JIP4_HUMAN
ID JIP4_HUMAN Reviewed; 1321 AA.
AC O60271; A6H8U5; A8MSX0; B4DHH2; O60905; Q3KQU8; Q3MKM7; Q86WC7; Q86WC8;
AC Q8IZX7; Q96II0; Q9H811;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 4.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=C-Jun-amino-terminal kinase-interacting protein 4;
DE Short=JIP-4;
DE Short=JNK-interacting protein 4;
DE AltName: Full=Cancer/testis antigen 89;
DE Short=CT89;
DE AltName: Full=Human lung cancer oncogene 6 protein;
DE Short=HLC-6;
DE AltName: Full=JNK-associated leucine-zipper protein;
DE Short=JLP;
DE AltName: Full=Mitogen-activated protein kinase 8-interacting protein 4;
DE AltName: Full=Proliferation-inducing protein 6;
DE AltName: Full=Protein highly expressed in testis;
DE Short=PHET;
DE AltName: Full=Sperm surface protein;
DE AltName: Full=Sperm-associated antigen 9;
DE AltName: Full=Sperm-specific protein;
DE AltName: Full=Sunday driver 1;
GN Name=SPAG9 {ECO:0000312|HGNC:HGNC:14524};
GN Synonyms=HSS, KIAA0516, MAPK8IP4, SYD1; ORFNames=HLC6;
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=Liver;
RX PubMed=12391307; DOI=10.1073/pnas.232310199;
RA Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.;
RT "JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules and
RT transcription factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND TISSUE SPECIFICITY.
RX PubMed=16112646; DOI=10.1016/j.bbrc.2005.08.024;
RA Guinn B.-A., Bland E.A., Lodi U., Liggins A.P., Tobal K., Petters S.,
RA Wells J.W., Banham A.H., Mufti G.J.;
RT "Humoral detection of leukaemia-associated antigens in presentation acute
RT myeloid leukaemia.";
RL Biochem. Biophys. Res. Commun. 335:1293-1304(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6).
RC TISSUE=Brain, 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-478 (ISOFORMS 2/4/5).
RC TISSUE=Eye, and 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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 130-1321 (ISOFORM 5), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=9480848; DOI=10.1006/bbrc.1997.7943;
RA Shankar S., Mohapatra B., Suri A.;
RT "Cloning of a novel human testis mRNA specifically expressed in testicular
RT haploid germ cells, having unique palindromic sequences and encoding a
RT leucine zipper dimerization motif.";
RL Biochem. Biophys. Res. Commun. 243:561-565(1998).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 162-1321 (ISOFORM 3), TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC TISSUE=Testis;
RX PubMed=14662895; DOI=10.4049/jimmunol.171.12.6883;
RA Yasuoka H., Ihn H., Medsger T.A. Jr., Hirakata M., Kawakami Y., Ikeda Y.,
RA Kuwana M.;
RT "A novel protein highly expressed in testis is overexpressed in systemic
RT sclerosis fibroblasts and targeted by autoantibodies.";
RL J. Immunol. 171:6883-6890(2003).
RN [10]
RP IDENTIFICATION BY 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 [11]
RP FUNCTION, AND INTERACTION WITH NFKB1.
RX PubMed=14743216; DOI=10.1038/ncb1086;
RA Bouwmeester T., Bauch A., Ruffner H., Angrand P.-O., Bergamini G.,
RA Croughton K., Cruciat C., Eberhard D., Gagneur J., Ghidelli S., Hopf C.,
RA Huhse B., Mangano R., Michon A.-M., Schirle M., Schlegl J., Schwab M.,
RA Stein M.A., Bauer A., Casari G., Drewes G., Gavin A.-C., Jackson D.B.,
RA Joberty G., Neubauer G., Rick J., Kuster B., Superti-Furga G.;
RT "A physical and functional map of the human TNF-alpha/NF-kappa B signal
RT transduction pathway.";
RL Nat. Cell Biol. 6:97-105(2004).
RN [12]
RP FUNCTION (ISOFORM 5), INTERACTION WITH MAPK9; MAPK10 AND MAPK8 (ISOFORM 5),
RP SUBCELLULAR LOCATION (ISOFORM 5), AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15693750; DOI=10.1042/bj20041577;
RA Jagadish N., Rana R., Selvi R., Mishra D., Garg M., Yadav S., Herr J.C.,
RA Okumura K., Hasegawa A., Koyama K., Suri A.;
RT "Characterization of a novel human sperm-associated antigen 9 (SPAG9)
RT having structural homology with c-Jun N-terminal kinase-interacting
RT protein.";
RL Biochem. J. 389:73-82(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND THR-217, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-265; SER-272 AND
RP THR-418, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-185; THR-217;
RP SER-311; SER-329; SER-332; THR-418; THR-586 AND SER-733, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; THR-217 AND SER-733, 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-194; SER-203;
RP THR-217; SER-251; SER-265; SER-268; SER-272; SER-329; SER-332; SER-347;
RP THR-348; THR-418; SER-730 AND SER-733, AND IDENTIFICATION BY MASS
RP 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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-185; SER-329 AND
RP SER-332, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-183; SER-185;
RP SER-203; THR-217; SER-238; SER-265; SER-311; THR-586; SER-588; THR-595;
RP SER-705; SER-728; SER-730; SER-733; SER-1188 AND THR-1264, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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-185; SER-203; THR-217;
RP SER-251; SER-588; SER-732 AND SER-733, AND IDENTIFICATION BY MASS
RP 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 FUNCTION, INTERACTION WITH PIP4P1, AND SUBCELLULAR LOCATION.
RX PubMed=29146937; DOI=10.1038/s41467-017-01871-z;
RA Willett R., Martina J.A., Zewe J.P., Wills R., Hammond G.R.V.,
RA Puertollano R.;
RT "TFEB regulates lysosomal positioning by modulating TMEM55B expression and
RT JIP4 recruitment to lysosomes.";
RL Nat. Commun. 8:1580-1580(2017).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 406-476 IN COMPLEX WITH ARF6,
RP COILED COIL, SUBUNIT, AND INTERACTION WITH ARF6.
RX PubMed=19644450; DOI=10.1038/emboj.2009.209;
RA Isabet T., Montagnac G., Regazzoni K., Raynal B., El Khadali F.,
RA England P., Franco M., Chavrier P., Houdusse A., Menetrey J.;
RT "The structural basis of Arf effector specificity: the crystal structure of
RT ARF6 in a complex with JIP4.";
RL EMBO J. 28:2835-2845(2009).
CC -!- FUNCTION: The JNK-interacting protein (JIP) group of scaffold proteins
CC selectively mediates JNK signaling by aggregating specific components
CC of the MAPK cascade to form a functional JNK signaling module
CC (PubMed:14743216). Regulates lysosomal positioning by acting as an
CC adapter protein which links PIP4P1-positive lysosomes to the dynein-
CC dynactin complex (PubMed:29146937). Assists PIKFYVE selective
CC functionality in microtubule-based endosome-to-TGN trafficking (By
CC similarity). {ECO:0000250|UniProtKB:Q58A65,
CC ECO:0000269|PubMed:14743216, ECO:0000269|PubMed:29146937}.
CC -!- ACTIVITY REGULATION: [Isoform 5]: May play a role in spermatozoa-egg-
CC interaction. {ECO:0000269|PubMed:15693750}.
CC -!- SUBUNIT: Homodimer (PubMed:19644450). The homodimer interacts with
CC ARF6, forming a heterotetramer (PubMed:19644450). Homooligomer
CC (PubMed:19644450). Interacts with MAX, MAPK14, MAP3K3, MYC, KNS2 and
CC MAP2K4 (By similarity). Interaction with KNS2 is important in the
CC formation of ternary complex with MAPK8 (By similarity). Interacts with
CC NFKB1 (PubMed:14743216). Interacts with PIP4P1 (PubMed:29146937).
CC Interacts with PIKFYVE (By similarity). {ECO:0000250|UniProtKB:Q58A65,
CC ECO:0000269|PubMed:14743216, ECO:0000269|PubMed:15693750,
CC ECO:0000269|PubMed:19644450, ECO:0000269|PubMed:29146937}.
CC -!- SUBUNIT: [Isoform 5]: Interacts with MAPK8, MAPK9, MAPK10.
CC {ECO:0000269|PubMed:15693750}.
CC -!- INTERACTION:
CC O60271; P84077: ARF1; NbExp=3; IntAct=EBI-1023301, EBI-447171;
CC O60271; P62330: ARF6; NbExp=8; IntAct=EBI-1023301, EBI-638181;
CC O60271; Q96A65: EXOC4; NbExp=3; IntAct=EBI-1023301, EBI-355383;
CC O60271; P61006: RAB8A; NbExp=3; IntAct=EBI-1023301, EBI-722293;
CC O60271; P62331: Arf6; Xeno; NbExp=2; IntAct=EBI-1023301, EBI-988682;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q58A65}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q58A65}. Lysosome
CC membrane {ECO:0000269|PubMed:29146937}. Note=Perinuclear distribution
CC in response to stress signals such as UV radiation.
CC {ECO:0000250|UniProtKB:Q58A65}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasmic vesicle, secretory
CC vesicle, acrosome {ECO:0000269|PubMed:15693750}. Note=Associated with
CC the plasma membrane of the acrosomal compartment and also localizes in
CC the acrosome matrix. {ECO:0000269|PubMed:15693750}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=JLP(L) {ECO:0000250|UniProtKB:Q58A65};
CC IsoId=O60271-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60271-2; Sequence=VSP_018214, VSP_018220;
CC Name=3;
CC IsoId=O60271-3; Sequence=VSP_018221, VSP_018222;
CC Name=4;
CC IsoId=O60271-4; Sequence=VSP_018214;
CC Name=5;
CC IsoId=O60271-5; Sequence=VSP_018214, VSP_018221, VSP_018222;
CC Name=6;
CC IsoId=O60271-9; Sequence=VSP_042253, VSP_018214, VSP_042254;
CC -!- TISSUE SPECIFICITY: Expressed only in testis on the round spermatids of
CC stage I, II and II. Absent in spermatogonia and spermatocyte.
CC {ECO:0000269|PubMed:9480848}.
CC -!- TISSUE SPECIFICITY: [Isoform 4]: Expressed in testis and in acute
CC myeloid leukemia (AML) patients. {ECO:0000269|PubMed:16112646}.
CC -!- TISSUE SPECIFICITY: [Isoform 3]: Expressed in testis.
CC {ECO:0000269|PubMed:14662895}.
CC -!- INDUCTION: [Isoform 3]: Increased in systemic sclerosis fibroblasts.
CC {ECO:0000269|PubMed:14662895}.
CC -!- PTM: Phosphorylated by MAPK8 and MAPK14. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 3]: Due to intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the JIP scaffold family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07524.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAH59946.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAI06049.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
CC Sequence=AAO66462.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA25442.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14812.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=CAA62987.1; Type=Erroneous initiation; Note=Truncated 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; AF327452; AAN61565.1; -; mRNA.
DR EMBL; AY850123; AAX47276.1; -; mRNA.
DR EMBL; AB011088; BAA25442.3; ALT_INIT; mRNA.
DR EMBL; AK024068; BAB14812.1; ALT_SEQ; mRNA.
DR EMBL; AK295098; BAG58134.1; -; mRNA.
DR EMBL; AK302789; BAG63993.1; -; mRNA.
DR EMBL; AC005920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007524; AAH07524.1; ALT_SEQ; mRNA.
DR EMBL; BC059946; AAH59946.1; ALT_SEQ; mRNA.
DR EMBL; BC106048; AAI06049.1; ALT_SEQ; mRNA.
DR EMBL; BC146755; AAI46756.1; -; mRNA.
DR EMBL; BC153878; AAI53879.1; -; mRNA.
DR EMBL; X91879; CAA62987.1; ALT_INIT; mRNA.
DR EMBL; AY219897; AAO66462.1; ALT_INIT; mRNA.
DR EMBL; AY219898; AAO66463.1; -; mRNA.
DR CCDS; CCDS11577.1; -. [O60271-4]
DR CCDS; CCDS45740.1; -. [O60271-1]
DR CCDS; CCDS58577.1; -. [O60271-9]
DR CCDS; CCDS58578.1; -. [O60271-2]
DR PIR; JC5958; JC5958.
DR RefSeq; NP_001123999.1; NM_001130527.2. [O60271-2]
DR RefSeq; NP_001124000.1; NM_001130528.2. [O60271-1]
DR RefSeq; NP_001238900.1; NM_001251971.1. [O60271-9]
DR RefSeq; NP_003962.3; NM_003971.5. [O60271-4]
DR PDB; 2W83; X-ray; 1.93 A; C/D=406-476.
DR PDBsum; 2W83; -.
DR AlphaFoldDB; O60271; -.
DR SMR; O60271; -.
DR BioGRID; 114505; 188.
DR CORUM; O60271; -.
DR IntAct; O60271; 60.
DR MINT; O60271; -.
DR STRING; 9606.ENSP00000262013; -.
DR GlyGen; O60271; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60271; -.
DR MetOSite; O60271; -.
DR PhosphoSitePlus; O60271; -.
DR BioMuta; SPAG9; -.
DR EPD; O60271; -.
DR jPOST; O60271; -.
DR MassIVE; O60271; -.
DR MaxQB; O60271; -.
DR PaxDb; O60271; -.
DR PeptideAtlas; O60271; -.
DR PRIDE; O60271; -.
DR ProteomicsDB; 49302; -. [O60271-1]
DR ProteomicsDB; 49303; -. [O60271-2]
DR ProteomicsDB; 49304; -. [O60271-3]
DR ProteomicsDB; 49305; -. [O60271-4]
DR ProteomicsDB; 49306; -. [O60271-5]
DR ProteomicsDB; 49307; -. [O60271-9]
DR Antibodypedia; 30731; 223 antibodies from 36 providers.
DR DNASU; 9043; -.
DR Ensembl; ENST00000262013.12; ENSP00000262013.7; ENSG00000008294.22. [O60271-1]
DR Ensembl; ENST00000357122.8; ENSP00000349636.4; ENSG00000008294.22. [O60271-4]
DR Ensembl; ENST00000505279.5; ENSP00000426900.1; ENSG00000008294.22. [O60271-2]
DR Ensembl; ENST00000510283.5; ENSP00000423165.1; ENSG00000008294.22. [O60271-9]
DR GeneID; 9043; -.
DR KEGG; hsa:9043; -.
DR MANE-Select; ENST00000262013.12; ENSP00000262013.7; NM_001130528.3; NP_001124000.1.
DR UCSC; uc002ita.4; human. [O60271-1]
DR CTD; 9043; -.
DR DisGeNET; 9043; -.
DR GeneCards; SPAG9; -.
DR HGNC; HGNC:14524; SPAG9.
DR HPA; ENSG00000008294; Low tissue specificity.
DR MIM; 605430; gene.
DR neXtProt; NX_O60271; -.
DR OpenTargets; ENSG00000008294; -.
DR PharmGKB; PA37890; -.
DR VEuPathDB; HostDB:ENSG00000008294; -.
DR eggNOG; KOG2077; Eukaryota.
DR GeneTree; ENSGT00940000153496; -.
DR HOGENOM; CLU_003841_0_0_1; -.
DR InParanoid; O60271; -.
DR OMA; KWTEMIR; -.
DR OrthoDB; 324912at2759; -.
DR PhylomeDB; O60271; -.
DR TreeFam; TF313096; -.
DR PathwayCommons; O60271; -.
DR Reactome; R-HSA-525793; Myogenesis.
DR SignaLink; O60271; -.
DR SIGNOR; O60271; -.
DR BioGRID-ORCS; 9043; 26 hits in 1079 CRISPR screens.
DR ChiTaRS; SPAG9; human.
DR EvolutionaryTrace; O60271; -.
DR GeneWiki; SPAG9; -.
DR GenomeRNAi; 9043; -.
DR Pharos; O60271; Tbio.
DR PRO; PR:O60271; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O60271; protein.
DR Bgee; ENSG00000008294; Expressed in calcaneal tendon and 202 other tissues.
DR ExpressionAtlas; O60271; baseline and differential.
DR Genevisible; O60271; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
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:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008432; F:JUN kinase binding; IBA:GO_Central.
DR GO; GO:0019894; F:kinesin binding; IBA:GO_Central.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; IBA:GO_Central.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central.
DR GO; GO:0032418; P:lysosome localization; IMP:UniProtKB.
DR GO; GO:1903860; P:negative regulation of dendrite extension; IEA:Ensembl.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:MGI.
DR GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR039911; JIP3/JIP4.
DR InterPro; IPR032486; JIP_LZII.
DR InterPro; IPR019143; JNK/Rab-associated_protein-1_N.
DR InterPro; IPR034743; RH1.
DR InterPro; IPR034744; RH2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13886; PTHR13886; 1.
DR Pfam; PF16471; JIP_LZII; 1.
DR Pfam; PF09744; Jnk-SapK_ap_N; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS51776; RH1; 1.
DR PROSITE; PS51777; RH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Lysosome; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1321
FT /note="C-Jun-amino-terminal kinase-interacting protein 4"
FT /id="PRO_0000234076"
FT DOMAIN 7..95
FT /note="RH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01112"
FT DOMAIN 500..571
FT /note="RH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01113"
FT REGION 203..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 66..166
FT /evidence="ECO:0000255"
FT COILED 408..534
FT /evidence="ECO:0000269|PubMed:19644450"
FT COILED 724..758
FT /evidence="ECO:0000255"
FT COMPBIAS 231..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 217
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 292
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q58A65"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 348
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 365
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q58A65"
FT MOD_RES 418
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
FT MOD_RES 586
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 595
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 705
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 732
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 733
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 1188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1264
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..196
FT /note="MELEDGVVYQEEPGGSGAVMSERVSGLAGSIYREFERLIGRYDEEVVKELMP
FT LVVAVLENLDSVFAQDQEHQVELELLRDDNEQLITQYEREKALRKHAEEKFIEFEDSQE
FT QEKKDLQTRVESLESQTRQLELKAKNYADQISRLEEREAELKKEYNALHQRHTEMIHNY
FT MEHLERTKLHQLSGSDQLESTAHSRI -> MSPGCMLLFVFGFVGGAVVINSAILVSLS
FT VLLLVHFSISTGVPALTQNLPRIL (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_042253"
FT VAR_SEQ 248..261
FT /note="Missing (in isoform 2, isoform 4, isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:12391307,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16112646, ECO:0000303|PubMed:9480848"
FT /id="VSP_018214"
FT VAR_SEQ 555
FT /note="F -> FVPTR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12391307"
FT /id="VSP_018220"
FT VAR_SEQ 938..945
FT /note="SNDSDAYK -> RYNNGSST (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14662895,
FT ECO:0000303|PubMed:9480848"
FT /id="VSP_018221"
FT VAR_SEQ 946..1321
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14662895,
FT ECO:0000303|PubMed:9480848"
FT /id="VSP_018222"
FT VAR_SEQ 1175
FT /note="T -> TVILHQGRLLGLRA (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_042254"
FT VARIANT 1320
FT /note="N -> S (in dbSNP:rs9896965)"
FT /id="VAR_059364"
FT CONFLICT 451
FT /note="E -> G (in Ref. 9; AAO66462)"
FT /evidence="ECO:0000305"
FT CONFLICT 680
FT /note="E -> K (in Ref. 8; CAA62987 and 9; AAO66462)"
FT /evidence="ECO:0000305"
FT HELIX 406..465
FT /evidence="ECO:0007829|PDB:2W83"
FT CONFLICT O60271-9:9
FT /note="F -> S (in Ref. 5; BAG58134)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1321 AA; 146205 MW; 5CAE349FBDF91B40 CRC64;
MELEDGVVYQ EEPGGSGAVM SERVSGLAGS IYREFERLIG RYDEEVVKEL MPLVVAVLEN
LDSVFAQDQE HQVELELLRD DNEQLITQYE REKALRKHAE EKFIEFEDSQ EQEKKDLQTR
VESLESQTRQ LELKAKNYAD QISRLEEREA ELKKEYNALH QRHTEMIHNY MEHLERTKLH
QLSGSDQLES TAHSRIRKER PISLGIFPLP AGDGLLTPDA QKGGETPGSE QWKFQELSQP
RSHTSLKVSN SPEPQKAVEQ EDELSDVSQG GSKATTPAST ANSDVATIPT DTPLKEENEG
FVKVTDAPNK SEISKHIEVQ VAQETRNVST GSAENEEKSE VQAIIESTPE LDMDKDLSGY
KGSSTPTKGI ENKAFDRNTE SLFEELSSAG SGLIGDVDEG ADLLGMGREV ENLILENTQL
LETKNALNIV KNDLIAKVDE LTCEKDVLQG ELEAVKQAKL KLEEKNRELE EELRKARAEA
EDARQKAKDD DDSDIPTAQR KRFTRVEMAR VLMERNQYKE RLMELQEAVR WTEMIRASRE
NPAMQEKKRS SIWQFFSRLF SSSSNTTKKP EPPVNLKYNA PTSHVTPSVK KRSSTLSQLP
GDKSKAFDFL SEETEASLAS RREQKREQYR QVKAHVQKED GRVQAFGWSL PQKYKQVTNG
QGENKMKNLP VPVYLRPLDE KDTSMKLWCA VGVNLSGGKT RDGGSVVGAS VFYKDVAGLD
TEGSKQRSAS QSSLDKLDQE LKEQQKELKN QEELSSLVWI CTSTHSATKV LIIDAVQPGN
ILDSFTVCNS HVLCIASVPG ARETDYPAGE DLSESGQVDK ASLCGSMTSN SSAETDSLLG
GITVVGCSAE GVTGAATSPS TNGASPVMDK PPEMEAENSE VDENVPTAEE ATEATEGNAG
SAEDTVDISQ TGVYTEHVFT DPLGVQIPED LSPVYQSSND SDAYKDQISV LPNEQDLVRE
EAQKMSSLLP TMWLGAQNGC LYVHSSVAQW RKCLHSIKLK DSILSIVHVK GIVLVALADG
TLAIFHRGVD GQWDLSNYHL LDLGRPHHSI RCMTVVHDKV WCGYRNKIYV VQPKAMKIEK
SFDAHPRKES QVRQLAWVGD GVWVSIRLDS TLRLYHAHTY QHLQDVDIEP YVSKMLGTGK
LGFSFVRITA LMVSCNRLWV GTGNGVIISI PLTETNKTSG VPGNRPGSVI RVYGDENSDK
VTPGTFIPYC SMAHAQLCFH GHRDAVKFFV AVPGQVISPQ SSSSGTDLTG DKAGPSAQEP
GSQTPLKSML VISGGEGYID FRMGDEGGES ELLGEDLPLE PSVTKAERSH LIVWQVMYGN
E
