STRN4_HUMAN
ID STRN4_HUMAN Reviewed; 753 AA.
AC Q9NRL3; A0A024R0V2; B4DQH7; F8VYA6; Q8NE53;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Striatin-4;
DE AltName: Full=Zinedin;
GN Name=STRN4; Synonyms=ZIN;
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 1).
RX PubMed=10748158; DOI=10.1074/jbc.m909782199;
RA Castets F., Rakitina T., Gaillard S., Moqrich A., Mattei M.-G.,
RA Monneron A.;
RT "Zinedin, SG2NA, and striatin are calmodulin-binding, WD repeat proteins
RT principally expressed in the brain.";
RL J. Biol. Chem. 275:19970-19977(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle, and Testis;
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, 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 [8]
RP IDENTIFICATION BY MASS 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 [9]
RP INTERACTION WITH CTTNBP2NL.
RX PubMed=18782753; DOI=10.1074/mcp.m800266-mcp200;
RA Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G.,
RA Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I.,
RA Aebersold R., Raught B., Gingras A.C.;
RT "A PP2A phosphatase high density interaction network identifies a novel
RT striatin-interacting phosphatase and kinase complex linked to the cerebral
RT cavernous malformation 3 (CCM3) protein.";
RL Mol. Cell. Proteomics 8:157-171(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53 AND SER-206, AND
RP 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, AND IDENTIFICATION BY
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Binds calmodulin in a calcium dependent manner. May function
CC as scaffolding or signaling protein.
CC -!- SUBUNIT: Interacts with CTTNBP2; this interaction may regulate
CC dendritic spine distribution of STRN4. Activation of glutamate
CC receptors weakens the interaction with CTTNBP2 (By similarity).
CC Interacts with CTTNBP2NL. {ECO:0000250, ECO:0000269|PubMed:18782753}.
CC -!- INTERACTION:
CC Q9NRL3; Q01658: DR1; NbExp=3; IntAct=EBI-717245, EBI-750300;
CC Q9NRL3; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-717245, EBI-1054873;
CC Q9NRL3; P05412: JUN; NbExp=3; IntAct=EBI-717245, EBI-852823;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cell projection, dendritic
CC spine {ECO:0000250}. Note=CTTNBP2-binding may regulate dendritic spine
CC distribution. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NRL3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NRL3-2; Sequence=VSP_056170, VSP_056171, VSP_056172;
CC Name=3;
CC IsoId=Q9NRL3-3; Sequence=VSP_056738;
CC -!- MISCELLANEOUS: The name 'Zinedin' probably originates from the name of
CC the famous soccer player from Marseille (Zinedine Zidane).
CC -!- SIMILARITY: Belongs to the WD repeat striatin family. {ECO:0000305}.
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DR EMBL; AF212940; AAF29527.1; -; mRNA.
DR EMBL; AK298804; BAG60939.1; -; mRNA.
DR EMBL; AC008622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471126; EAW57442.1; -; Genomic_DNA.
DR EMBL; CH471126; EAW57443.1; -; Genomic_DNA.
DR EMBL; BC004910; AAH04910.2; -; mRNA.
DR EMBL; BC034604; AAH34604.1; -; mRNA.
DR CCDS; CCDS12690.1; -. [Q9NRL3-1]
DR CCDS; CCDS42581.1; -. [Q9NRL3-3]
DR RefSeq; NP_001034966.1; NM_001039877.1. [Q9NRL3-3]
DR RefSeq; NP_037535.2; NM_013403.2. [Q9NRL3-1]
DR AlphaFoldDB; Q9NRL3; -.
DR SMR; Q9NRL3; -.
DR BioGRID; 118941; 136.
DR IntAct; Q9NRL3; 90.
DR MINT; Q9NRL3; -.
DR STRING; 9606.ENSP00000375777; -.
DR GlyGen; Q9NRL3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NRL3; -.
DR PhosphoSitePlus; Q9NRL3; -.
DR BioMuta; STRN4; -.
DR DMDM; 152031693; -.
DR EPD; Q9NRL3; -.
DR jPOST; Q9NRL3; -.
DR MassIVE; Q9NRL3; -.
DR MaxQB; Q9NRL3; -.
DR PaxDb; Q9NRL3; -.
DR PeptideAtlas; Q9NRL3; -.
DR PRIDE; Q9NRL3; -.
DR ProteomicsDB; 29195; -.
DR ProteomicsDB; 4874; -.
DR ProteomicsDB; 82385; -. [Q9NRL3-1]
DR ABCD; Q9NRL3; 1 sequenced antibody.
DR Antibodypedia; 49367; 179 antibodies from 25 providers.
DR DNASU; 29888; -.
DR Ensembl; ENST00000263280.11; ENSP00000263280.4; ENSG00000090372.15. [Q9NRL3-1]
DR Ensembl; ENST00000391910.7; ENSP00000375777.1; ENSG00000090372.15. [Q9NRL3-3]
DR Ensembl; ENST00000435164.6; ENSP00000473607.1; ENSG00000090372.15. [Q9NRL3-2]
DR GeneID; 29888; -.
DR KEGG; hsa:29888; -.
DR MANE-Select; ENST00000263280.11; ENSP00000263280.4; NM_013403.3; NP_037535.2.
DR UCSC; uc002pfl.4; human. [Q9NRL3-1]
DR CTD; 29888; -.
DR DisGeNET; 29888; -.
DR GeneCards; STRN4; -.
DR HGNC; HGNC:15721; STRN4.
DR HPA; ENSG00000090372; Low tissue specificity.
DR MalaCards; STRN4; -.
DR MIM; 614767; gene.
DR neXtProt; NX_Q9NRL3; -.
DR OpenTargets; ENSG00000090372; -.
DR PharmGKB; PA134863218; -.
DR VEuPathDB; HostDB:ENSG00000090372; -.
DR eggNOG; KOG0642; Eukaryota.
DR GeneTree; ENSGT00950000183095; -.
DR HOGENOM; CLU_009108_2_0_1; -.
DR InParanoid; Q9NRL3; -.
DR OMA; NRTIRFM; -.
DR OrthoDB; 334070at2759; -.
DR PhylomeDB; Q9NRL3; -.
DR TreeFam; TF313387; -.
DR PathwayCommons; Q9NRL3; -.
DR SignaLink; Q9NRL3; -.
DR SIGNOR; Q9NRL3; -.
DR BioGRID-ORCS; 29888; 22 hits in 1079 CRISPR screens.
DR ChiTaRS; STRN4; human.
DR GeneWiki; STRN4; -.
DR GenomeRNAi; 29888; -.
DR Pharos; Q9NRL3; Tbio.
DR PRO; PR:Q9NRL3; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NRL3; protein.
DR Bgee; ENSG00000090372; Expressed in left testis and 158 other tissues.
DR ExpressionAtlas; Q9NRL3; baseline and differential.
DR Genevisible; Q9NRL3; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0090443; C:FAR/SIN/STRIPAK complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070016; F:armadillo repeat domain binding; IPI:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR013258; Striatin_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF08232; Striatin; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Cell projection; Coiled coil;
KW Cytoplasm; Membrane; Phosphoprotein; Reference proteome; Repeat; Synapse;
KW WD repeat.
FT CHAIN 1..753
FT /note="Striatin-4"
FT /id="PRO_0000051239"
FT REPEAT 436..475
FT /note="WD 1"
FT REPEAT 489..528
FT /note="WD 2"
FT REPEAT 542..581
FT /note="WD 3"
FT REPEAT 587..628
FT /note="WD 4"
FT REPEAT 635..674
FT /note="WD 5"
FT REPEAT 677..716
FT /note="WD 6"
FT REPEAT 723..752
FT /note="WD 7"
FT REGION 10..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..79
FT /note="Caveolin-binding"
FT /evidence="ECO:0000255"
FT REGION 165..182
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT REGION 213..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 69..136
FT /evidence="ECO:0000255"
FT COMPBIAS 302..317
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..119
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056170"
FT VAR_SEQ 347..376
FT /note="ESRRVKLQGILADLRDVDGLPPKVTGPPPG -> GPELHSPTEWQGALSVGK
FT ASPMPDWVGTAG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056171"
FT VAR_SEQ 377..753
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056172"
FT VAR_SEQ 384
FT /note="E -> EGSFGFSS (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_056738"
FT VARIANT 568
FT /note="V -> I (in dbSNP:rs10409124)"
FT /id="VAR_053419"
FT CONFLICT 356
FT /note="I -> V (in Ref. 1; AAF29527)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 753 AA; 80596 MW; 339AC24E26A9CD54 CRC64;
MMEERAAAAV AAAASSCRPL GSGAGPGPTG AAPVSAPAPG PGPAGKGGGG GGSPGPTAGP
EPLSLPGILH FIQHEWARFE AEKARWEAER AELQAQVAFL QGERKGQENL KTDLVRRIKM
LEYALKQERA KYHKLKFGTD LNQGEKKADV SEQVSNGPVE SVTLENSPLV WKEGRQLLRQ
YLEEVGYTDT ILDMRSKRVR SLLGRSLELN GAVEPSEGAP RAPPGPAGLS GGESLLVKQI
EEQIKRNAAG KDGKERLGGS VLGQIPFLQN CEDEDSDEDD ELDSVQHKKQ RVKLPSKALV
PEMEDEDEED DSEDAINEFD FLGSGEDGEG APDPRRCTVD GSPHELESRR VKLQGILADL
RDVDGLPPKV TGPPPGTPQP RPHEDVFIMD TIGGGEVSLG DLADLTVTND NDLSCDLSDS
KDAFKKTWNP KFTLRSHYDG IRSLAFHHSQ SALLTASEDG TLKLWNLQKA VTAKKNAALD
VEPIHAFRAH RGPVLAVAMG SNSEYCYSGG ADACIHSWKI PDLSMDPYDG YDPSVLSHVL
EGHGDAVWGL AFSPTSQRLA SCSADGTVRI WDPSSSSPAC LCTFPTASEH GVPTSVAFTS
TEPAHIVASF RSGDTVLYDM EVGSALLTLE SRGSSGPTQI NQVVSHPNQP LTITAHDDRG
IRFLDNRTGK PVHSMVAHLD AVTCLAVDPN GAFLMSGSHD CSLRLWSLDN KTCVQEITAH
RKKHEEAIHA VACHPSKALI ASAGADALAK VFV
