S12A5_MOUSE
ID S12A5_MOUSE Reviewed; 1138 AA.
AC Q91V14; A2A5L0; Q3UHQ2; Q7TQC9; Q80TI5; Q9Z0M7;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Solute carrier family 12 member 5;
DE AltName: Full=Electroneutral potassium-chloride cotransporter 2;
DE AltName: Full=K-Cl cotransporter 2;
DE Short=mKCC2;
DE AltName: Full=Neuronal K-Cl cotransporter;
GN Name=Slc12a5; Synonyms=Kcc2, Kiaa1176;
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 2).
RC STRAIN=ILS, and ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-227 (ISOFORM 2).
RX PubMed=10077537;
RA Haapa S., Suomalainen S., Eerikaeinen S., Airaksinen M., Paulin L.,
RA Savilahti H.;
RT "An efficient DNA sequencing strategy based on bacteriophage Mu in vitro
RT DNA transposition reaction.";
RL Genome Res. 9:308-315(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72 (ISOFORM 1), TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=17715129; DOI=10.1074/jbc.m705095200;
RA Uvarov P., Ludwig A., Markkanen M., Pruunsild P., Kaila K., Delpire E.,
RA Timmusk T., Rivera C., Airaksinen M.S.;
RT "A novel N-terminal isoform of the neuron-specific K-Cl cotransporter
RT KCC2.";
RL J. Biol. Chem. 282:30570-30576(2007).
RN [8]
RP PROTEIN SEQUENCE OF 532-538; 726-747; 813-819; 833-843; 952-961; 1042-1052;
RP 1078-1085 AND 1091-1101, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=11395011; DOI=10.1016/s0896-6273(01)00297-5;
RA Huebner C.A., Stein V., Hermans-Borgmeyer I., Meyer T., Ballanyi K.,
RA Jentsch T.J.;
RT "Disruption of KCC2 reveals an essential role of K-Cl cotransport already
RT in early synaptic inhibition.";
RL Neuron 30:515-524(2001).
RN [10]
RP INTERACTION WITH AP2A1, AND MUTAGENESIS OF 680-LEU-LEU-681 AND
RP 684-GLU-GLU-685.
RX PubMed=18625303; DOI=10.1016/j.cellsig.2008.06.011;
RA Zhao B., Wong A.Y.C., Murshid A., Bowie D., Presley J.F., Bedford F.K.;
RT "Identification of a novel di-leucine motif mediating K(+)/Cl(-)
RT cotransporter KCC2 constitutive endocytosis.";
RL Cell. Signal. 20:1769-1779(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1044; SER-1047 AND SER-1048,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Mediates electroneutral potassium-chloride cotransport in
CC mature neurons and is required for neuronal Cl(-) homeostasis. As major
CC extruder of intracellular chloride, it establishes the low neuronal
CC Cl(-) levels required for chloride influx after binding of GABA-A and
CC glycine to their receptors, with subsequent hyperpolarization and
CC neuronal inhibition. Involved in the regulation of dendritic spine
CC formation and maturation. {ECO:0000250|UniProtKB:Q63633}.
CC -!- ACTIVITY REGULATION: Inhibited by WNK3. {ECO:0000250}.
CC -!- SUBUNIT: Homomultimer and heteromultimer with other K-Cl cotransporters
CC (By similarity). Interacts with AP2A1. {ECO:0000250,
CC ECO:0000269|PubMed:18625303}.
CC -!- SUBCELLULAR LOCATION: Cell projection, dendrite
CC {ECO:0000269|PubMed:11395011}. Cell membrane
CC {ECO:0000269|PubMed:11395011}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11395011}. Note=Detected on dendrites, but not on
CC axons of spinal cord neurons and at GPHN-positive inhibitory synapses.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=KCC2a;
CC IsoId=Q91V14-1; Sequence=Displayed;
CC Name=2; Synonyms=KCC2b;
CC IsoId=Q91V14-2; Sequence=VSP_029910;
CC -!- TISSUE SPECIFICITY: Isoform 2 expressed in brainstem and spinal cord,
CC isoform 1 expressed in brainstem, spinal cord and olfactory bulb of 17
CC dpc embryos. Isoforms 1 and 2 expressed in all parts of the brain and
CC spinal cord in postnatal day 14 mice. {ECO:0000269|PubMed:17715129}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 predominant isoform in 17 dpc brain.
CC Isoform 2 predominant isoform during postnatal development. Detected in
CC the ventral horns of the spinal cord at 12.5 dpc, and throughout the
CC spinal cord at birth.
CC -!- DISRUPTION PHENOTYPE: Death at birth due to severe motor deficits
CC including respiratory failure. Mice lacking isoform 2 die within 2
CC weeks after birth. {ECO:0000269|PubMed:17715129}.
CC -!- SIMILARITY: Belongs to the SLC12A transporter family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65742.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF332063; AAK56092.1; -; mRNA.
DR EMBL; AF332064; AAK56093.1; -; mRNA.
DR EMBL; AK122460; BAC65742.1; ALT_INIT; mRNA.
DR EMBL; AK147262; BAE27805.1; -; mRNA.
DR EMBL; AL591495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC054808; AAH54808.1; -; mRNA.
DR EMBL; AJ011033; CAA09464.1; -; Genomic_DNA.
DR CCDS; CCDS38332.1; -. [Q91V14-2]
DR CCDS; CCDS89581.1; -. [Q91V14-1]
DR RefSeq; NP_065066.2; NM_020333.2. [Q91V14-2]
DR RefSeq; XP_006500006.2; XM_006499943.3.
DR PDB; 7D14; EM; 3.80 A; A/B=1-1138.
DR PDBsum; 7D14; -.
DR AlphaFoldDB; Q91V14; -.
DR SMR; Q91V14; -.
DR BioGRID; 208213; 10.
DR IntAct; Q91V14; 6.
DR MINT; Q91V14; -.
DR STRING; 10090.ENSMUSP00000096690; -.
DR DrugBank; DB01216; Finasteride.
DR GlyConnect; 2730; 5 N-Linked glycans (3 sites).
DR GlyGen; Q91V14; 5 sites, 5 N-linked glycans (3 sites).
DR iPTMnet; Q91V14; -.
DR PhosphoSitePlus; Q91V14; -.
DR SwissPalm; Q91V14; -.
DR MaxQB; Q91V14; -.
DR PaxDb; Q91V14; -.
DR PeptideAtlas; Q91V14; -.
DR PRIDE; Q91V14; -.
DR ProteomicsDB; 253339; -. [Q91V14-1]
DR ProteomicsDB; 253340; -. [Q91V14-2]
DR ABCD; Q91V14; 1 sequenced antibody.
DR Antibodypedia; 1580; 344 antibodies from 29 providers.
DR DNASU; 57138; -.
DR Ensembl; ENSMUST00000099092; ENSMUSP00000096690; ENSMUSG00000017740. [Q91V14-2]
DR Ensembl; ENSMUST00000202623; ENSMUSP00000144623; ENSMUSG00000017740. [Q91V14-1]
DR GeneID; 57138; -.
DR KEGG; mmu:57138; -.
DR UCSC; uc056zqu.1; mouse. [Q91V14-1]
DR CTD; 57468; -.
DR MGI; MGI:1862037; Slc12a5.
DR VEuPathDB; HostDB:ENSMUSG00000017740; -.
DR eggNOG; KOG2082; Eukaryota.
DR GeneTree; ENSGT00940000160827; -.
DR HOGENOM; CLU_001883_1_2_1; -.
DR InParanoid; Q91V14; -.
DR OMA; RAGGHCS; -.
DR OrthoDB; 349744at2759; -.
DR PhylomeDB; Q91V14; -.
DR TreeFam; TF313657; -.
DR Reactome; R-MMU-426117; Cation-coupled Chloride cotransporters.
DR BioGRID-ORCS; 57138; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Slc12a5; mouse.
DR PRO; PR:Q91V14; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q91V14; protein.
DR Bgee; ENSMUSG00000017740; Expressed in retrosplenial region and 188 other tissues.
DR ExpressionAtlas; Q91V14; baseline and differential.
DR Genevisible; Q91V14; MM.
DR GO; GO:0071944; C:cell periphery; IDA:ARUK-UCL.
DR GO; GO:0032590; C:dendrite membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015379; F:potassium:chloride symporter activity; IMP:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0072488; P:ammonium transmembrane transport; ISO:MGI.
DR GO; GO:0006884; P:cell volume homeostasis; IBA:GO_Central.
DR GO; GO:0030644; P:cellular chloride ion homeostasis; ISO:MGI.
DR GO; GO:0006873; P:cellular ion homeostasis; ISO:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
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:0006821; P:chloride transport; IMP:MGI.
DR GO; GO:0060996; P:dendritic spine development; ISO:MGI.
DR GO; GO:0006971; P:hypotonic response; ISO:MGI.
DR GO; GO:0051452; P:intracellular pH reduction; ISO:MGI.
DR GO; GO:0006811; P:ion transport; ISO:MGI.
DR GO; GO:0007612; P:learning; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
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:0006813; P:potassium ion transport; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR GO; GO:0040040; P:thermosensory behavior; IMP:MGI.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR030358; KCC2.
DR InterPro; IPR000076; KCL_cotranspt.
DR InterPro; IPR018491; SLC12_C.
DR InterPro; IPR004842; SLC12A_fam.
DR PANTHER; PTHR11827; PTHR11827; 1.
DR PANTHER; PTHR11827:SF54; PTHR11827:SF54; 1.
DR Pfam; PF00324; AA_permease; 2.
DR Pfam; PF03522; SLC12; 3.
DR PRINTS; PR01081; KCLTRNSPORT.
DR TIGRFAMs; TIGR00930; 2a30; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Chloride; Direct protein sequencing; Glycoprotein; Ion transport; Membrane;
KW Phosphoprotein; Potassium; Potassium transport; Reference proteome;
KW Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1138
FT /note="Solute carrier family 12 member 5"
FT /id="PRO_0000178035"
FT TOPO_DOM 1..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..418
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..496
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 570..590
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 591..630
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 631..651
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 848..868
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 869..1138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..966
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..996
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1039
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 57
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q63633"
FT MOD_RES 1044
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1047
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1048
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 833
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..40
FT /note="MSRRFTVTSLPPAASAASADPESRRHSVADPRRLPREDVK -> MLNNLTDC
FT EDGDGGANP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11471062,
FT ECO:0000303|PubMed:12693553, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_029910"
FT MUTAGEN 680..681
FT /note="LL->AA: Inhibits endocytosis. Abolishes interaction
FT with AP2A1."
FT /evidence="ECO:0000269|PubMed:18625303"
FT MUTAGEN 684..685
FT /note="EE->AA: Decreases endocytosis."
FT /evidence="ECO:0000269|PubMed:18625303"
FT CONFLICT 64
FT /note="Missing (in Ref. 5; AAH54808)"
FT /evidence="ECO:0000305"
FT CONFLICT 859
FT /note="G -> D (in Ref. 3; BAE27805)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1138 AA; 126271 MW; 56059F065B89C407 CRC64;
MSRRFTVTSL PPAASAASAD PESRRHSVAD PRRLPREDVK GDGNPKESSP FINSTDTEKG
REYDGRNMAL FEEEMDTSPM VSSLLSGLAN YTNLPQGSRE HEEAENNEGG KKKPVQAPRM
GTFMGVYLPC LQNIFGVILF LRLTWVVGIA GIMESFCMVF ICCSCTMLTA ISMSAIATNG
VVPAGGSYYM ISRSLGPEFG GAVGLCFYLG TTFAGAMYIL GTIEILLAYL FPAMAIFKAE
DASGEAAAML NNMRVYGTCV LTCMATVVFV GVKYVNKFAL VFLGCVILSI LAIYAGVIKS
AFDPPNFPIC LLGNRTLSRH GFDVCAKLAW EGNETVTTRL WGLFCSSRLL NATCDEYFTR
NNVTEIQGIP GAASGLIKEN LWSSYLTKGV IVERRGMPSV GLADGTPVDM DHPYVFSDMT
SYFTLLVGIY FPSVTGIMAG SNRSGDLRDA QKSIPTGTIL AIATTSAVYI SSVVLFGACI
EGVVLRDKFG EAVNGNLVVG TLAWPSPWVI VIGSFFSTCG AGLQSLTGAP RLLQAISRDG
IVPFLQVFGH GKANGEPTWA LLLTACICEI GILIASLDEV APILSMFFLM CYMFVNLACA
VQTLLRTPNW RPRFRYYHWT LSFLGMSLCL ALMFICSWYY ALVAMLIAGL IYKYIEYRGA
EKEWGDGIRG LSLSAARYAL LRLEEGPPHT KNWRPQLLVL VRVDQDQNVV HPQLLSLTSQ
LKAGKGLTIV GSVLEGTFLD NHPQAQRAEE SIRRLMEAEK VKGFCQVVIS SNLRDGVSHL
IQSGGLGGLQ HNTVLVGWPR NWRQKEDHQT WRNFIELVRE TTAGHLALLV TKNVSMFPGN
PERFSEGSID VWWIVHDGGM LMLLPFLLRH HKVWRKCKMR IFTVAQMDDN SIQMKKDLTT
FLYHLRITAE VEVVEMHESD ISAYTYEKTL VMEQRSQILK QMHLTKNERE REIQSITDES
RGSIRRKNPA NPRLRLNVPE ETACDNEEKP EEEVQLIHDQ SAPSCPSSSP SPGEEPEGER
ETDPEVHLTW TKDKSVAEKN KGPSPVSSEG IKDFFSMKPE WENLNQSNVR RMHTAVRLNE
VIVNKSRDAK LVLLNMPGPP RNRNGDENYM EFLEVLTEQL DRVMLVRGGG REVITIYS
