ID   CUX1_MOUSE              Reviewed;        1515 AA.
AC   P53564; O08994; P70301; Q571L6; Q91ZD2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 3.
DT   24-JAN-2024, entry version 185.
DE   RecName: Full=Homeobox protein cut-like 1 {ECO:0000305};
DE   AltName: Full=CCAAT displacement protein;
DE            Short=CDP;
DE   AltName: Full=Homeobox protein cux-1;
DE   Contains:
DE     RecName: Full=CDP/Cux p110 {ECO:0000303|PubMed:15099520};
GN   Name=Cux1 {ECO:0000312|MGI:MGI:88568}; Synonyms=Cutl1, Cux, Kiaa4047;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC   STRAIN=A/J, and BALB/cJ; TISSUE=Brain;
RX   PubMed=7910552; DOI=10.1242/dev.119.3.881;
RA   Valarche I., Tissier-Seta J.-P., Hirsch M.R., Martinez S., Goridis C.,
RA   Brunet J.-F.;
RT   "The mouse homeodomain protein Phox2 regulates Ncam promoter activity in
RT   concert with Cux/CDP and is a putative determinant of neurotransmitter
RT   phenotype.";
RL   Development 119:881-896(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Testis;
RX   PubMed=8879483; DOI=10.1095/biolreprod55.4.731;
RA   Vanden Heuvel G.B., Quaggin S.E., Igarashi P.;
RT   "A unique variant of a homeobox gene related to Drosophila cut is expressed
RT   in mouse testis.";
RL   Biol. Reprod. 55:731-739(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND FUNCTION.
RX   PubMed=11544187; DOI=10.1101/gad.200101;
RA   Ellis T., Gambardella L., Horcher M., Tschanz S., Capol J., Bertram P.,
RA   Jochum W., Barrandon Y., Busslinger M.;
RT   "The transcriptional repressor CDP (Cutl1) is essential for epithelial cell
RT   differentiation of the lung and the hair follicle.";
RL   Genes Dev. 15:2307-2319(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Embryonic tail;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT   complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT   screening of terminal sequences of cDNA clones randomly sampled from size-
RT   fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 121-1515 (ISOFORM 2), AND FUNCTION.
RC   STRAIN=C57BL/6N;
RX   PubMed=9858552; DOI=10.1128/mcb.19.1.284;
RA   Wang Z., Goldstein A., Zong R.-T., Lin D., Neufeld E.J., Scheuermann R.H.,
RA   Tucker P.W.;
RT   "Cux/CDP homeoprotein is a component of NF-muNR and represses the
RT   immunoglobulin heavy chain intronic enhancer by antagonizing the bright
RT   transcription activator.";
RL   Mol. Cell. Biol. 19:284-295(1999).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 762-1515 (ISOFORMS 2/3/4/5).
RX   PubMed=8840273; DOI=10.1038/ki.1996.336;
RA   Vanden Heuvel G.B., Bodmer R., McConnell K.R., Nagami G.T., Igarashi P.;
RT   "Expression of a cut-related homeobox gene in developing and polycystic
RT   mouse kidney.";
RL   Kidney Int. 50:453-461(1996).
RN   [7]
RP   INTERACTION WITH SATB1.
RX   PubMed=10373541; DOI=10.1128/mcb.19.7.4918;
RA   Liu J., Barnett A., Neufeld E.J., Dudley J.P.;
RT   "Homeoproteins CDP and SATB1 interact: potential for tissue-specific
RT   regulation.";
RL   Mol. Cell. Biol. 19:4918-4926(1999).
RN   [8]
RP   FUNCTION, INTERACTION WITH BANP, AND SUBCELLULAR LOCATION.
RX   PubMed=15371550; DOI=10.1093/nar/gkh807;
RA   Kaul-Ghanekar R., Jalota-Badhwar A., Pavithra L., Tucker P.,
RA   Chattopadhyay S.;
RT   "SMAR1 and Cux/CDP modulate chromatin and act as negative regulators of the
RT   TCRbeta enhancer (Ebeta).";
RL   Nucleic Acids Res. 32:4862-4875(2004).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, AND DNA-BINDING.
RX   PubMed=15099520; DOI=10.1016/s1097-2765(04)00209-6;
RA   Goulet B., Baruch A., Moon N.S., Poirier M., Sansregret L.L., Erickson A.,
RA   Bogyo M., Nepveu A.;
RT   "A cathepsin L isoform that is devoid of a signal peptide localizes to the
RT   nucleus in S phase and processes the CDP/Cux transcription factor.";
RL   Mol. Cell 14:207-219(2004).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427; SER-1332 AND SER-1506,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [11]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20510857; DOI=10.1016/j.neuron.2010.04.038;
RA   Cubelos B., Sebastian-Serrano A., Beccari L., Calcagnotto M.E.,
RA   Cisneros E., Kim S., Dopazo A., Alvarez-Dolado M., Redondo J.M.,
RA   Bovolenta P., Walsh C.A., Nieto M.;
RT   "Cux1 and Cux2 regulate dendritic branching, spine morphology, and synapses
RT   of the upper layer neurons of the cortex.";
RL   Neuron 66:523-535(2010).
CC   -!- FUNCTION: Transcription factor involved in the control of neuronal
CC       differentiation in the brain. Regulates dendrite development and
CC       branching, and dendritic spine formation in cortical layers II-III
CC       (PubMed:20510857). Also involved in the control of synaptogenesis
CC       (Probable). In addition, it has probably a broad role in mammalian
CC       development as a repressor of developmentally regulated gene
CC       expression. May act by preventing binding of positively-activing CCAAT
CC       factors to promoters. Component of nf-munr repressor; binds to the
CC       matrix attachment regions (MARs) (5' and 3') of the immunoglobulin
CC       heavy chain enhancer. Represses T-cell receptor (TCR) beta enhancer
CC       function by binding to MARbeta, an ATC-rich DNA sequence located
CC       upstream of the TCR beta enhancer. Binds to the TH enhancer; may
CC       require the basic helix-loop-helix protein TCF4 as a coactivator.
CC       {ECO:0000269|PubMed:11544187, ECO:0000269|PubMed:15371550,
CC       ECO:0000269|PubMed:20510857, ECO:0000269|PubMed:9858552,
CC       ECO:0000305|PubMed:20510857}.
CC   -!- FUNCTION: [CDP/Cux p110]: Plays a role in cell cycle progression, in
CC       particular at the G1/S transition. As cells progress into S phase, a
CC       fraction of CUX1 molecules is proteolytically processed into N-
CC       terminally truncated proteins of 110 kDa. While CUX1 only transiently
CC       binds to DNA and carries the CCAAT-displacement activity, CDP/Cux p110
CC       makes a stable interaction with DNA and stimulates expression of genes
CC       such as POLA1. {ECO:0000269|PubMed:15099520}.
CC   -!- SUBUNIT: Interacts with BANP. Interacts with SATB1 (via DNA-binding
CC       domains); the interaction inhibits the attachment of both proteins to
CC       DNA. {ECO:0000269|PubMed:10373541, ECO:0000269|PubMed:15371550}.
CC   -!- INTERACTION:
CC       P53564; Q8VI24: Satb2; NbExp=3; IntAct=EBI-642309, EBI-5737999;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC       ECO:0000255|PROSITE-ProRule:PRU00374, ECO:0000269|PubMed:15371550}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=5;
CC         IsoId=P53564-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P53564-2; Sequence=VSP_002311;
CC       Name=3;
CC         IsoId=P53564-3; Sequence=VSP_015749, VSP_015750;
CC       Name=4;
CC         IsoId=P53564-4; Sequence=VSP_015748;
CC       Name=6;
CC         IsoId=P53564-5; Sequence=VSP_017360;
CC       Name=1; Synonyms=CASP;
CC         IsoId=P70403-1; Sequence=External;
CC   -!- TISSUE SPECIFICITY: [Isoform 6]: Testis-specific where it is expressed
CC       in germ cells. {ECO:0000269|PubMed:8879483}.
CC   -!- DEVELOPMENTAL STAGE: In postpubertal testis, isoform 6 is expressed
CC       from stages IV-V of spermatogenesis in the outer layer of round
CC       spermatids. Expression continues through stages VI-VII but no
CC       expression is detected in stages IX-XI. In prepubertal testis, isoform
CC       6 is expressed in post-meiotic germ cells at the round spermatid stage.
CC       {ECO:0000269|PubMed:8879483}.
CC   -!- PTM: Phosphorylated by PKA. {ECO:0000250|UniProtKB:P53565}.
CC   -!- PTM: As cells progress into S phase, a fraction of CUX1 molecules is
CC       proteolytically processed into N-terminally truncated proteins of 110
CC       kDa by CTSL. Cell cycle-dependent processing of CUX1 serves to generate
CC       a CDP/Cux p110 with distinct DNA binding and transcriptional
CC       properties. {ECO:0000269|PubMed:15099520}.
CC   -!- DISRUPTION PHENOTYPE: Brains from knockout mice show neurons in layer
CC       II-III with a significant decrease in the dendritic length and the
CC       number of branches, as well as a severe reduction of dendritic spines
CC       density. {ECO:0000269|PubMed:20510857}.
CC   -!- MISCELLANEOUS: Asn-1285 may participate in regulating DNA-binding
CC       activity by promoting homo- and heterodimerization.
CC   -!- SIMILARITY: Belongs to the CUT homeobox family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90358.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X75013; CAA52922.1; -; mRNA.
DR   EMBL; U46684; AAB41146.1; -; mRNA.
DR   EMBL; AY037807; AAK59986.1; -; mRNA.
DR   EMBL; AK220173; BAD90358.1; ALT_INIT; mRNA.
DR   EMBL; AF004225; AAD12485.1; -; mRNA.
DR   EMBL; U46683; AAC52775.1; -; mRNA.
DR   CCDS; CCDS71684.1; -. [P53564-3]
DR   PIR; I48314; I48314.
DR   RefSeq; NP_001278162.1; NM_001291233.1.
DR   RefSeq; NP_001278163.1; NM_001291234.1.
DR   RefSeq; NP_034116.3; NM_009986.4.
DR   AlphaFoldDB; P53564; -.
DR   SMR; P53564; -.
DR   BioGRID; 198981; 6.
DR   IntAct; P53564; 5.
DR   MINT; P53564; -.
DR   STRING; 10090.ENSMUSP00000135223; -.
DR   GlyGen; P53564; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P53564; -.
DR   PhosphoSitePlus; P53564; -.
DR   EPD; P53564; -.
DR   jPOST; P53564; -.
DR   MaxQB; P53564; -.
DR   PaxDb; 10090-ENSMUSP00000004097; -.
DR   PeptideAtlas; P53564; -.
DR   ProteomicsDB; 284063; -. [P53564-1]
DR   ProteomicsDB; 284064; -. [P53564-2]
DR   ProteomicsDB; 284065; -. [P53564-3]
DR   ProteomicsDB; 284066; -. [P53564-4]
DR   ProteomicsDB; 284067; -. [P53564-5]
DR   Pumba; P53564; -.
DR   DNASU; 13047; -.
DR   GeneID; 13047; -.
DR   KEGG; mmu:13047; -.
DR   AGR; MGI:88568; -.
DR   CTD; 1523; -.
DR   MGI; MGI:88568; Cux1.
DR   InParanoid; P53564; -.
DR   OrthoDB; 74668at2759; -.
DR   PhylomeDB; P53564; -.
DR   BioGRID-ORCS; 13047; 6 hits in 78 CRISPR screens.
DR   ChiTaRS; Cux1; mouse.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P53564; Protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IMP:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0042491; P:inner ear auditory receptor cell differentiation; IMP:MGI.
DR   GO; GO:0001822; P:kidney development; IGI:MGI.
DR   GO; GO:0030324; P:lung development; IMP:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0000301; P:retrograde transport, vesicle recycling within Golgi; ISO:MGI.
DR   CDD; cd00086; homeodomain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 3.
DR   InterPro; IPR003350; CUT_dom.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   PANTHER; PTHR14043; CCAAT DISPLACEMENT PROTEIN-RELATED; 1.
DR   PANTHER; PTHR14043:SF4; HOMEOBOX PROTEIN CUT-LIKE 1; 1.
DR   Pfam; PF02376; CUT; 3.
DR   Pfam; PF00046; Homeodomain; 1.
DR   SMART; SM01109; CUT; 3.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 3.
DR   PROSITE; PS51042; CUT; 3.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Developmental protein; DNA-binding;
KW   Homeobox; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Repressor; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..1515
FT                   /note="Homeobox protein cut-like 1"
FT                   /id="PRO_0000202394"
FT   CHAIN           754..1515
FT                   /note="CDP/Cux p110"
FT                   /evidence="ECO:0000250|UniProtKB:P39880"
FT                   /id="PRO_0000450798"
FT   DNA_BIND        540..627
FT                   /note="CUT 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00374"
FT   DNA_BIND        929..1016
FT                   /note="CUT 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00374"
FT   DNA_BIND        1112..1199
FT                   /note="CUT 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00374"
FT   DNA_BIND        1239..1298
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          393..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          509..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          644..666
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          680..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          769..871
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          884..923
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1032..1105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1207..1242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1307..1488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          56..361
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        433..453
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..544
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        684..702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        833..847
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        848..869
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        884..905
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        906..923
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1032..1073
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1307..1328
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1449..1467
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            641..642
FT                   /note="Cleavage; by CTSL"
FT                   /evidence="ECO:0000250|UniProtKB:P39880"
FT   SITE            745..753
FT                   /note="Cleavage; by CTSL"
FT                   /evidence="ECO:0000250|UniProtKB:P39880"
FT   MOD_RES         427
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         761
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P39880"
FT   MOD_RES         904
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53565"
FT   MOD_RES         1054
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P39880"
FT   MOD_RES         1064
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53565"
FT   MOD_RES         1265
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P39880"
FT   MOD_RES         1332
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1468
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P39880"
FT   MOD_RES         1496
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P39880"
FT   MOD_RES         1506
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CROSSLNK        783
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P39880"
FT   CROSSLNK        809
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P39880"
FT   CROSSLNK        840
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P39880"
FT   CROSSLNK        1279
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P39880"
FT   VAR_SEQ         1..1055
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:8879483"
FT                   /id="VSP_017360"
FT   VAR_SEQ         1..183
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:7910552"
FT                   /id="VSP_015748"
FT   VAR_SEQ         1..10
FT                   /note="MLCVAGAKLK -> MAANVGSMFQYWKRFDLQQLQ (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_015749"
FT   VAR_SEQ         406..507
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9858552"
FT                   /id="VSP_002311"
FT   VAR_SEQ         630..651
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_015750"
FT   CONFLICT        276
FT                   /note="V -> VEQ (in Ref. 3; AAK59986)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        649
FT                   /note="R -> G (in Ref. 1; CAA52922 and 5; AAD12485)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1480
FT                   /note="G -> A (in Ref. 1; CAA52922)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1485
FT                   /note="P -> L (in Ref. 5; AAD12485)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1515 AA;  165596 MW;  72BC6E8D8ECD78DE CRC64;
     MLCVAGAKLK RELDATATVL ANRQDESEQS RKRLIEQSRE FKKNTPEDLR KQVAPLLKSF
     QGEIDALSKR SKEAEAAFLT VYKRLIDVPD PVPALDVGQQ LEIKVQRLHD IETENQKLRE
     TLEEYNKEFA EVKNQEVTIK ALKEKIREYE QTLKSQAETI ALEKEQKLQN DFAEKERKLQ
     ETQMSTTSKL EEAEHKLQTL QTALEKTRTE LFDLKTKYDE ETTAKADEIE MIMTDLERAN
     QRAEVAQREA ETLREQLSSA NHSLQLASQI QKAPDVAIEV LTRSSLEVEL AAKEREIAQL
     VEDVQRLQAS LTKLRENSAS QISQLEQQLN AKNSTLKQLE EKLKGQADYE EVKKELNTLK
     SMEFAPSEGA GTQDSTKPLE VLLLEKNRSL QSENATLRIS NSDLSGSARR KGRDQPESRR
     PGPLPASPPP QLPRNTGEQV SNTNGTHHFS PAGLSQDFFS SNLASPSLPL ASTGKFALNS
     LLQRQLMQSF YSKAMQEAGS TSTIFSTGPY STNSISSPSP LQQSPDVNGM APSPSQSESA
     GSISEGEEID TAEIARQVKE QLIKHNIGQR IFGHYVLGLS QGSVSEILAR PKPWNKLTVR
     GKEPFHKMKQ FLSDEQNILA LRSIQGRQRE NPGQSLNRLF QEVPKRRNRS EGNITTRIRA
     SETGSDEAIK SILEQAKREL QVQKTAEPVQ TSSTSSSGNS DDAIRSILQQ ARREMEAQQA
     ALDPALKPAP LSQPDLTILT PKHLSASPMS TVSTYPPLAI SLKKTPAAPE TSTAALPSAP
     ALKKEAQDVP TLDPPGSADA AQGVLRPMKS ELVRGSTWKD PWWSPIQPER RNLTSSEETK
     ADETTASGKE RAGSSQPRAE RSQLQGPSAS AEYWKEWPSA ESPYSQSSEL SLTGASRSET
     PQNSPLPSSP IVPMAKPAKP SVPPLTPEQY EVYMYQEVDT IELTRQVKEK LAKNGICQRI
     FGEKVLGLSQ GSVSDMLSRP KPWSKLTQKG REPFIRMQLW LNGELGQGVL PVQGQQQGPV
     LHSVASLQDP LQQGCVSSES TPKTSASCSP APESPMSSSE SVKSLTELVQ QPCPAIETSK
     EGKPPEPSDP PASDSQPTTP LPLSGHSALS IQELVAMSPE LDTYGITKRV KEVLTDNNLG
     QRLFGETILG LTQGSVSDLL ARPKPWHKLS LKGREPFVRM QLWLNDPNNV EKLMDMKRME
     KKAYMKRRHS SVSDSQPCEP PSVGIDYSQG ASPQPQHQLK KPRVVLAPEE KEALKRAYQQ
     KPYPSPKTIE ELATQLNLKT STVINWFHNY RSRIRRELFI EEIQAGSQGQ AGASDSPSAR
     SSRAAPSSEG DSCDGVEATD AEEPGGNIVA TKSQGGLAEV AAAPADREEA TQPAEKAKAQ
     PLCSGTPGQD DGEDASRPRP LPEGLADAPA PVPSLAAPAA GEDAATSATA PATATEAPGA
     ARAGPAERSS ALPSTSAPAN APARRPSSLQ SLFGLPEAAG ARDNPVRKKK AANLNSIIHR
     LEKAASREEP IEWEF
//