|UniProtKB:P97924}; DE EC=2.7.11.1; DE AltName: Full=Huntingtin-associated protein-interacting protein; DE AltName: Full=Protein Duo; DE AltName: Full=Serine/threonine-protein kinase with Dbl- and pleckstrin homology domain; GN Name=KALRN {ECO:0000312|HGNC:HGNC:4814}; GN Synonyms=DUET, DUO, HAPIP, TRAD; 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). RC TISSUE=Frontal cortex; RX PubMed=9285789; DOI=10.1093/hmg/6.9.1519; RA Colomer V., Engelender S., Sharp A.H., Duan K., Cooper J.K., Lanahan A., RA Lyford G., Worley P., Ross C.A.; RT "Huntingtin-associated protein 1 (HAP1) binds to a Trio-like polypeptide, RT with a rac1 guanine nucleotide exchange factor domain."; RL Hum. Mol. Genet. 6:1519-1525(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, MUTAGENESIS OF LYS-2713, RP AUTOPHOSPHORYLATION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RC TISSUE=Skeletal muscle; RX PubMed=10023074; DOI=10.1016/s0378-1119(98)00605-2; RA Kawai T., Sanjo H., Akira S.; RT "Duet is a novel serine/threonine kinase with Dbl-homology (DH) and RT pleckstrin-homology (PH) domains."; RL Gene 227:249-255(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 641-1464 (ISOFORM 1). RC TISSUE=Amygdala, and Testis; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [5] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1917 (ISOFORM 6), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2105-2986 (ISOFORM 5). RC TISSUE=Kidney; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2017-2986 (ISOFORM 5). RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1750; SER-1753; SER-1799; RP SER-1817 AND SER-2262, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1799, AND IDENTIFICATION BY RP 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 [10] RP INTERACTION WITH FASLG. RX PubMed=19807924; DOI=10.1186/1471-2172-10-53; RA Voss M., Lettau M., Janssen O.; RT "Identification of SH3 domain interaction partners of human FasL (CD178) by RT phage display screening."; RL BMC Immunol. 10:53-53(2009). RN [11] RP SPECTRIN REPEATS. RX PubMed=22738176; DOI=10.1021/bi300583s; RA Vishwanatha K.S., Wang Y.P., Keutmann H.T., Mains R.E., Eipper B.A.; RT "Structural organization of the nine spectrin repeats of Kalirin."; RL Biochemistry 51:5663-5673(2012). RN [12] RP VARIANTS [LARGE SCALE ANALYSIS] TRP-213 AND CYS-1897. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [13] RP VARIANT [LARGE SCALE ANALYSIS] LEU-196. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Promotes the exchange of GDP by GTP. Activates specific Rho CC GTPase family members, thereby inducing various signaling mechanisms CC that regulate neuronal shape, growth, and plasticity, through their CC effects on the actin cytoskeleton. Induces lamellipodia independent of CC its GEF activity. {ECO:0000269|PubMed:10023074}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- SUBUNIT: Interacts with the C-terminal of peptidylglycine alpha- CC amidating monooxygenase (PAM) and with the huntingtin-associated CC protein 1 (HAP1) (By similarity). Interacts with FASLG. {ECO:0000250, CC ECO:0000269|PubMed:19807924}. CC -!- INTERACTION: CC O60229; PRO_0000449631 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-949233, EBI-25475920; CC O60229; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-949233, EBI-25492395; CC O60229-2; Q9Y6H5-1: SNCAIP; NbExp=3; IntAct=EBI-9075360, EBI-9075374; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10023074}. CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10023074}. Note=Associated CC with the cytoskeleton. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=O60229-1; Sequence=Displayed; CC Name=2; CC IsoId=O60229-2; Sequence=VSP_028910, VSP_028911; CC Name=4; Synonyms=DUET, TRAD; CC IsoId=O60229-4; Sequence=VSP_028903, VSP_028912; CC Name=5; CC IsoId=O60229-5; Sequence=VSP_028904, VSP_028909, VSP_028913, CC VSP_028914, VSP_028915; CC Name=6; CC IsoId=O60229-6; Sequence=VSP_028903, VSP_028912, VSP_028913; CC -!- TISSUE SPECIFICITY: Isoform 2 is brain specific. Highly expressed in CC cerebral cortex, putamen, amygdala, hippocampus and caudate nucleus. CC Weakly expressed in brain stem and cerebellum. Isoform 4 is expressed CC in skeletal muscle. {ECO:0000269|PubMed:10023074}. CC -!- DOMAIN: The two GEF domains catalyze nucleotide exchange for RAC1 and CC RhoA which are bound by DH1 and DH2 respectively. The two GEF domains CC appear to play differing roles in neuronal development and axonal CC outgrowth. SH3 1 binds to the first GEF domain inhibiting GEF activity CC only when in the presence of a PXXP peptide, suggesting that the SH3 CC domain/peptide interaction mediates binding to GEF1. CRK1 SH3 domain CC binds to and inhibits GEF1 activity (By similarity). {ECO:0000250}. CC -!- PTM: Autophosphorylated. CC -!- MISCELLANEOUS: Called DUO because the encoded protein is closely CC related to but shorter than TRIO. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr CC protein kinase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH58015.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=BAD18530.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U94190; AAC15791.1; -; mRNA. DR EMBL; AB011422; BAA76314.1; -; mRNA. DR EMBL; AK125979; BAC86373.1; -; mRNA. DR EMBL; AK131379; BAD18530.1; ALT_SEQ; mRNA. DR EMBL; AC022336; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC069233; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC080008; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC112129; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC117401; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF457679; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471052; EAW79410.1; -; Genomic_DNA. DR EMBL; BC026865; AAH26865.1; -; mRNA. DR EMBL; BC058015; AAH58015.1; ALT_SEQ; mRNA. DR EMBL; AL137629; CAB70850.1; -; mRNA. DR CCDS; CCDS3027.1; -. [O60229-2] DR CCDS; CCDS3028.1; -. [O60229-4] DR PIR; T46482; T46482. DR RefSeq; NP_001019831.2; NM_001024660.4. [O60229-1] DR RefSeq; NP_001309917.1; NM_001322988.1. DR RefSeq; NP_001309918.1; NM_001322989.1. DR RefSeq; NP_001309923.1; NM_001322994.1. DR RefSeq; NP_001309924.1; NM_001322995.1. DR RefSeq; NP_001309925.1; NM_001322996.1. DR RefSeq; NP_001309926.1; NM_001322997.1. DR RefSeq; NP_001309927.1; NM_001322998.1. DR RefSeq; NP_001309928.1; NM_001322999.1. DR RefSeq; NP_001309929.1; NM_001323000.1. DR RefSeq; NP_001309930.1; NM_001323001.1. DR RefSeq; NP_003938.1; NM_003947.5. [O60229-2] DR RefSeq; NP_008995.2; NM_007064.4. [O60229-4] DR PDB; 5QQD; X-ray; 1.91 A; B=1280-1459. DR PDB; 5QQE; X-ray; 1.95 A; B=1280-1459. DR PDB; 5QQF; X-ray; 2.26 A; B=1280-1459. DR PDB; 5QQG; X-ray; 2.23 A; B=1280-1459. DR PDB; 5QQH; X-ray; 2.09 A; B=1280-1459. DR PDB; 5QQI; X-ray; 2.08 A; B=1280-1459. DR PDB; 5QQJ; X-ray; 1.90 A; B=1280-1459. DR PDB; 5QQK; X-ray; 2.24 A; B=1280-1459. DR PDB; 5QQL; X-ray; 2.25 A; B=1280-1459. DR PDB; 5QQM; X-ray; 2.02 A; B=1280-1459. DR PDB; 5QQN; X-ray; 2.26 A; B=1280-1459. DR PDB; 5QU9; X-ray; 2.00 A; B=1280-1459. DR PDBsum; 5QQD; -. DR PDBsum; 5QQE; -. DR PDBsum; 5QQF; -. DR PDBsum; 5QQG; -. DR PDBsum; 5QQH; -. DR PDBsum; 5QQI; -. DR PDBsum; 5QQJ; -. DR PDBsum; 5QQK; -. DR PDBsum; 5QQL; -. DR PDBsum; 5QQM; -. DR PDBsum; 5QQN; -. DR PDBsum; 5QU9; -. DR SMR; O60229; -. DR BioGRID; 114478; 29. DR IntAct; O60229; 27. DR MINT; O60229; -. DR STRING; 9606.ENSP00000240874; -. DR GlyGen; O60229; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O60229; -. DR PhosphoSitePlus; O60229; -. DR SwissPalm; O60229; -. DR BioMuta; KALRN; -. DR EPD; O60229; -. DR jPOST; O60229; -. DR MassIVE; O60229; -. DR MaxQB; O60229; -. DR PaxDb; 9606-ENSP00000240874; -. DR PeptideAtlas; O60229; -. DR ProteomicsDB; 11196; -. DR ProteomicsDB; 49252; -. [O60229-1] DR ProteomicsDB; 49253; -. [O60229-2] DR ProteomicsDB; 49255; -. [O60229-4] DR ProteomicsDB; 49256; -. [O60229-5] DR ProteomicsDB; 49257; -. [O60229-6] DR Pumba; O60229; -. DR Antibodypedia; 2142; 205 antibodies from 34 providers. DR DNASU; 8997; -. DR Ensembl; ENST00000240874.7; ENSP00000240874.3; ENSG00000160145.16. [O60229-2] DR Ensembl; ENST00000291478.9; ENSP00000291478.4; ENSG00000160145.16. [O60229-4] DR Ensembl; ENST00000360013.7; ENSP00000353109.3; ENSG00000160145.16. [O60229-1] DR GeneID; 8997; -. DR KEGG; hsa:8997; -. DR UCSC; uc003ehf.2; human. [O60229-1] DR AGR; HGNC:4814; -. DR CTD; 8997; -. DR DisGeNET; 8997; -. DR GeneCards; KALRN; -. DR HGNC; HGNC:4814; KALRN. DR HPA; ENSG00000160145; Tissue enhanced (brain). DR MalaCards; KALRN; -. DR MIM; 604605; gene. DR neXtProt; NX_O60229; -. DR OpenTargets; ENSG00000160145; -. DR PharmGKB; PA29189; -. DR VEuPathDB; HostDB:ENSG00000160145; -. DR eggNOG; KOG4240; Eukaryota. DR GeneTree; ENSGT00940000155248; -. DR HOGENOM; CLU_000373_0_1_1; -. DR InParanoid; O60229; -. DR OMA; AKXFIMA; -. DR OrthoDB; 2906033at2759; -. DR PhylomeDB; O60229; -. DR TreeFam; TF318080; -. DR PathwayCommons; O60229; -. DR Reactome; R-HSA-193648; NRAGE signals death through JNK. DR Reactome; R-HSA-3928662; EPHB-mediated forward signaling. DR Reactome; R-HSA-416476; G alpha (q) signalling events. DR Reactome; R-HSA-416482; G alpha (12/13) signalling events. DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling. DR Reactome; R-HSA-8980692; RHOA GTPase cycle. DR Reactome; R-HSA-9013149; RAC1 GTPase cycle. DR Reactome; R-HSA-9013408; RHOG GTPase cycle. DR SignaLink; O60229; -. DR SIGNOR; O60229; -. DR BioGRID-ORCS; 8997; 10 hits in 1180 CRISPR screens. DR ChiTaRS; KALRN; human. DR GeneWiki; Kalirin; -. DR GenomeRNAi; 8997; -. DR Pharos; O60229; Tbio. DR PRO; PR:O60229; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; O60229; Protein. DR Bgee; ENSG00000160145; Expressed in secondary oocyte and 167 other cell types or tissues. DR ExpressionAtlas; O60229; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; EXP:Reactome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:ProtInc. DR GO; GO:0007411; P:axon guidance; IBA:GO_Central. DR GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome. DR GO; GO:0035556; P:intracellular signal transduction; ISS:HGNC-UCL. DR GO; GO:0007399; P:nervous system development; ISS:HGNC-UCL. DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc. DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc. DR CDD; cd00063; FN3; 1. DR CDD; cd13240; PH1_Kalirin_Trio_like; 1. DR CDD; cd13241; PH2_Kalirin_Trio_p63RhoGEF; 1. DR CDD; cd00160; RhoGEF; 2. DR CDD; cd00170; SEC14; 1. DR CDD; cd11852; SH3_Kalirin_1; 1. DR CDD; cd11853; SH3_Kalirin_2; 1. DR CDD; cd00176; SPEC; 4. DR CDD; cd14115; STKc_Kalirin_C; 1. DR Gene3D; 1.20.58.60; -; 5. DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1. DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 2. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2. DR Gene3D; 2.30.30.40; SH3 Domains; 2. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR001251; CRAL-TRIO_dom. DR InterPro; IPR036865; CRAL-TRIO_dom_sf. DR InterPro; IPR035899; DBL_dom_sf. DR InterPro; IPR000219; DH-domain. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR047054; Kalirin_TRIO_PH_1. DR InterPro; IPR028570; Kalirin_TRIO_SH3_1. DR InterPro; IPR047053; Kalirin_TRIO_SH3_2. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR018159; Spectrin/alpha-actinin. DR InterPro; IPR002017; Spectrin_repeat. DR PANTHER; PTHR22826:SF49; KALIRIN; 1. DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1. DR Pfam; PF13716; CRAL_TRIO_2; 1. DR Pfam; PF00041; fn3; 1. DR Pfam; PF07679; I-set; 1. DR Pfam; PF00169; PH; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00621; RhoGEF; 2. DR Pfam; PF16609; SH3-RhoG_link; 1. DR Pfam; PF00435; Spectrin; 4. DR SMART; SM00060; FN3; 1. DR SMART; SM00409; IG; 1. DR SMART; SM00408; IGc2; 1. DR SMART; SM00233; PH; 2. DR SMART; SM00325; RhoGEF; 2. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00516; SEC14; 1. DR SMART; SM00326; SH3; 2. DR SMART; SM00150; SPEC; 7. DR SUPFAM; SSF52087; CRAL/TRIO domain; 1. DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 2. DR SUPFAM; SSF49265; Fibronectin type III; 1. DR SUPFAM; SSF50729; PH domain-like; 2. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF50044; SH3-domain; 2. DR SUPFAM; SSF46966; Spectrin repeat; 6. DR PROSITE; PS50191; CRAL_TRIO; 1. DR PROSITE; PS50010; DH_2; 2. DR PROSITE; PS50853; FN3; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS50003; PH_DOMAIN; 2. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50002; SH3; 2. DR Genevisible; O60229; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Cytoskeleton; KW Disulfide bond; Guanine-nucleotide releasing factor; Immunoglobulin domain; KW Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Repeat; Serine/threonine-protein kinase; SH3 domain; KW Transferase. FT CHAIN 1..2986 FT /note="Kalirin" FT /id="PRO_0000080955" FT DOMAIN 35..180 FT /note="CRAL-TRIO" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056" FT REPEAT 167..308 FT /note="Spectrin 1" FT /evidence="ECO:0000255" FT REPEAT 310..417 FT /note="Spectrin 2" FT /evidence="ECO:0000255" FT REPEAT 418..535 FT /note="Spectrin 3" FT /evidence="ECO:0000255" FT REPEAT 536..639 FT /note="Spectrin 4" FT /evidence="ECO:0000255" FT REPEAT 640..770 FT /note="Spectrin 5" FT /evidence="ECO:0000255" FT REPEAT 771..888 FT /note="Spectrin 6" FT /evidence="ECO:0000255" FT REPEAT 889..1004 FT /note="Spectrin 7" FT /evidence="ECO:0000255" FT REPEAT 1005..1128 FT /note="Spectrin 8" FT /evidence="ECO:0000255" FT REPEAT 1129..1234 FT /note="Spectrin 9" FT /evidence="ECO:0000255" FT DOMAIN 1281..1456 FT /note="DH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062" FT DOMAIN 1468..1580 FT /note="PH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 1646..1711 FT /note="SH3 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 1929..2104 FT /note="DH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062" FT DOMAIN 2116..2226 FT /note="PH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 2321..2386 FT /note="SH3 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 2471..2564 FT /note="Ig-like C2-type" FT DOMAIN 2571..2665 FT /note="Fibronectin type-III" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 2684..2938 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 710..735 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1594..1642 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1750..1857 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2244..2310 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2412..2454 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 721..735 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1617..1642 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1750..1773 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1782..1804 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1813..1837 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2286..2300 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2412..2434 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 2803 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 2690..2698 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 2713 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT MOD_RES 1750 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087" FT MOD_RES 1753 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087" FT MOD_RES 1799 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:18669648" FT MOD_RES 1812 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P97924" FT MOD_RES 1817 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087" FT MOD_RES 1913 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:A2CG49" FT MOD_RES 2262 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087" FT DISULFID 2492..2548 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 1..1697 FT /note="Missing (in isoform 4 and isoform 6)" FT /evidence="ECO:0000303|PubMed:10023074" FT /id="VSP_028903" FT VAR_SEQ 1..1627 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005" FT /id="VSP_028904" FT VAR_SEQ 1628..1643 FT /note="ISIASRTSQNTVDSDK -> MLKWISWRQSKANKAQ (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005" FT /id="VSP_028909" FT VAR_SEQ 1644..1663 FT /note="LSGGCELTVVLQDFSAGHSS -> DGNLVPRWHLGPGDPFSTYV (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:9285789" FT /id="VSP_028910" FT VAR_SEQ 1664..2986 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9285789" FT /id="VSP_028911" FT VAR_SEQ 1698..1725 FT /note="EGLVPSSALCISHSRSSVEMDCFFPLVK -> MKGGDRAYTRGPSLGWLFAK FT CCCCFPCR (in isoform 4 and isoform 6)" FT /evidence="ECO:0000303|PubMed:10023074" FT /id="VSP_028912" FT VAR_SEQ 1857..1888 FT /note="Missing (in isoform 5 and isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005" FT /id="VSP_028913" FT VAR_SEQ 2314 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005" FT /id="VSP_028914" FT VAR_SEQ 2399..2986 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005" FT /id="VSP_028915" FT VARIANT 196 FT /note="S -> L" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041898" FT VARIANT 213 FT /note="R -> W (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs1187034389)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035976" FT VARIANT 1326 FT /note="E -> D (in dbSNP:rs2289838)" FT /id="VAR_020192" FT VARIANT 1897 FT /note="S -> C (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035625" FT VARIANT 1930 FT /note="R -> M (in dbSNP:rs35298864)" FT /id="VAR_057190" FT MUTAGEN 2713 FT /note="K->A: Loss of autophosphorylation." FT /evidence="ECO:0000269|PubMed:10023074" FT CONFLICT 2459 FT /note="E -> G (in Ref. 2; BAA76314)" FT /evidence="ECO:0000305" FT HELIX 1281..1305 FT /evidence="ECO:0007829|PDB:5QQJ" FT HELIX 1307..1313 FT /evidence="ECO:0007829|PDB:5QQJ" FT STRAND 1314..1316 FT /evidence="ECO:0007829|PDB:5QQJ" FT TURN 1320..1324 FT /evidence="ECO:0007829|PDB:5QQJ" FT HELIX 1326..1330 FT /evidence="ECO:0007829|PDB:5QQJ" FT HELIX 1333..1342 FT /evidence="ECO:0007829|PDB:5QQJ" FT HELIX 1344..1350 FT /evidence="ECO:0007829|PDB:5QQJ" FT TURN 1351..1353 FT /evidence="ECO:0007829|PDB:5QQJ" FT HELIX 1355..1358 FT /evidence="ECO:0007829|PDB:5QQJ" FT HELIX 1359..1364 FT /evidence="ECO:0007829|PDB:5QQJ" FT TURN 1365..1367 FT /evidence="ECO:0007829|PDB:5QQJ" FT HELIX 1368..1370 FT /evidence="ECO:0007829|PDB:5QQJ" FT HELIX 1371..1389 FT /evidence="ECO:0007829|PDB:5QQJ" FT HELIX 1393..1401 FT /evidence="ECO:0007829|PDB:5QQJ" FT HELIX 1407..1429 FT /evidence="ECO:0007829|PDB:5QQJ" FT HELIX 1437..1455 FT /evidence="ECO:0007829|PDB:5QQJ" SQ SEQUENCE 2986 AA; 340261 MW; EA7B559A9E4AFFA0 CRC64; MTDRFWDQWY LWYLRLLRLL DRGSFRNDGL KASDVLPILK EKVAFVSGGR DKRGGPILTF PARSNHDRIR QEDLRKLVTY LASVPSEDVC KRGFTVIIDM RGSKWDLIKP LLKTLQEAFP AEIHVALIIK PDNFWQKQKT NFGSSKFIFE TSMVSVEGLT KLVDPSQLTE EFDGSLDYNH EEWIELRLSL EEFFNSAVHL LSRLEDLQEM LARKEFPVDV EGSRRLIDEH TQLKKKVLKA PVEELDREGQ RLLQCIRCSD GFSGRNCIPG SADFQSLVPK ITSLLDKLHS TRQHLHQMWH VRKLKLDQCF QLRLFEQDAE KMFDWISHNK ELFLQSHTEI GVSYQYALDL QTQHNHFAMN SMNAYVNINR IMSVASRLSE AGHYASQQIK QISTQLDQEW KSFAAALDER STILAMSAVF HQKAEQFLSG VDAWCKMCSE GGLPSEMQDL ELAIHHHQTL YEQVTQAYTE VSQDGKALLD VLQRPLSPGN SESLTATANY SKAVHQVLDV VHEVLHHQRR LESIWQHRKV RLHQRLQLCV FQQDVQQVLD WIENHGEAFL SKHTGVGKSL HRARALQKRH DDFEEVAQNT YTNADKLLEA AEQLAQTGEC DPEEIYKAAR HLEVRIQDFV RRVEQRKLLL DMSVSFHTHT KELWTWMEDL QKEMLEDVCA DSVDAVQELI KQFQQQQTAT LDATLNVIKE GEDLIQQLRS APPSLGEPSE ARDSAVSNNK TPHSSSISHI ESVLQQLDDA QVQMEELFHE RKIKLDIFLQ LRIFEQYTIE VTAELDAWNE DLLRQMNDFN TEDLTLAEQR LQRHTERKLA MNNMTFEVIQ QGQDLHQYIT EVQASGIELI CEKDIDLAAQ VQELLEFLHE KQHELELNAE QTHKRLEQCL QLRHLQAEVK QVLGWIRNGE SMLNASLVNA SSLSEAEQLQ REHEQFQLAI ESLFHATSLQ KTHQSALQVQ QKAEVLLQAG HYDADAIREC AEKVALHWQQ LMLKMEDRLK LVNASVAFYK TSEQVCSVLE SLEQEYRRDE DWCGGRDKLG PAAEIDHVIP LISKHLEQKE AFLKACTLAR RNAEVFLKYI HRNNVSMPSV ASHTRGPEQQ VKAILSELLQ RENRVLHFWT LKKRRLDQCQ QYVVFERSAK QALDWIQETG EFYLSTHTST GETTEETQEL LKEYGEFRVP AKQTKEKVKL LIQLADSFVE KGHIHATEIR KWVTTVDKHY RDFSLRMGKY RYSLEKALGV NTEDNKDLEL DIIPASLSDR EVKLRDANHE VNEEKRKSAR KKEFIMAELL QTEKAYVRDL HECLETYLWE MTSGVEEIPP GILNKEHIIF GNIQEIYDFH NNIFLKELEK YEQLPEDVGH CFVTWADKFQ MYVTYCKNKP DSNQLILEHA GTFFDEIQQR HGLANSISSY LIKPVQRITK YQLLLKELLT CCEEGKGELK DGLEVMLSVP KKANDAMHVS MLEGFDENLD VQGELILQDA FQVWDPKSLI RKGRERHLFL FEISLVFSKE IKDSSGHTKY VYKNKLLTSE LGVTEHVEGD PCKFALWSGR TPSSDNKTVL KASNIETKQE WIKNIREVIQ ERIIHLKGAL KEPLQLPKTP AKQRNNSKRD GVEDIDSQGD GSSQPDTISI ASRTSQNTVD SDKLSGGCEL TVVLQDFSAG HSSELTIQVG QTVELLERPS ERPGWCLVRT TERSPPLEGL VPSSALCISH SRSSVEMDCF FPLVKDAYSH SSSENGGKSE SVANLQAQPS LNSIHSSPGP KRSTNTLKKW LTSPVRRLNS GKADGNIKKQ KKVRDGRKSF DLGSPKPGDE TTPQGDSADE KSKKGWGEDE PDEESHTPLP PPMKIFDNDP TQDEMSSSLL AARQASTEVP TAADLVNAIE KLVKNKLSLE GSSYRGSLKD PAGCLNEGMA PPTPPKNPEE EQKAKALRGR MFVLNELVQT EKDYVKDLGI VVEGFMKRIE EKGVPEDMRG KDKIVFGNIH QIYDWHKDFF LAELEKCIQE QDRLAQLFIK HERKLHIYVW YCQNKPRSEY IVAEYDAYFE EVKQEINQRL TLSDFLIKPI QRITKYQLLL KDFLRYSEKA GLECSDIEKA VELMCLVPKR CNDMMNLGRL QGFEGTLTAQ GKLLQQDTFY VIELDAGMQS RTKERRVFLF EQIVIFSELL RKGSLTPGYM FKRSIKMNYL VLEENVDNDP CKFALMNRET SERVVLQAAN ADIQQAWVQD INQVLETQRD FLNALQSPIE YQRKERSTAV MRSQPARLPQ ASPRPYSSVP AGSEKPPKGS SYNPPLPPLK ISTSNGSPGF EYHQPGDKFE ASKQNDLGGC NGTSSMAVIK DYYALKENEI CVSQGEVVQV LAVNQQNMCL VYQPASDHSP AAEGWVPGSI LAPLTKATAA ESSDGSIKKS CSWHTLRMRK RAEVENTGKN EATGPRKPKD ILGNKVSVKE TNSSEESECD DLDPNTSMEI LNPNFIQEVA PEFLVPLVDV TCLLGDTVIL QCKVCGRPKP TITWKGPDQN ILDTDNSSAT YTVSSCDSGE ITLKICNLMP QDSGIYTCIA TNDHGTTSTS ATVKVQGVPA APNRPIAQER SCTSVILRWL PPSSTGNCTI SGYTVEYREE GSQIWQQSVA STLDTYLVIE DLSPGCPYQF RVSASNPWGI SLPSEPSEFV RLPEYDAAAD GATISWKENF DSAYTELNEI GRGRFSIVKK CIHKATRKDV AVKFVSKKMK KKEQAAHEAA LLQHLQHPQY ITLHDTYESP TSYILILELM DDGRLLDYLM NHDELMEEKV AFYIRDIMEA LQYLHNCRVA HLDIKPENLL IDLRIPVPRV KLIDLEDAVQ ISGHFHIHHL LGNPEFAAPE VIQGIPVSLG TDIWSIGVLT YVMLSGVSPF LDESKEETCI NVCRVDFSFP HEYFCGVSNA ARDFINVILQ EDFRRRPTAA TCLQHPWLQP HNGSYSKIPL DTSRLACFIE RRKHQNDVRP IPNVKSYIVN RVNQGT //