ID ITSN2_HUMAN Reviewed; 1697 AA. AC Q9NZM3; O95062; Q15812; Q9HAK4; Q9NXE6; Q9NYG0; Q9NZM2; Q9ULG4; DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 20-APR-2010, sequence version 3. DT 27-MAR-2024, entry version 228. DE RecName: Full=Intersectin-2; DE AltName: Full=SH3 domain-containing protein 1B; DE AltName: Full=SH3P18; DE AltName: Full=SH3P18-like WASP-associated protein; GN Name=ITSN2; Synonyms=KIAA1256, SH3D1B, SWAP; 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] (ISOFORMS 1 AND 3). RC TISSUE=Fetal brain, and Fetal liver; RX PubMed=10922467; DOI=10.1016/s0014-5793(00)01793-2; RA Pucharcos C., Estivill X., de la Luna S.; RT "Intersectin 2, a new multimodular protein involved in clathrin-mediated RT endocytosis."; RL FEBS Lett. 478:43-51(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Seifert M., Engel M., Welter C.; RT "Intersectin 2 (SH3D1B), human homolog of mouse Ese2 protein."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 259-721 (ISOFORM 2), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 1262-1697, AND VARIANT ILE-291. RC TISSUE=Embryo; 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 822-1285 (ISOFORM 1). RA Wilson L.A., Fields D., Cruz L., Friesen J., Siminovitch K.A.; RT "SH3P18-like wasp associated protein (SWAP): a multiple SH3 domain RT containing protein that interacts with WASP."; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 945-1192 (ISOFORM 4). RC TISSUE=Bone marrow; RX PubMed=9630982; DOI=10.1038/nbt0696-741; RA Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.; RT "Cloning of ligand targets: systematic isolation of SH3 domain-containing RT proteins."; RL Nat. Biotechnol. 14:741-744(1996). RN [8] RP ALTERNATIVE SPLICING. RC TISSUE=Brain, and Fetal liver; RX PubMed=11690630; DOI=10.1016/s0167-4781(01)00276-7; RA Pucharcos C., Casas C., Nadal M., Estivill X., de la Luna S.; RT "The human intersectin genes and their spliced variants are differentially RT expressed."; RL Biochim. Biophys. Acta 1521:1-11(2001). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-968, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=15144186; DOI=10.1021/ac035352d; RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., RA Peters E.C.; RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from RT human T cells using immobilized metal affinity chromatography and tandem RT mass spectrometry."; RL Anal. Chem. 76:2763-2772(2004). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-968, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [11] RP INTERACTION WITH HUMAN HERPESVIRUS 8 PROTEIN K15 (MICROBIAL INFECTION). RX PubMed=17696407; DOI=10.1021/bi700357s; RA Lim C.S., Seet B.T., Ingham R.J., Gish G., Matskova L., Winberg G., RA Ernberg I., Pawson T.; RT "The K15 protein of Kaposi's sarcoma-associated herpesvirus recruits the RT endocytic regulator intersectin 2 through a selective SH3 domain RT interaction."; RL Biochemistry 46:9874-9885(2007). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-889, 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 [14] 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 [15] RP INTERACTION WITH ADAM15. RX PubMed=19718658; DOI=10.1002/jcb.22317; RA Kleino I., Ortiz R.M., Yritys M., Huovila A.P., Saksela K.; RT "Alternative splicing of ADAM15 regulates its interactions with cellular RT SH3 proteins."; RL J. Cell. Biochem. 108:877-885(2009). RN [16] RP FUNCTION. RX PubMed=19458185; DOI=10.1091/mbc.e09-03-0256; RA Mettlen M., Stoeber M., Loerke D., Antonescu C.N., Danuser G., Schmid S.L.; RT "Endocytic accessory proteins are functionally distinguished by their RT differential effects on the maturation of clathrin-coated pits."; RL Mol. Biol. Cell 20:3251-3260(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210; SER-889 AND TYR-968, AND RP IDENTIFICATION BY 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; THR-573; SER-889 AND RP TYR-968, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [19] RP INTERACTION WITH FCHO2. RX PubMed=20448150; DOI=10.1126/science.1188462; RA Henne W.M., Boucrot E., Meinecke M., Evergren E., Vallis Y., Mittal R., RA McMahon H.T.; RT "FCHo proteins are nucleators of clathrin-mediated endocytosis."; RL Science 328:1281-1284(2010). RN [20] 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 [21] RP FUNCTION. RX PubMed=22648170; DOI=10.1091/mbc.e11-12-1007; RA Teckchandani A., Mulkearns E.E., Randolph T.W., Toida N., Cooper J.A.; RT "The clathrin adaptor Dab2 recruits EH domain scaffold proteins to regulate RT integrin beta1 endocytosis."; RL Mol. Biol. Cell 23:2905-2916(2012). RN [22] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=23999003; DOI=10.1016/j.jdermsci.2013.07.010; RA Yoo J.C., Lim T.Y., Park J.S., Hah Y.S., Park N., Hong S.G., Park J.Y., RA Yoon T.J.; RT "SYT14L, especially its C2 domain, is involved in regulating melanocyte RT differentiation."; RL J. Dermatol. Sci. 72:246-251(2013). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-210; THR-573; RP SER-884 AND SER-889, 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 [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-889, 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 [25] 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). RN [26] RP STRUCTURE BY NMR OF 762-1187. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of SH3 domains of human intersectin 2 (KIAA1256)."; RL Submitted (AUG-2004) to the PDB data bank. CC -!- FUNCTION: Adapter protein that may provide indirect link between the CC endocytic membrane traffic and the actin assembly machinery. May CC regulate the formation of clathrin-coated vesicles (CCPs). Seems to be CC involved in CCPs maturation including invagination or budding. Involved CC in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor CC (TFR). Plays a role in dendrite formation by melanocytes CC (PubMed:23999003). {ECO:0000269|PubMed:19458185, CC ECO:0000269|PubMed:22648170, ECO:0000269|PubMed:23999003}. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00041}; CC -!- SUBUNIT: Belongs to a complex that may contain multimers of ITSN1, CC ITSN2 and EPS15, and different partners according to the step in the CC endocytic process. Interacts with ADAM15. Interacts with FASLG. CC Interacts with ANKRD54 (By similarity). Interacts with FCHO2. CC {ECO:0000250, ECO:0000269|PubMed:19718658, ECO:0000269|PubMed:19807924, CC ECO:0000269|PubMed:20448150}. CC -!- SUBUNIT: (Microbial infection) Interacts with herpes virus 8 protein CC K15. {ECO:0000269|PubMed:17696407}. CC -!- INTERACTION: CC Q9NZM3; P00533: EGFR; NbExp=3; IntAct=EBI-308689, EBI-297353; CC Q9NZM3; Q9WNA9: K15-M; Xeno; NbExp=2; IntAct=EBI-308689, EBI-7555439; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Additional isoforms seem to exist.; CC Name=1; Synonyms=ITSN2-L; CC IsoId=Q9NZM3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NZM3-2; Sequence=VSP_003892; CC Name=3; Synonyms=ITSN2-S1; CC IsoId=Q9NZM3-3; Sequence=VSP_003893, VSP_003894; CC Name=4; Synonyms=ITSN2-S2, SH3P18; CC IsoId=Q9NZM3-4; Sequence=VSP_003895; CC -!- TISSUE SPECIFICITY: Expressed in melanocytes (PubMed:23999003). CC Ubiquitous. Isoform 1 is primarily expressed in adult heart and liver. CC {ECO:0000269|PubMed:23999003}. CC -!- MISCELLANEOUS: Overexpression results in the inhibition of the CC transferrin uptake and the blockage of the clathrin-mediated CC endocytosis. CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator. CC {ECO:0000305}. CC -!- CAUTION: Studies in clathrin-mediated endocytosis of ITGB1 and TFR used CC a siRNA mixture of ISTN1 and ISTN2 suggesting a partially overlapping CC role of the EH domain-containing proteins. CC {ECO:0000305|PubMed:22648170}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF59903.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF59904.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF63600.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAA86570.1; Type=Erroneous initiation; Note=Extended N-terminus.; 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; AF182198; AAF59903.1; ALT_INIT; mRNA. DR EMBL; AF182199; AAF59904.1; ALT_INIT; mRNA. DR EMBL; AF248540; AAF63600.1; ALT_INIT; mRNA. DR EMBL; AB033082; BAA86570.1; ALT_INIT; mRNA. DR EMBL; AC008073; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC009228; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK021545; BAB13841.1; -; mRNA. DR EMBL; AK000302; BAA91068.1; -; mRNA. DR EMBL; AF001630; AAD00899.1; -; mRNA. DR EMBL; U61167; AAC50593.1; -; mRNA. DR CCDS; CCDS1710.2; -. [Q9NZM3-1] DR CCDS; CCDS1711.2; -. [Q9NZM3-2] DR CCDS; CCDS46230.1; -. [Q9NZM3-3] DR RefSeq; NP_006268.2; NM_006277.2. [Q9NZM3-1] DR RefSeq; NP_062541.3; NM_019595.3. [Q9NZM3-2] DR RefSeq; NP_671494.2; NM_147152.2. [Q9NZM3-3] DR PDB; 1J3T; NMR; -; A=898-958. DR PDB; 1UDL; NMR; -; A=1103-1187. DR PDB; 1UE9; NMR; -; A=1056-1122. DR PDB; 1UFF; NMR; -; A=762-842. DR PDB; 1UHF; NMR; -; A=983-1038. DR PDB; 3GF9; X-ray; 2.50 A; A=1130-1406. DR PDB; 3JZY; X-ray; 1.56 A; A=1201-1692. DR PDB; 4IIO; X-ray; 1.70 A; A/B=901-955. DR PDBsum; 1J3T; -. DR PDBsum; 1UDL; -. DR PDBsum; 1UE9; -. DR PDBsum; 1UFF; -. DR PDBsum; 1UHF; -. DR PDBsum; 3GF9; -. DR PDBsum; 3JZY; -. DR PDBsum; 4IIO; -. DR AlphaFoldDB; Q9NZM3; -. DR SMR; Q9NZM3; -. DR BioGRID; 119098; 146. DR IntAct; Q9NZM3; 54. DR MINT; Q9NZM3; -. DR STRING; 9606.ENSP00000347244; -. DR CarbonylDB; Q9NZM3; -. DR GlyCosmos; Q9NZM3; 13 sites, 2 glycans. DR GlyGen; Q9NZM3; 14 sites, 2 O-linked glycans (14 sites). DR iPTMnet; Q9NZM3; -. DR MetOSite; Q9NZM3; -. DR PhosphoSitePlus; Q9NZM3; -. DR BioMuta; ITSN2; -. DR DMDM; 294862505; -. DR EPD; Q9NZM3; -. DR jPOST; Q9NZM3; -. DR MassIVE; Q9NZM3; -. DR MaxQB; Q9NZM3; -. DR PaxDb; 9606-ENSP00000347244; -. DR PeptideAtlas; Q9NZM3; -. DR ProteomicsDB; 83445; -. [Q9NZM3-1] DR ProteomicsDB; 83446; -. [Q9NZM3-2] DR ProteomicsDB; 83447; -. [Q9NZM3-3] DR ProteomicsDB; 83448; -. [Q9NZM3-4] DR Pumba; Q9NZM3; -. DR ABCD; Q9NZM3; 9 sequenced antibodies. DR Antibodypedia; 27453; 106 antibodies from 18 providers. DR DNASU; 50618; -. DR Ensembl; ENST00000355123.9; ENSP00000347244.4; ENSG00000198399.16. [Q9NZM3-1] DR Ensembl; ENST00000361999.7; ENSP00000354561.2; ENSG00000198399.16. [Q9NZM3-2] DR Ensembl; ENST00000406921.7; ENSP00000384499.3; ENSG00000198399.16. [Q9NZM3-3] DR GeneID; 50618; -. DR KEGG; hsa:50618; -. DR MANE-Select; ENST00000355123.9; ENSP00000347244.4; NM_006277.3; NP_006268.2. DR UCSC; uc002rfe.3; human. [Q9NZM3-1] DR AGR; HGNC:6184; -. DR DisGeNET; 50618; -. DR GeneCards; ITSN2; -. DR HGNC; HGNC:6184; ITSN2. DR HPA; ENSG00000198399; Low tissue specificity. DR MIM; 604464; gene. DR neXtProt; NX_Q9NZM3; -. DR OpenTargets; ENSG00000198399; -. DR PharmGKB; PA29982; -. DR VEuPathDB; HostDB:ENSG00000198399; -. DR eggNOG; KOG1029; Eukaryota. DR eggNOG; KOG4305; Eukaryota. DR GeneTree; ENSGT00940000155936; -. DR HOGENOM; CLU_002819_2_0_1; -. DR InParanoid; Q9NZM3; -. DR OMA; WKANYER; -. DR OrthoDB; 2910300at2759; -. DR PhylomeDB; Q9NZM3; -. DR TreeFam; TF324293; -. DR PathwayCommons; Q9NZM3; -. DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis. DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis. DR Reactome; R-HSA-9013420; RHOU GTPase cycle. DR SignaLink; Q9NZM3; -. DR BioGRID-ORCS; 50618; 23 hits in 1154 CRISPR screens. DR ChiTaRS; ITSN2; human. DR EvolutionaryTrace; Q9NZM3; -. DR GeneWiki; ITSN2; -. DR GenomeRNAi; 50618; -. DR Pharos; Q9NZM3; Tbio. DR PRO; PR:Q9NZM3; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q9NZM3; Protein. DR Bgee; ENSG00000198399; Expressed in buccal mucosa cell and 207 other cell types or tissues. DR ExpressionAtlas; Q9NZM3; baseline and differential. DR GO; GO:0005813; C:centrosome; IDA:CACAO. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0097708; C:intracellular vesicle; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro. DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0150007; P:clathrin-dependent synaptic vesicle endocytosis; IBA:GO_Central. DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central. DR GO; GO:1903861; P:positive regulation of dendrite extension; IDA:UniProtKB. DR CDD; cd08375; C2_Intersectin; 1. DR CDD; cd00052; EH; 2. DR CDD; cd13264; PH_ITSN; 1. DR CDD; cd00160; RhoGEF; 1. DR CDD; cd11988; SH3_Intersectin2_1; 1. DR CDD; cd11990; SH3_Intersectin2_2; 1. DR CDD; cd11992; SH3_Intersectin2_3; 1. DR CDD; cd11994; SH3_Intersectin2_4; 1. DR CDD; cd11996; SH3_Intersectin2_5; 1. DR CDD; cd22265; UDM1_RNF168; 1. DR Gene3D; 2.60.40.150; C2 domain; 1. DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1. DR Gene3D; 1.10.238.10; EF-hand; 2. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR Gene3D; 2.30.30.40; SH3 Domains; 5. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR035899; DBL_dom_sf. DR InterPro; IPR000219; DH-domain. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR002048; EF_hand_dom. DR InterPro; IPR000261; EH_dom. DR InterPro; IPR035737; Intersectin-2_SH3_1. DR InterPro; IPR035738; Intersectin-2_SH3_2. DR InterPro; IPR035739; Intersectin-2_SH3_3. DR InterPro; IPR035740; Intersectin-2_SH3_4. DR InterPro; IPR035741; Intersectin-2_SH3_5. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR46006:SF9; INTERSECTIN-2 ISOFORM X1; 1. DR PANTHER; PTHR46006; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR AT 64C, ISOFORM A; 1. DR Pfam; PF00168; C2; 1. DR Pfam; PF12763; EF-hand_4; 2. DR Pfam; PF16652; PH_13; 1. DR Pfam; PF00621; RhoGEF; 1. DR Pfam; PF00018; SH3_1; 2. DR Pfam; PF07653; SH3_2; 1. DR Pfam; PF14604; SH3_9; 2. DR PRINTS; PR00499; P67PHOX. DR PRINTS; PR00452; SH3DOMAIN. DR SMART; SM00239; C2; 1. DR SMART; SM00054; EFh; 2. DR SMART; SM00027; EH; 2. DR SMART; SM00233; PH; 1. DR SMART; SM00325; RhoGEF; 1. DR SMART; SM00326; SH3; 5. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1. DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1. DR SUPFAM; SSF47473; EF-hand; 2. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF50044; SH3-domain; 5. DR PROSITE; PS50004; C2; 1. DR PROSITE; PS50010; DH_2; 1. DR PROSITE; PS00018; EF_HAND_1; 1. DR PROSITE; PS50222; EF_HAND_2; 2. DR PROSITE; PS50031; EH; 2. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS50002; SH3; 5. DR Genevisible; Q9NZM3; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Coiled coil; Cytoplasm; KW Differentiation; Endocytosis; Host-virus interaction; Metal-binding; KW Phosphoprotein; Reference proteome; Repeat; SH3 domain. FT CHAIN 1..1697 FT /note="Intersectin-2" FT /id="PRO_0000080961" FT DOMAIN 22..110 FT /note="EH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077" FT DOMAIN 54..89 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 244..333 FT /note="EH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077" FT DOMAIN 277..312 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 757..818 FT /note="SH3 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 898..956 FT /note="SH3 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 981..1039 FT /note="SH3 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 1053..1117 FT /note="SH3 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 1127..1186 FT /note="SH3 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 1209..1395 FT /note="DH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062" FT DOMAIN 1434..1544 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 1552..1668 FT /note="C2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT REGION 219..241 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 350..378 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 691..752 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 361..756 FT /evidence="ECO:0000255" FT COMPBIAS 219..240 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 351..378 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 67 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 69 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 71 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 73 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 78 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 1640 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 1643 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT BINDING 1646 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT MOD_RES 110 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 210 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 230 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 553 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9Z0R6" FT MOD_RES 573 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 882 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9Z0R6" FT MOD_RES 884 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 889 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 968 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15144186, FT ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231" FT VAR_SEQ 622..648 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10574462, FT ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2" FT /id="VSP_003892" FT VAR_SEQ 1193..1697 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:9630982" FT /id="VSP_003895" FT VAR_SEQ 1235..1249 FT /note="FQKRMAESGFLTEGE -> RRLLLASSRGICCLS (in isoform 3)" FT /evidence="ECO:0000303|PubMed:10922467" FT /id="VSP_003893" FT VAR_SEQ 1250..1697 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:10922467" FT /id="VSP_003894" FT VARIANT 254 FT /note="T -> A (in dbSNP:rs6744320)" FT /id="VAR_024287" FT VARIANT 291 FT /note="V -> I (in dbSNP:rs7603997)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_024288" FT VARIANT 1287 FT /note="I -> T (in dbSNP:rs3731625)" FT /id="VAR_020193" FT VARIANT 1534 FT /note="A -> T (in dbSNP:rs2303291)" FT /id="VAR_021937" FT CONFLICT 679 FT /note="R -> G (in Ref. 5; BAB13841)" FT /evidence="ECO:0000305" FT CONFLICT 823..828 FT /note="KAVSPK -> FAAAST (in Ref. 6; AAD00899)" FT /evidence="ECO:0000305" FT CONFLICT 945..951 FT /note="WFPKSYV -> EFAAAST (in Ref. 7; AAC50593)" FT /evidence="ECO:0000305" FT CONFLICT 1279..1285 FT /note="GEKMPVQ -> VDAAANS (in Ref. 6; AAD00899)" FT /evidence="ECO:0000305" FT CONFLICT 1553 FT /note="K -> Q (in Ref. 2; AAF63600 and 3; BAA86570)" FT /evidence="ECO:0000305" FT STRAND 762..766 FT /evidence="ECO:0007829|PDB:1UFF" FT STRAND 772..774 FT /evidence="ECO:0007829|PDB:1UFF" FT STRAND 783..786 FT /evidence="ECO:0007829|PDB:1UFF" FT STRAND 793..801 FT /evidence="ECO:0007829|PDB:1UFF" FT STRAND 804..809 FT /evidence="ECO:0007829|PDB:1UFF" FT STRAND 812..815 FT /evidence="ECO:0007829|PDB:1UFF" FT STRAND 818..821 FT /evidence="ECO:0007829|PDB:1UFF" FT STRAND 901..907 FT /evidence="ECO:0007829|PDB:4IIO" FT STRAND 924..931 FT /evidence="ECO:0007829|PDB:4IIO" FT STRAND 934..939 FT /evidence="ECO:0007829|PDB:4IIO" FT STRAND 942..947 FT /evidence="ECO:0007829|PDB:4IIO" FT HELIX 948..950 FT /evidence="ECO:0007829|PDB:4IIO" FT STRAND 951..954 FT /evidence="ECO:0007829|PDB:4IIO" FT STRAND 983..987 FT /evidence="ECO:0007829|PDB:1UHF" FT STRAND 995..999 FT /evidence="ECO:0007829|PDB:1UHF" FT STRAND 1007..1010 FT /evidence="ECO:0007829|PDB:1UHF" FT STRAND 1012..1014 FT /evidence="ECO:0007829|PDB:1UHF" FT STRAND 1017..1020 FT /evidence="ECO:0007829|PDB:1UHF" FT STRAND 1027..1029 FT /evidence="ECO:0007829|PDB:1UHF" FT HELIX 1031..1033 FT /evidence="ECO:0007829|PDB:1UHF" FT STRAND 1056..1060 FT /evidence="ECO:0007829|PDB:1UE9" FT STRAND 1079..1085 FT /evidence="ECO:0007829|PDB:1UE9" FT STRAND 1087..1095 FT /evidence="ECO:0007829|PDB:1UE9" FT STRAND 1104..1108 FT /evidence="ECO:0007829|PDB:1UE9" FT STRAND 1111..1114 FT /evidence="ECO:0007829|PDB:1UE9" FT STRAND 1129..1136 FT /evidence="ECO:0007829|PDB:1UDL" FT STRAND 1153..1156 FT /evidence="ECO:0007829|PDB:1UDL" FT STRAND 1161..1166 FT /evidence="ECO:0007829|PDB:1UDL" FT STRAND 1168..1171 FT /evidence="ECO:0007829|PDB:1UDL" FT STRAND 1180..1183 FT /evidence="ECO:0007829|PDB:1UDL" FT HELIX 1207..1234 FT /evidence="ECO:0007829|PDB:3GF9" FT HELIX 1236..1242 FT /evidence="ECO:0007829|PDB:3GF9" FT STRAND 1243..1245 FT /evidence="ECO:0007829|PDB:3GF9" FT HELIX 1247..1254 FT /evidence="ECO:0007829|PDB:3GF9" FT HELIX 1257..1272 FT /evidence="ECO:0007829|PDB:3GF9" FT HELIX 1288..1294 FT /evidence="ECO:0007829|PDB:3GF9" FT HELIX 1299..1321 FT /evidence="ECO:0007829|PDB:3GF9" FT HELIX 1323..1333 FT /evidence="ECO:0007829|PDB:3GF9" FT TURN 1336..1340 FT /evidence="ECO:0007829|PDB:3GF9" FT HELIX 1343..1346 FT /evidence="ECO:0007829|PDB:3GF9" FT HELIX 1349..1366 FT /evidence="ECO:0007829|PDB:3GF9" FT HELIX 1375..1393 FT /evidence="ECO:0007829|PDB:3GF9" FT STRAND 1569..1580 FT /evidence="ECO:0007829|PDB:3JZY" FT STRAND 1592..1598 FT /evidence="ECO:0007829|PDB:3JZY" FT STRAND 1601..1604 FT /evidence="ECO:0007829|PDB:3JZY" FT STRAND 1615..1625 FT /evidence="ECO:0007829|PDB:3JZY" FT TURN 1627..1629 FT /evidence="ECO:0007829|PDB:3JZY" FT STRAND 1631..1638 FT /evidence="ECO:0007829|PDB:3JZY" FT STRAND 1641..1644 FT /evidence="ECO:0007829|PDB:3JZY" FT STRAND 1647..1654 FT /evidence="ECO:0007829|PDB:3JZY" FT HELIX 1655..1665 FT /evidence="ECO:0007829|PDB:3JZY" FT STRAND 1670..1673 FT /evidence="ECO:0007829|PDB:3JZY" FT STRAND 1675..1679 FT /evidence="ECO:0007829|PDB:3JZY" FT STRAND 1681..1690 FT /evidence="ECO:0007829|PDB:3JZY" FT CONFLICT Q9NZM3-3:1235 FT /note="R -> W (in Ref. 1; AAF59904)" FT /evidence="ECO:0000305" SQ SEQUENCE 1697 AA; 193461 MW; 49C41AE1E32E1BD0 CRC64; MMAQFPTAMN GGPNMWAITS EERTKHDRQF DNLKPSGGYI TGDQARNFFL QSGLPAPVLA EIWALSDLNK DGKMDQQEFS IAMKLIKLKL QGQQLPVVLP PIMKQPPMFS PLISARFGMG SMPNLSIPQP LPPAAPITSL SSATSGTNLP PLMMPTPLVP SVSTSSLPNG TASLIQPLPI PYSSSTLPHG SSYSLMMGGF GGASIQKAQS LIDLGSSSST SSTASLSGNS PKTGTSEWAV PQPTRLKYRQ KFNTLDKSMS GYLSGFQARN ALLQSNLSQT QLATIWTLAD VDGDGQLKAE EFILAMHLTD MAKAGQPLPL TLPPELVPPS FRGGKQIDSI NGTLPSYQKM QEEEPQKKLP VTFEDKRKAN YERGNMELEK RRQALMEQQQ REAERKAQKE KEEWERKQRE LQEQEWKKQL ELEKRLEKQR ELERQREEER RKDIERREAA KQELERQRRL EWERIRRQEL LNQKNREQEE IVRLNSKKKN LHLELEALNG KHQQISGRLQ DVRLKKQTQK TELEVLDKQC DLEIMEIKQL QQELQEYQNK LIYLVPEKQL LNERIKNMQF SNTPDSGVSL LHKKSLEKEE LCQRLKEQLD ALEKETASKL SEMDSFNNQL KCGNMDDSVL QCLLSLLSCL NNLFLLLKEL RETYNTQQLA LEQLYKIKRD KLKEIERKRL ELMQKKKLED EAARKAKQGK ENLWKENLRK EEEEKQKRLQ EEKTQEKIQE EERKAEEKQR KDKDTLKAEE KKRETASVLV NYRALYPFEA RNHDEMSFNS GDIIQVDEKT VGEPGWLYGS FQGNFGWFPC NYVEKMPSSE NEKAVSPKKA LLPPTVSLSA TSTSSEPLSS NQPASVTDYQ NVSFSNLTVN TSWQKKSAFT RTVSPGSVSP IHGQGQVVEN LKAQALCSWT AKKDNHLNFS KHDIITVLEQ QENWWFGEVH GGRGWFPKSY VKIIPGSEVK REEPEALYAA VNKKPTSAAY SVGEEYIALY PYSSVEPGDL TFTEGEEILV TQKDGEWWTG SIGDRSGIFP SNYVKPKDQE SFGSASKSGA SNKKPEIAQV TSAYVASGSE QLSLAPGQLI LILKKNTSGW WQGELQARGK KRQKGWFPAS HVKLLGPSSE RATPAFHPVC QVIAMYDYAA NNEDELSFSK GQLINVMNKD DPDWWQGEIN GVTGLFPSNY VKMTTDSDPS QQWCADLQTL DTMQPIERKR QGYIHELIQT EERYMADLQL VVEVFQKRMA ESGFLTEGEM ALIFVNWKEL IMSNTKLLKA LRVRKKTGGE KMPVQMIGDI LAAELSHMQA YIRFCSCQLN GAALLQQKTD EDTDFKEFLK KLASDPRCKG MPLSSFLLKP MQRITRYPLL IRSILENTPE SHADHSSLKL ALERAEELCS QVNEGVREKE NSDRLEWIQA HVQCEGLAEQ LIFNSLTNCL GPRKLLHSGK LYKTKSNKEL HGFLFNDFLL LTYMVKQFAV SSGSEKLFSS KSNAQFKMYK TPIFLNEVLV KLPTDPSSDE PVFHISHIDR VYTLRTDNIN ERTAWVQKIK AASEQYIDTE KKKREKAYQA RSQKTSGIGR LMVHVIEATE LKACKPNGKS NPYCEISMGS QSYTTRTIQD TLNPKWNFNC QFFIKDLYQD VLCLTLFDRD QFSPDDFLGR TEIPVAKIRT EQESKGPMTR RLLLHEVPTG EVWVRFDLQL FEQKTLL //