ITSN2_HUMAN
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 03-AUG-2022, entry version 219.
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;
CC Evidence={ECO:0000255|PROSITE-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; 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};
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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; 135.
DR IntAct; Q9NZM3; 48.
DR MINT; Q9NZM3; -.
DR STRING; 9606.ENSP00000347244; -.
DR CarbonylDB; Q9NZM3; -.
DR GlyGen; Q9NZM3; 13 sites, 2 O-linked glycans (13 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; Q9NZM3; -.
DR PeptideAtlas; Q9NZM3; -.
DR PRIDE; Q9NZM3; -.
DR ProteomicsDB; 83445; -. [Q9NZM3-1]
DR ProteomicsDB; 83446; -. [Q9NZM3-2]
DR ProteomicsDB; 83447; -. [Q9NZM3-3]
DR ProteomicsDB; 83448; -. [Q9NZM3-4]
DR ABCD; Q9NZM3; 9 sequenced antibodies.
DR Antibodypedia; 27453; 86 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 CTD; 50618; -.
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; RDNNDYG; -.
DR OrthoDB; 807060at2759; -.
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 1077 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 205 other tissues.
DR ExpressionAtlas; Q9NZM3; baseline and differential.
DR Genevisible; Q9NZM3; HS.
DR GO; GO:0005813; C:centrosome; IDA:CACAO.
DR GO; GO:0005905; C:clathrin-coated pit; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
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:0006897; P: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; cd00052; EH; 2.
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 Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
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; IPR027029; Intersectin-2.
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; PTHR11216:SF29; PTHR11216:SF29; 3.
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; 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; SSF47473; SSF47473; 2.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF50044; SSF50044; 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.
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
