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   27-MAR-2024, entry version 196.
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; 154.
DR   IntAct; Q9NRL3; 94.
DR   MINT; Q9NRL3; -.
DR   STRING; 9606.ENSP00000375777; -.
DR   GlyGen; Q9NRL3; 2 sites, 1 O-linked glycan (2 sites).
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; 9606-ENSP00000375777; -.
DR   PeptideAtlas; Q9NRL3; -.
DR   ProteomicsDB; 29195; -.
DR   ProteomicsDB; 4874; -.
DR   ProteomicsDB; 82385; -. [Q9NRL3-1]
DR   Pumba; Q9NRL3; -.
DR   ABCD; Q9NRL3; 1 sequenced antibody.
DR   Antibodypedia; 49367; 203 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   AGR; HGNC:15721; -.
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; GKAVHSM; -.
DR   OrthoDB; 5481146at2759; -.
DR   PhylomeDB; Q9NRL3; -.
DR   TreeFam; TF313387; -.
DR   PathwayCommons; Q9NRL3; -.
DR   SignaLink; Q9NRL3; -.
DR   SIGNOR; Q9NRL3; -.
DR   BioGRID-ORCS; 29888; 26 hits in 1157 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 160 other cell types or tissues.
DR   ExpressionAtlas; Q9NRL3; baseline and differential.
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   CDD; cd00200; WD40; 1.
DR   Gene3D; 1.20.5.300; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR15653; STRIATIN; 1.
DR   PANTHER; PTHR15653:SF1; STRIATIN-4; 1.
DR   Pfam; PF08232; Striatin; 1.
DR   Pfam; PF00400; WD40; 5.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR   Genevisible; Q9NRL3; HS.
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
//