ID   S12A7_MOUSE             Reviewed;        1083 AA.
AC   Q9WVL3; Q3TB23; Q3TDX1; Q3UE50; Q6KAS8;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Solute carrier family 12 member 7;
DE   AltName: Full=Electroneutral potassium-chloride cotransporter 4;
DE   AltName: Full=K-Cl cotransporter 4;
GN   Name=Slc12a7; Synonyms=Kcc4 {ECO:0000303|PubMed:11551954};
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 1), AND TISSUE SPECIFICITY.
RX   PubMed=10347194; DOI=10.1074/jbc.274.23.16355;
RA   Mount D.B., Mercado A., Song L., Xu J., George A.L. Jr., Delpire E.,
RA   Gamba G.;
RT   "Cloning and characterization of KCC3 and KCC4, new members of the cation-
RT   chloride cotransporter gene family.";
RL   J. Biol. Chem. 274:16355-16362(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT   complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT   by screening of terminal sequences of cDNA clones randomly sampled from
RT   size-fractionated libraries.";
RL   DNA Res. 11:127-135(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1-1079 (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Dendritic cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   SUBUNIT, FUNCTION, AND TRANSPORTER ACTIVITY.
RX   PubMed=11551954; DOI=10.1074/jbc.m107155200;
RA   Casula S., Shmukler B.E., Wilhelm S., Stuart-Tilley A.K., Su W.,
RA   Chernova M.N., Brugnara C., Alper S.L.;
RT   "A dominant negative mutant of the KCC1 K-Cl cotransporter: both N- and C-
RT   terminal cytoplasmic domains are required for K-Cl cotransport activity.";
RL   J. Biol. Chem. 276:41870-41878(2001).
RN   [5]
RP   FUNCTION, AND TRANSPORTER ACTIVITY.
RC   TISSUE=Brain;
RX   PubMed=12106695; DOI=10.1016/s0169-328x(02)00190-0;
RA   Song L., Mercado A., Vazquez N., Xie Q., Desai R., George A.L. Jr.,
RA   Gamba G., Mount D.B.;
RT   "Molecular, functional, and genomic characterization of human KCC2, the
RT   neuronal K-Cl cotransporter.";
RL   Brain Res. Mol. Brain Res. 103:91-105(2002).
RN   [6]
RP   FUNCTION, DISEASE, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=11976689; DOI=10.1038/416874a;
RA   Boettger T., Huebner C.A., Maier H., Rust M.B., Beck F.X., Jentsch T.J.;
RT   "Deafness and renal tubular acidosis in mice lacking the K-Cl co-
RT   transporter Kcc4.";
RL   Nature 416:874-878(2002).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-33; THR-37 AND
RP   SER-50, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-331.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA   Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [10]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-331.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; THR-973 AND THR-980, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC   Testis;
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   [12]
RP   SUBCELLULAR LOCATION, AND GLYCOSYLATION AT ASN-312; ASN-331; ASN-344 AND
RP   ASN-360.
RX   PubMed=23376777; DOI=10.1016/j.bbamcr.2013.01.018;
RA   Weng T.Y., Chiu W.T., Liu H.S., Cheng H.C., Shen M.R., Mount D.B.,
RA   Chou C.Y.;
RT   "Glycosylation regulates the function and membrane localization of KCC4.";
RL   Biochim. Biophys. Acta 1833:1133-1146(2013).
CC   -!- FUNCTION: Mediates electroneutral potassium-chloride cotransport when
CC       activated by cell swelling (PubMed:11551954, PubMed:12106695). May
CC       mediate K(+) uptake into Deiters' cells in the cochlea and contribute
CC       to K(+) recycling in the inner ear. Important for the survival of
CC       cochlear outer and inner hair cells and the maintenance of the organ of
CC       Corti (PubMed:11976689). May be required for basolateral Cl(-)
CC       extrusion in the kidney and contribute to renal acidification
CC       (Probable). {ECO:0000269|PubMed:11551954, ECO:0000269|PubMed:11976689,
CC       ECO:0000269|PubMed:12106695, ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(in) + K(+)(in) = chloride(out) + K(+)(out);
CC         Xref=Rhea:RHEA:72427, ChEBI:CHEBI:17996, ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000269|PubMed:11551954, ECO:0000269|PubMed:12106695};
CC   -!- ACTIVITY REGULATION: Activated by N-ethylmaleimide (NEM). Inhibited by
CC       furosemide, DIDS and bumetanide. The inhibition is much stronger in the
CC       presence of 50 mM K(+) in the uptake medium. Inhibited by DIOA.
CC       Inhibited by WNK3. {ECO:0000250|UniProtKB:Q9Y666}.
CC   -!- SUBUNIT: Homomultimer and heteromultimer with other K-Cl
CC       cotransporters. {ECO:0000305|PubMed:11551954}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23376777};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:23376777}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9WVL3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9WVL3-2; Sequence=VSP_027770;
CC   -!- TISSUE SPECIFICITY: Detected in proximal tubules in the kidney, in
CC       particular in basolateral membranes of intercalated cells in the
CC       cortical collecting duct. {ECO:0000269|PubMed:10347194,
CC       ECO:0000269|PubMed:11976689}.
CC   -!- DEVELOPMENTAL STAGE: In 8 day old mice, before the onset of hearing,
CC       detected in membranes of the stria vascularis and in most cells of the
CC       organ of Corti. At P14, when the organ of Corti has matured, expression
CC       is no longer detected in hair cells and the stria, but is restricted to
CC       Deiters' cells that are supporting outer hair cells and to phalangeal
CC       cells enveloping the inner hair cells. {ECO:0000269|PubMed:11976689}.
CC   -!- PTM: Glycosylation at Asn-331 and Asn-344 is required for proper
CC       trafficking to the cell surface, and augments protein stability.
CC       {ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770,
CC       ECO:0000269|PubMed:23376777}.
CC   -!- DISEASE: Note=Defects in Slc12a7 are a cause of deafness due to the
CC       progressive degeneration of outer and inner hair cells in the cochlea
CC       and of neurons in the cochlear ganglion, leading to the loss of the
CC       organ of Corti. {ECO:0000269|PubMed:11976689}.
CC   -!- SIMILARITY: Belongs to the SLC12A transporter family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD21379.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAE42491.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF087436; AAD38328.1; -; mRNA.
DR   EMBL; AK131129; BAD21379.1; ALT_INIT; mRNA.
DR   EMBL; AK149750; BAE29061.1; -; mRNA.
DR   EMBL; AK169950; BAE41477.1; -; mRNA.
DR   EMBL; AK171498; BAE42491.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS26635.1; -. [Q9WVL3-1]
DR   RefSeq; NP_035520.1; NM_011390.2. [Q9WVL3-1]
DR   PDB; 6UKN; EM; 3.65 A; A=1-1083.
DR   PDBsum; 6UKN; -.
DR   AlphaFoldDB; Q9WVL3; -.
DR   EMDB; EMD-20807; -.
DR   SMR; Q9WVL3; -.
DR   BioGRID; 203280; 3.
DR   STRING; 10090.ENSMUSP00000017900; -.
DR   GlyCosmos; Q9WVL3; 4 sites, No reported glycans.
DR   GlyGen; Q9WVL3; 5 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9WVL3; -.
DR   PhosphoSitePlus; Q9WVL3; -.
DR   EPD; Q9WVL3; -.
DR   jPOST; Q9WVL3; -.
DR   MaxQB; Q9WVL3; -.
DR   PaxDb; 10090-ENSMUSP00000017900; -.
DR   PeptideAtlas; Q9WVL3; -.
DR   ProteomicsDB; 255439; -. [Q9WVL3-1]
DR   ProteomicsDB; 255440; -. [Q9WVL3-2]
DR   Pumba; Q9WVL3; -.
DR   Antibodypedia; 22300; 261 antibodies from 30 providers.
DR   DNASU; 20499; -.
DR   Ensembl; ENSMUST00000017900.9; ENSMUSP00000017900.8; ENSMUSG00000017756.10. [Q9WVL3-1]
DR   GeneID; 20499; -.
DR   KEGG; mmu:20499; -.
DR   UCSC; uc007reb.1; mouse. [Q9WVL3-2]
DR   UCSC; uc007rec.1; mouse. [Q9WVL3-1]
DR   AGR; MGI:1342283; -.
DR   CTD; 10723; -.
DR   MGI; MGI:1342283; Slc12a7.
DR   VEuPathDB; HostDB:ENSMUSG00000017756; -.
DR   eggNOG; KOG2082; Eukaryota.
DR   GeneTree; ENSGT00940000157657; -.
DR   HOGENOM; CLU_001883_1_2_1; -.
DR   InParanoid; Q9WVL3; -.
DR   OMA; ICEMGIL; -.
DR   OrthoDB; 5490251at2759; -.
DR   PhylomeDB; Q9WVL3; -.
DR   TreeFam; TF313657; -.
DR   Reactome; R-MMU-426117; Cation-coupled Chloride cotransporters.
DR   BioGRID-ORCS; 20499; 3 hits in 79 CRISPR screens.
DR   ChiTaRS; Slc12a7; mouse.
DR   PRO; PR:Q9WVL3; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q9WVL3; Protein.
DR   Bgee; ENSMUSG00000017756; Expressed in vestibular membrane of cochlear duct and 221 other cell types or tissues.
DR   ExpressionAtlas; Q9WVL3; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0008519; F:ammonium transmembrane transporter activity; IDA:ARUK-UCL.
DR   GO; GO:0015379; F:potassium:chloride symporter activity; IDA:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR   GO; GO:0140157; P:ammonium import across plasma membrane; IDA:ARUK-UCL.
DR   GO; GO:0006884; P:cell volume homeostasis; ISO:MGI.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IDA:MGI.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0055064; P:chloride ion homeostasis; IBA:GO_Central.
DR   GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR   GO; GO:0055075; P:potassium ion homeostasis; IBA:GO_Central.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
DR   Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR   InterPro; IPR004841; AA-permease/SLC12A_dom.
DR   InterPro; IPR000076; KCL_cotranspt.
DR   InterPro; IPR018491; SLC12_C.
DR   InterPro; IPR004842; SLC12A_fam.
DR   NCBIfam; TIGR00930; 2a30; 1.
DR   PANTHER; PTHR11827:SF47; SOLUTE CARRIER FAMILY 12 MEMBER 7; 1.
DR   PANTHER; PTHR11827; SOLUTE CARRIER FAMILY 12, CATION COTRANSPORTERS; 1.
DR   Pfam; PF00324; AA_permease; 2.
DR   Pfam; PF03522; SLC12; 2.
DR   PRINTS; PR01081; KCLTRNSPORT.
DR   Genevisible; Q9WVL3; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Chloride; Deafness;
KW   Glycoprotein; Ion transport; Membrane; Phosphoprotein; Potassium;
KW   Potassium transport; Reference proteome; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..1083
FT                   /note="Solute carrier family 12 member 7"
FT                   /id="PRO_0000178040"
FT   TOPO_DOM        1..118
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        162..200
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        253..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        274..275
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        416..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        437..456
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        457..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        494..514
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        515..553
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        554..574
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        578..598
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        599..624
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        625..645
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        845..865
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        866..1083
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         37
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         50
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT   MOD_RES         62
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y666"
FT   MOD_RES         973
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         980
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        312
FT                   /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT                   /evidence="ECO:0000269|PubMed:23376777"
FT   CARBOHYD        331
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973,
FT                   ECO:0000269|PubMed:19656770, ECO:0000269|PubMed:23376777"
FT   CARBOHYD        344
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:23376777"
FT   CARBOHYD        360
FT                   /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT                   /evidence="ECO:0000269|PubMed:23376777"
FT   VAR_SEQ         1010..1080
FT                   /note="DQSNVRRMHTAVKLNGVVLNKSQDAQLVLLNMPGPPKSRQGDENYMEFLEVL
FT                   TEGLNRVLLVRGGGREVIT -> LLHFMLFENRCWTKHTVIVPFPWSEFRVPVMKGLTG
FT                   ATETHL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_027770"
FT   CONFLICT        40
FT                   /note="T -> M (in Ref. 3; BAE41477)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        355
FT                   /note="Y -> F (in Ref. 3; BAE41477)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        951
FT                   /note="Q -> P (in Ref. 3; BAE29061)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1083 AA;  119481 MW;  E339D43F7D3B6BD7 CRC64;
     MPTNFTVVPV EARADGAGDE AAERTEEPES PESVDQTSPT PGDGNPRENS PFINNVEVER
     ESYFEGKNMA LFEEEMDSNP MVSSLLNKLA NYTNLSQGVV EHEEDEDSRR REVKAPRMGT
     FIGVYLPCLQ NILGVILFLR LTWIVGAAGV MESFLIVAMC CTCTMLTAIS MSAIATNGVV
     PAGGSYYMIS RSLGPEFGGA VGLCFYLGTT FAGAMYILGT IEIFLTYISP SAAIFQAETA
     DGEAAALLNN MRVYGSCALA LMAVVVFVGV KYVNKLALVF LACVVLSILA IYAGVIKTAF
     APPDIPVCLL GNRTLANRNF DTCAKMQVVS NGTVTTALWR LFCNGSSLGA TCDEYFAQNN
     VTEIQGIPGV ASGVFLDNLW STYSDKGAFV EKKGVSSVPV SEESRPGGLP YVLTDIMTYF
     TMLVGIYFPS VTGIMAGSNR SGDLKDAQKS IPTGTILAIV TTSFIYLSCI VLFGACIEGV
     VLRDKFGEAL QGNLVIGMLA WPSPWVIVIG SFFSTCGAGL QSLTGAPRLL QAIARDGIIP
     FLQVFGHGKA NGEPTWALLL TALICETGIL IASLDSVAPI LSMFFLMCYM FVNLACAVQT
     LLRTPNWRPR FKFYHWTLSF LGMSLCLALM FICSWYYALF AMLIAGCIYK YIEYRGAEKE
     WGDGIRGLSL NAARYALLRV EHGPPHTKNW RPQVLVMLNL DSEQCVKHPR LLSFTSQLKA
     GKGLTIVGSV LEGTYLDKHV EAQRAEENIR SLMSAEKTKG FCQLVVSSNL RDGASHLIQS
     AGLGGMKHNT VLMAWPEAWK EADNPFSWKN FVDTVRDTTA AHQALLVAKN IDLFPQNQER
     FSDGNIDVWW IVHDGGMLML LPFLLRQHKV WRKCRMRIFT VAQVDDNSIQ MKKDLQMFLY
     HLRISAEVEV VEMVENDISA FTYEKTLMME QRSQMLKQMQ LSKNEREREA QLIHDRNTAS
     HTTATARTQA PPTPDKVQMT WTKEKLIAEK HRNKDTGPSG FKDLFSLKPD QSNVRRMHTA
     VKLNGVVLNK SQDAQLVLLN MPGPPKSRQG DENYMEFLEV LTEGLNRVLL VRGGGREVIT
     IYS
//