LOCUS S12A7_MOUSE 1083 aa linear ROD 27-NOV-2024
DEFINITION RecName: Full=Solute carrier family 12 member 7; AltName:
Full=Electroneutral potassium-chloride cotransporter 4; AltName:
Full=K-Cl cotransporter 4.
ACCESSION Q9WVL3
VERSION Q9WVL3.1
DBSOURCE UniProtKB: locus S12A7_MOUSE, accession Q9WVL3;
class: standard.
extra accessions:Q3TB23,Q3TDX1,Q3UE50,Q6KAS8
created: Dec 13, 2002.
sequence updated: Nov 1, 1999.
annotation updated: Nov 27, 2024.
xrefs: AF087436.1, AAD38328.1, AK131129.1, BAD21379.1, AK149750.1,
BAE29061.1, AK169950.1, BAE41477.1, AK171498.1, BAE42491.1,
NP_035520.1, 6UKN_A
xrefs (non-sequence databases): CCDS:CCDS26635.1, PDBsum:6UKN,
AlphaFoldDB:Q9WVL3, EMDB:EMD-20807, SMR:Q9WVL3, BioGRID:203280,
STRING:10090.ENSMUSP00000017900, GlyCosmos:Q9WVL3, GlyGen:Q9WVL3,
iPTMnet:Q9WVL3, PhosphoSitePlus:Q9WVL3, jPOST:Q9WVL3,
PaxDb:10090-ENSMUSP00000017900, PeptideAtlas:Q9WVL3,
ProteomicsDB:255439, ProteomicsDB:255440, Pumba:Q9WVL3,
Antibodypedia:22300, DNASU:20499, Ensembl:ENSMUST00000017900.9,
Ensembl:ENSMUSP00000017900.8, Ensembl:ENSMUSG00000017756.10,
GeneID:20499, KEGG:mmu:20499, UCSC:uc007reb.1, UCSC:uc007rec.1,
AGR:MGI:1342283, CTD:10723, MGI:1342283,
VEuPathDB:HostDB:ENSMUSG00000017756, eggNOG:KOG2082,
GeneTree:ENSGT00940000157657, HOGENOM:CLU_001883_1_2_1,
InParanoid:Q9WVL3, OMA:ICEMGIL, OrthoDB:5490251at2759,
PhylomeDB:Q9WVL3, TreeFam:TF313657, Reactome:R-MMU-426117,
BioGRID-ORCS:20499, ChiTaRS:Slc12a7, PRO:PR:Q9WVL3,
Proteomes:UP000000589, RNAct:Q9WVL3, Bgee:ENSMUSG00000017756,
ExpressionAtlas:Q9WVL3, GO:0005886, GO:0032991, GO:0015377,
GO:0046872, GO:0015379, GO:0019901, GO:0071333, GO:1902476,
GO:1990573, GO:0071805, FunFam:1.20.1740.10:FF:000049,
FunFam:1.20.1740.10:FF:000040, Gene3D:1.20.1740.10,
InterPro:IPR004841, InterPro:IPR000076, InterPro:IPR018491,
InterPro:IPR004842, NCBIfam:TIGR00930, PANTHER:PTHR11827:SF47,
PANTHER:PTHR11827, Pfam:PF00324, Pfam:PF03522, PRINTS:PR01081
KEYWORDS 3D-structure; Alternative splicing; Cell membrane; Chloride;
Deafness; Glycoprotein; Ion transport; Membrane; Metal-binding;
Phosphoprotein; Potassium; Potassium transport; Reference proteome;
Symport; Transmembrane; Transmembrane helix; Transport.
SOURCE Mus musculus (house mouse)
ORGANISM Mus musculus
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE 1 (residues 1 to 1083)
AUTHORS Mount,D.B., Mercado,A., Song,L., Xu,J., George,A.L. Jr., Delpire,E.
and Gamba,G.
TITLE Cloning and characterization of KCC3 and KCC4, new members of the
cation-chloride cotransporter gene family
JOURNAL J Biol Chem 274 (23), 16355-16362 (1999)
PUBMED 10347194
REMARK NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
REFERENCE 2 (residues 1 to 1083)
AUTHORS Okazaki,N., Kikuno,R., Ohara,R., Inamoto,S., Koseki,H., Hiraoka,S.,
Saga,Y., Kitamura,H., Nakagawa,T., Nagase,T., Ohara,O. and Koga,H.
TITLE Prediction of the coding sequences of mouse homologues of FLJ
genes: the complete nucleotide sequences of 110 mouse
FLJ-homologous cDnas identified by screening of terminal sequences
of cDNA clones randomly sampled from size-fractionated libraries
JOURNAL DNA Res 11 (2), 127-135 (2004)
PUBMED 15449545
REMARK NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).;
TISSUE=Embryonic tail
REFERENCE 3 (residues 1 to 1083)
AUTHORS Carninci,P., Kasukawa,T., Katayama,S., Gough,J., Frith,M.C.,
Maeda,N., Oyama,R., Ravasi,T., Lenhard,B., Wells,C., Kodzius,R.,
Shimokawa,K., Bajic,V.B., Brenner,S.E., Batalov,S., Forrest,A.R.,
Zavolan,M., Davis,M.J., Wilming,L.G., Aidinis,V., Allen,J.E.,
Ambesi-Impiombato,A., Apweiler,R., Aturaliya,R.N., Bailey,T.L.,
Bansal,M., Baxter,L., Beisel,K.W., Bersano,T., Bono,H., Chalk,A.M.,
Chiu,K.P., Choudhary,V., Christoffels,A., Clutterbuck,D.R.,
Crowe,M.L., Dalla,E., Dalrymple,B.P., de Bono,B., Della Gatta,G.,
di Bernardo,D., Down,T., Engstrom,P., Fagiolini,M., Faulkner,G.,
Fletcher,C.F., Fukushima,T., Furuno,M., Futaki,S., Gariboldi,M.,
Georgii-Hemming,P., Gingeras,T.R., Gojobori,T., Green,R.E.,
Gustincich,S., Harbers,M., Hayashi,Y., Hensch,T.K., Hirokawa,N.,
Hill,D., Huminiecki,L., Iacono,M., Ikeo,K., Iwama,A., Ishikawa,T.,
Jakt,M., Kanapin,A., Katoh,M., Kawasawa,Y., Kelso,J., Kitamura,H.,
Kitano,H., Kollias,G., Krishnan,S.P., Kruger,A., Kummerfeld,S.K.,
Kurochkin,I.V., Lareau,L.F., Lazarevic,D., Lipovich,L., Liu,J.,
Liuni,S., McWilliam,S., Madan Babu,M., Madera,M., Marchionni,L.,
Matsuda,H., Matsuzawa,S., Miki,H., Mignone,F., Miyake,S.,
Morris,K., Mottagui-Tabar,S., Mulder,N., Nakano,N., Nakauchi,H.,
Ng,P., Nilsson,R., Nishiguchi,S., Nishikawa,S., Nori,F., Ohara,O.,
Okazaki,Y., Orlando,V., Pang,K.C., Pavan,W.J., Pavesi,G.,
Pesole,G., Petrovsky,N., Piazza,S., Reed,J., Reid,J.F., Ring,B.Z.,
Ringwald,M., Rost,B., Ruan,Y., Salzberg,S.L., Sandelin,A.,
Schneider,C., Schonbach,C., Sekiguchi,K., Semple,C.A., Seno,S.,
Sessa,L., Sheng,Y., Shibata,Y., Shimada,H., Shimada,K., Silva,D.,
Sinclair,B., Sperling,S., Stupka,E., Sugiura,K., Sultana,R.,
Takenaka,Y., Taki,K., Tammoja,K., Tan,S.L., Tang,S., Taylor,M.S.,
Tegner,J., Teichmann,S.A., Ueda,H.R., van Nimwegen,E., Verardo,R.,
Wei,C.L., Yagi,K., Yamanishi,H., Zabarovsky,E., Zhu,S., Zimmer,A.,
Hide,W., Bult,C., Grimmond,S.M., Teasdale,R.D., Liu,E.T.,
Brusic,V., Quackenbush,J., Wahlestedt,C., Mattick,J.S., Hume,D.A.,
Kai,C., Sasaki,D., Tomaru,Y., Fukuda,S., Kanamori-Katayama,M.,
Suzuki,M., Aoki,J., Arakawa,T., Iida,J., Imamura,K., Itoh,M.,
Kato,T., Kawaji,H., Kawagashira,N., Kawashima,T., Kojima,M.,
Kondo,S., Konno,H., Nakano,K., Ninomiya,N., Nishio,T., Okada,M.,
Plessy,C., Shibata,K., Shiraki,T., Suzuki,S., Tagami,M., Waki,K.,
Watahiki,A., Okamura-Oho,Y., Suzuki,H., Kawai,J. and Hayashizaki,Y.
CONSRTM FANTOM Consortium; RIKEN Genome Exploration Research Group and
Genome Science Group (Genome Network Project Core Group)
TITLE The transcriptional landscape of the mammalian genome
JOURNAL Science 309 (5740), 1559-1563 (2005)
PUBMED 16141072
REMARK NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-1079 (ISOFORM 1).;
STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Dendritic cell
Erratum:[Science. 2006 Mar 24;311(5768):1713]
REFERENCE 4 (residues 1 to 1083)
AUTHORS Casula,S., Shmukler,B.E., Wilhelm,S., Stuart-Tilley,A.K., Su,W.,
Chernova,M.N., Brugnara,C. and Alper,S.L.
TITLE A dominant negative mutant of the KCC1 K-Cl cotransporter: both N-
and C-terminal cytoplasmic domains are required for K-Cl
cotransport activity
JOURNAL J Biol Chem 276 (45), 41870-41878 (2001)
PUBMED 11551954
REMARK SUBUNIT, FUNCTION, AND TRANSPORTER ACTIVITY.
REFERENCE 5 (residues 1 to 1083)
AUTHORS Song,L., Mercado,A., Vazquez,N., Xie,Q., Desai,R., George,A.L. Jr.,
Gamba,G. and Mount,D.B.
TITLE Molecular, functional, and genomic characterization of human KCC2,
the neuronal K-Cl cotransporter
JOURNAL Brain Res Mol Brain Res 103 (1-2), 91-105 (2002)
PUBMED 12106695
REMARK FUNCTION, AND TRANSPORTER ACTIVITY.;
TISSUE=Brain
REFERENCE 6 (residues 1 to 1083)
AUTHORS Boettger,T., Hubner,C.A., Maier,H., Rust,M.B., Beck,F.X. and
Jentsch,T.J.
TITLE Deafness and renal tubular acidosis in mice lacking the K-Cl
co-transporter Kcc4
JOURNAL Nature 416 (6883), 874-878 (2002)
PUBMED 11976689
REMARK FUNCTION, DISEASE, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
REFERENCE 7 (residues 1 to 1083)
AUTHORS Villen,J., Beausoleil,S.A., Gerber,S.A. and Gygi,S.P.
TITLE Large-scale phosphorylation analysis of mouse liver
JOURNAL Proc Natl Acad Sci U S A 104 (5), 1488-1493 (2007)
PUBMED 17242355
REMARK PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].;
TISSUE=Liver
REFERENCE 8 (residues 1 to 1083)
AUTHORS Trost,M., English,L., Lemieux,S., Courcelles,M., Desjardins,M. and
Thibault,P.
TITLE The phagosomal proteome in interferon-gamma-activated macrophages
JOURNAL Immunity 30 (1), 143-154 (2009)
PUBMED 19144319
REMARK PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-33; THR-37
AND SER-50, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
REFERENCE 9 (residues 1 to 1083)
AUTHORS Gundry,R.L., Raginski,K., Tarasova,Y., Tchernyshyov,I.,
Bausch-Fluck,D., Elliott,S.T., Boheler,K.R., Van Eyk,J.E. and
Wollscheid,B.
TITLE The mouse C2C12 myoblast cell surface N-linked glycoproteome:
identification, glycosite occupancy, and membrane orientation
JOURNAL Mol Cell Proteomics 8 (11), 2555-2569 (2009)
PUBMED 19656770
REMARK GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-331.;
TISSUE=Myoblast
REFERENCE 10 (residues 1 to 1083)
AUTHORS Wollscheid,B., Bausch-Fluck,D., Henderson,C., O'Brien,R., Bibel,M.,
Schiess,R., Aebersold,R. and Watts,J.D.
TITLE Mass-spectrometric identification and relative quantification of
N-linked cell surface glycoproteins
JOURNAL Nat Biotechnol 27 (4), 378-386 (2009)
PUBMED 19349973
REMARK GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-331.
Erratum:[Nat Biotechnol. 2009 Sep;27(9):864]
REFERENCE 11 (residues 1 to 1083)
AUTHORS Huttlin,E.L., Jedrychowski,M.P., Elias,J.E., Goswami,T., Rad,R.,
Beausoleil,S.A., Villen,J., Haas,W., Sowa,M.E. and Gygi,S.P.
TITLE A tissue-specific atlas of mouse protein phosphorylation and
expression
JOURNAL Cell 143 (7), 1174-1189 (2010)
PUBMED 21183079
REMARK PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; THR-973 AND
THR-980, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].;
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen,
and Testis
REFERENCE 12 (residues 1 to 1083)
AUTHORS Weng,T.Y., Chiu,W.T., Liu,H.S., Cheng,H.C., Shen,M.R., Mount,D.B.
and Chou,C.Y.
TITLE Glycosylation regulates the function and membrane localization of
KCC4
JOURNAL Biochim Biophys Acta 1833 (5), 1133-1146 (2013)
PUBMED 23376777
REMARK SUBCELLULAR LOCATION, AND GLYCOSYLATION AT ASN-312; ASN-331;
ASN-344 AND ASN-360.
COMMENT On or before Oct 22, 2007 this sequence version replaced
gi:123789734, gi:123786558, gi:123784449, gi:81891892.
[FUNCTION] Mediates electroneutral potassium-chloride cotransport
when activated by cell swelling (PubMed:11551954, PubMed:12106695).
May mediate K(+) uptake into Deiters' cells in the cochlea and
contribute to K(+) recycling in the inner ear. Important for the
survival of cochlear outer and inner hair cells and the maintenance
of the organ of Corti (PubMed:11976689). May be required for
basolateral Cl(-) extrusion in the kidney and contribute to renal
acidification (Probable). {ECO:0000269|PubMed:11551954,
ECO:0000269|PubMed:11976689, ECO:0000269|PubMed:12106695,
ECO:0000305}.
[CATALYTIC ACTIVITY] Reaction=K(+)(in) + chloride(in) = K(+)(out) +
chloride(out); Xref=Rhea:RHEA:72427, ChEBI:CHEBI:17996,
ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:11551954,
ECO:0000269|PubMed:12106695}.
ACTIVITY REGULATION: Activated by N-ethylmaleimide (NEM). Inhibited
by furosemide, DIDS and bumetanide. The inhibition is much stronger
in the presence of 50 mM K(+) in the uptake medium. Inhibited by
DIOA. Inhibited by WNK3. {ECO:0000250|UniProtKB:Q9Y666}.
[SUBUNIT] Homodimer; adopts a domain-swap conformation at the
scissor helices connecting the transmembrane domain and C-terminal
domain (By similarity). Heterodimer with K-Cl cotransporter SLC12A5
(By similarity). {ECO:0000250|UniProtKB:Q9Y666}.
[SUBCELLULAR LOCATION] Cell membrane {ECO:0000269|PubMed:23376777};
Multi-pass membrane protein {ECO:0000269|PubMed:23376777}.
[ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
isoforms=2; Name=1; IsoId=Q9WVL3-1; Sequence=Displayed; Name=2;
IsoId=Q9WVL3-2; Sequence=VSP_027770.
[TISSUE SPECIFICITY] Detected in proximal tubules in the kidney, in
particular in basolateral membranes of intercalated cells in the
cortical collecting duct. {ECO:0000269|PubMed:10347194,
ECO:0000269|PubMed:11976689}.
[DEVELOPMENTAL STAGE] In 8 day old mice, before the onset of
hearing, detected in membranes of the stria vascularis and in most
cells of the organ of Corti. At P14, when the organ of Corti has
matured, expression is no longer detected in hair cells and the
stria, but is restricted to Deiters' cells that are supporting
outer hair cells and to phalangeal cells enveloping the inner hair
cells. {ECO:0000269|PubMed:11976689}.
[PTM] Glycosylation at Asn-331 and Asn-344 is required for proper
trafficking to the cell surface, and augments protein stability.
{ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770,
ECO:0000269|PubMed:23376777}.
[DISEASE] Note=Defects in Slc12a7 are a cause of deafness due to
the progressive degeneration of outer and inner hair cells in the
cochlea and of neurons in the cochlear ganglion, leading to the
loss of the organ of Corti. {ECO:0000269|PubMed:11976689}.
[SIMILARITY] Belongs to the SLC12A transporter family. K/Cl
co-transporter subfamily. {ECO:0000305}.
[SEQUENCE CAUTION] Sequence=BAD21379.1; Type=Erroneous initiation;
Note=Extended N-terminus.; Evidence={ECO:0000305};
Sequence=BAE42491.1; Type=Frameshift; Evidence={ECO:0000305}.
FEATURES Location/Qualifiers
source 1..1083
/organism="Mus musculus"
/db_xref="taxon:10090"
gene 1..1083
/gene="Slc12a7"
/gene_synonym="Kcc4"
Protein 1..1083
/product="Solute carrier family 12 member 7"
/note="Electroneutral potassium-chloride cotransporter 4;
K-Cl cotransporter 4"
/UniProtKB_evidence="Evidence at protein level"
Region 1..1083
/region_name="Mature chain"
/note="Solute carrier family 12 member 7.
/id=PRO_0000178040."
Region 1..119
/region_name="Topological domain"
/note="Cytoplasmic. /evidence=ECO:0000305."
Region 1..55
/region_name="Region of interest in the sequence"
/note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
Region 16..31
/region_name="Compositionally biased region"
/note="Basic and acidic residues.
/evidence=ECO:0000256|SAM:MobiDB-lite."
Site 30
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:19144319."
Region 32..55
/region_name="Compositionally biased region"
/note="Polar residues.
/evidence=ECO:0000256|SAM:MobiDB-lite."
Site 33
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:19144319."
Site 37
/site_type="phosphorylation"
/note="Phosphothreonine.
/evidence=ECO:0007744|PubMed:19144319."
Region 40
/region_name="Conflict"
/note="T -> M (in Ref. 3; BAE41477).
/evidence=ECO:0000305."
Region 45..1083
/region_name="AA_permease_2"
/note="Amino acid permease; cl45918"
/db_xref="CDD:459263"
Site 50
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:17242355,
ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079."
Site 62
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:Q9Y666."
Region 120..142
/region_name="Transmembrane region"
/note="Discontinuously helical; Name=1.
/evidence=ECO:0000250|UniProtKB:Q9Y666."
Region 143..149
/region_name="Topological domain"
/note="Extracellular. /evidence=ECO:0000305."
Region 150..172
/region_name="Transmembrane region"
/note="Helical; Name=2.
/evidence=ECO:0000250|UniProtKB:Q9Y666."
Region 173..196
/region_name="Topological domain"
/note="Cytoplasmic. /evidence=ECO:0000305."
Region 197..225
/region_name="Transmembrane region"
/note="Helical; Name=3.
/evidence=ECO:0000250|UniProtKB:Q9Y666."
Region 226..249
/region_name="Topological domain"
/note="Extracellular. /evidence=ECO:0000305."
Region 250..271
/region_name="Transmembrane region"
/note="Helical; Name=4.
/evidence=ECO:0000250|UniProtKB:Q9Y666."
Region 272..300
/region_name="Transmembrane region"
/note="Helical; Name=5.
/evidence=ECO:0000250|UniProtKB:Q9Y666."
Region 301..419
/region_name="Topological domain"
/note="Extracellular. /evidence=ECO:0000305."
Site 312
/site_type="glycosylation"
/note="N-linked (GlcNAc...) (high mannose) asparagine.
/evidence=ECO:0000269|PubMed:23376777."
Site 331
/site_type="glycosylation"
/note="N-linked (GlcNAc...) (complex) asparagine.
/evidence=ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:19656770, ECO:0000269|PubMed:23376777."
Site 344
/site_type="glycosylation"
/note="N-linked (GlcNAc...) (complex) asparagine.
/evidence=ECO:0000269|PubMed:23376777."
Region 355
/region_name="Conflict"
/note="Y -> F (in Ref. 3; BAE41477).
/evidence=ECO:0000305."
Site 360
/site_type="glycosylation"
/note="N-linked (GlcNAc...) (high mannose) asparagine.
/evidence=ECO:0000269|PubMed:23376777."
Region 420..440
/region_name="Transmembrane region"
/note="Helical; Name=6.
/evidence=ECO:0000250|UniProtKB:Q9Y666."
Region 441..450
/region_name="Topological domain"
/note="Cytoplasmic. /evidence=ECO:0000305."
Region 451..473
/region_name="Transmembrane region"
/note="Helical; Name=7.
/evidence=ECO:0000250|UniProtKB:Q9Y666."
Region 474..504
/region_name="Topological domain"
/note="Extracellular. /evidence=ECO:0000305."
Region 505..531
/region_name="Transmembrane region"
/note="Helical; Name=8.
/evidence=ECO:0000250|UniProtKB:Q9Y666."
Region 532..554
/region_name="Topological domain"
/note="Cytoplasmic. /evidence=ECO:0000305."
Region 555..573
/region_name="Transmembrane region"
/note="Helical; Name=9.
/evidence=ECO:0000250|UniProtKB:Q9Y666."
Region 574..598
/region_name="Transmembrane region"
/note="Helical; Name=10.
/evidence=ECO:0000250|UniProtKB:Q9Y666."
Region 599..612
/region_name="Topological domain"
/note="Cytoplasmic. /evidence=ECO:0000305."
Region 613..635
/region_name="Transmembrane region"
/note="Helical; Name=11.
/evidence=ECO:0000250|UniProtKB:Q9Y666."
Region 636..651
/region_name="Transmembrane region"
/note="Helical; Name=12.
/evidence=ECO:0000250|UniProtKB:Q9Y666."
Region 652..1083
/region_name="Topological domain"
/note="Cytoplasmic. /evidence=ECO:0000305."
Region 664..680
/region_name="Region of interest in the sequence"
/note="Scissor helix.
/evidence=ECO:0000250|UniProtKB:Q9Y666."
Region 951
/region_name="Conflict"
/note="Q -> P (in Ref. 3; BAE29061).
/evidence=ECO:0000305."
Site 973
/site_type="phosphorylation"
/note="Phosphothreonine.
/evidence=ECO:0007744|PubMed:21183079."
Site 980
/site_type="phosphorylation"
/note="Phosphothreonine.
/evidence=ECO:0007744|PubMed:21183079."
Region 1010..1080
/region_name="Splicing variant"
/note="DQSNVRRMHTAVKLNGVVLNKSQDAQLVLLNMPGPPKSRQGDENYMEFLEV
LTEGLNRVLLVRGGGREVIT ->
LLHFMLFENRCWTKHTVIVPFPWSEFRVPVMKGLTGATETHL (in isoform 2).
/evidence=ECO:0000303|PubMed:16141072. /id=VSP_027770."
ORIGIN
1 mptnftvvpv earadgagde aaerteepes pesvdqtspt pgdgnprens pfinnvever
61 esyfegknma lfeeemdsnp mvssllnkla nytnlsqgvv eheededsrr revkaprmgt
121 figvylpclq nilgvilflr ltwivgaagv mesflivamc ctctmltais msaiatngvv
181 paggsyymis rslgpefgga vglcfylgtt fagamyilgt ieifltyisp saaifqaeta
241 dgeaaallnn mrvygscala lmavvvfvgv kyvnklalvf lacvvlsila iyagviktaf
301 appdipvcll gnrtlanrnf dtcakmqvvs ngtvttalwr lfcngsslga tcdeyfaqnn
361 vteiqgipgv asgvfldnlw stysdkgafv ekkgvssvpv seesrpgglp yvltdimtyf
421 tmlvgiyfps vtgimagsnr sgdlkdaqks iptgtilaiv ttsfiylsci vlfgaciegv
481 vlrdkfgeal qgnlvigmla wpspwvivig sffstcgagl qsltgaprll qaiardgiip
541 flqvfghgka ngeptwalll talicetgil iasldsvapi lsmfflmcym fvnlacavqt
601 llrtpnwrpr fkfyhwtlsf lgmslclalm ficswyyalf amliagciyk yieyrgaeke
661 wgdgirglsl naaryallrv ehgpphtknw rpqvlvmlnl dseqcvkhpr llsftsqlka
721 gkgltivgsv legtyldkhv eaqraeenir slmsaektkg fcqlvvssnl rdgashliqs
781 aglggmkhnt vlmawpeawk eadnpfswkn fvdtvrdtta ahqallvakn idlfpqnqer
841 fsdgnidvww ivhdggmlml lpfllrqhkv wrkcrmrift vaqvddnsiq mkkdlqmfly
901 hlrisaevev vemvendisa ftyektlmme qrsqmlkqmq lsknererea qlihdrntas
961 httatartqa pptpdkvqmt wtkekliaek hrnkdtgpsg fkdlfslkpd qsnvrrmhta
1021 vklngvvlnk sqdaqlvlln mpgppksrqg denymeflev lteglnrvll vrgggrevit
1081 iys
//