S4A10_HUMAN
ID S4A10_HUMAN Reviewed; 1118 AA.
AC Q6U841; B7Z1R0; B7Z2J0; B7ZLC5; B9EG69; F8W675; Q4ZFX6; Q8TCP2; Q9HCQ6;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Sodium-driven chloride bicarbonate exchanger {ECO:0000303|PubMed:10993873};
DE AltName: Full=Solute carrier family 4 member 10 {ECO:0000312|HGNC:HGNC:13811};
GN Name=SLC4A10 {ECO:0000312|HGNC:HGNC:13811};
GN Synonyms=NBCN2 {ECO:0000303|PubMed:18319254},
GN NCBE {ECO:0000303|PubMed:10993873};
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 2), AND FUNCTION.
RX PubMed=10993873; DOI=10.1074/jbc.c000456200;
RA Wang C.-Z., Yano H., Nagashima K., Seino S.;
RT "The Na+-driven Cl-/HCO3- exchanger. Cloning, tissue distribution, and
RT functional characterization.";
RL J. Biol. Chem. 275:35486-35490(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ALTERNATIVE SPLICING, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=18319254; DOI=10.1074/jbc.m707829200;
RA Parker M.D., Musa-Aziz R., Rojas J.D., Choi I., Daly C.M., Boron W.F.;
RT "Characterization of human SLC4A10 as an electroneutral Na/HCO3
RT cotransporter (NBCn2) with Cl- self-exchange activity.";
RL J. Biol. Chem. 283:12777-12788(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Brain, and Cerebellum;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum, 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 897-1118 (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP GLYCOSYLATION AT ASN-677; ASN-687 AND ASN-697, AND MUTAGENESIS OF ASN-677;
RP ASN-687 AND ASN-697.
RX PubMed=18061361; DOI=10.1016/j.neuroscience.2007.10.015;
RA Chen L.M., Kelly M.L., Rojas J.D., Parker M.D., Gill H.S., Davis B.A.,
RA Boron W.F.;
RT "Use of a new polyclonal antibody to study the distribution and
RT glycosylation of the sodium-coupled bicarbonate transporter NCBE in rodent
RT brain.";
RL Neuroscience 151:374-385(2008).
CC -!- FUNCTION: Sodium/bicarbonate cotransporter which plays an important
CC role in regulating intracellular pH (PubMed:10993873, PubMed:18319254).
CC Has been shown to act as a sodium/bicarbonate cotransporter in exchange
CC for intracellular chloride (By similarity). Has also been shown to act
CC as a sodium/biocarbonate cotransporter which does not couple net influx
CC of bicarbonate to net efflux of chloride, with the observed chloride
CC efflux being due to chloride self-exchange (PubMed:18319254). Controls
CC neuronal pH and may contribute to the secretion of cerebrospinal fluid
CC (By similarity). Reduces the excitability of CA1 pyramidal neurons and
CC modulates short-term synaptic plasticity (By similarity). Required in
CC retinal cells to maintain normal pH which is necessary for normal
CC vision (By similarity). In the kidney, likely to mediate bicarbonate
CC reclamation in the apical membrane of the proximal tubules (By
CC similarity). {ECO:0000250|UniProtKB:Q5DTL9,
CC ECO:0000250|UniProtKB:Q80ZA5, ECO:0000269|PubMed:10993873,
CC ECO:0000269|PubMed:18319254}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q5DTL9}; Multi-pass membrane protein
CC {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q80ZA5};
CC Multi-pass membrane protein {ECO:0000255}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q5DTL9}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q5DTL9}. Perikaryon
CC {ECO:0000250|UniProtKB:Q5DTL9}. Presynapse
CC {ECO:0000250|UniProtKB:Q5DTL9}. Postsynapse
CC {ECO:0000250|UniProtKB:Q5DTL9}. Note=Detected in dendrites and axon
CC terminals of retinal OFF bipolar cells and in axon terminals of ON
CC bipolar cells. In amacrine cells, located in the perikaryon. Also
CC detected in basal and apical dendrites of hippocampal pyramidal cells.
CC {ECO:0000250|UniProtKB:Q5DTL9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=NCBE-B {ECO:0000303|PubMed:18319254};
CC IsoId=Q6U841-1; Sequence=Displayed;
CC Name=2; Synonyms=NCBE-A {ECO:0000303|PubMed:18319254};
CC IsoId=Q6U841-2; Sequence=VSP_019653;
CC Name=3;
CC IsoId=Q6U841-3; Sequence=VSP_044993, VSP_019653;
CC Name=4;
CC IsoId=Q6U841-4; Sequence=VSP_054471, VSP_054472;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the brain.
CC {ECO:0000269|PubMed:18319254}.
CC -!- DOMAIN: The N-terminal cytoplasmic domain is likely to have a high
CC level of intrinsic disorder. {ECO:0000250|UniProtKB:Q80ZA5}.
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000305}.
CC -!- CAUTION: Has been shown to act as a sodium/bicarbonate cotransporter in
CC exchange for intracellular chloride (By similarity). Has also been
CC shown to act as a sodium/biocarbonate cotransporter which is not
CC responsible for net efflux of chloride, with the observed chloride
CC efflux being due to chloride self-exchange (PubMed:18319254).
CC {ECO:0000250|UniProtKB:Q5DTL9, ECO:0000269|PubMed:18319254}.
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DR EMBL; AB040457; BAB18301.1; -; mRNA.
DR EMBL; AY376402; AAQ83632.1; -; mRNA.
DR EMBL; AK293793; BAH11596.1; -; mRNA.
DR EMBL; AK294767; BAH11876.1; -; mRNA.
DR EMBL; AC008063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC062022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC096654; AAX88962.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11364.1; -; Genomic_DNA.
DR EMBL; BC136269; AAI36270.1; -; mRNA.
DR EMBL; BC143714; AAI43715.1; -; mRNA.
DR EMBL; AL713680; CAD28484.1; -; mRNA.
DR EMBL; AL832525; CAD38630.1; -; mRNA.
DR CCDS; CCDS46438.1; -. [Q6U841-2]
DR CCDS; CCDS54411.1; -. [Q6U841-1]
DR CCDS; CCDS54412.1; -. [Q6U841-3]
DR RefSeq; NP_001171486.1; NM_001178015.1. [Q6U841-1]
DR RefSeq; NP_001171487.1; NM_001178016.1. [Q6U841-3]
DR RefSeq; NP_071341.2; NM_022058.3. [Q6U841-2]
DR AlphaFoldDB; Q6U841; -.
DR SMR; Q6U841; -.
DR BioGRID; 121475; 6.
DR IntAct; Q6U841; 6.
DR STRING; 9606.ENSP00000393066; -.
DR DrugBank; DB01390; Sodium bicarbonate.
DR TCDB; 2.A.31.2.14; the anion exchanger (ae) family.
DR GlyGen; Q6U841; 4 sites.
DR iPTMnet; Q6U841; -.
DR PhosphoSitePlus; Q6U841; -.
DR SwissPalm; Q6U841; -.
DR BioMuta; SLC4A10; -.
DR DMDM; 74710237; -.
DR jPOST; Q6U841; -.
DR MassIVE; Q6U841; -.
DR MaxQB; Q6U841; -.
DR PaxDb; Q6U841; -.
DR PeptideAtlas; Q6U841; -.
DR PRIDE; Q6U841; -.
DR ProteomicsDB; 29736; -.
DR ProteomicsDB; 6443; -.
DR ProteomicsDB; 67398; -. [Q6U841-1]
DR ProteomicsDB; 67399; -. [Q6U841-2]
DR Antibodypedia; 48063; 28 antibodies from 12 providers.
DR DNASU; 57282; -.
DR Ensembl; ENST00000375514.9; ENSP00000364664.5; ENSG00000144290.17. [Q6U841-3]
DR Ensembl; ENST00000415876.6; ENSP00000395797.2; ENSG00000144290.17. [Q6U841-2]
DR Ensembl; ENST00000446997.6; ENSP00000393066.1; ENSG00000144290.17. [Q6U841-1]
DR GeneID; 57282; -.
DR KEGG; hsa:57282; -.
DR MANE-Select; ENST00000446997.6; ENSP00000393066.1; NM_001178015.2; NP_001171486.1.
DR UCSC; uc002ubx.5; human. [Q6U841-1]
DR CTD; 57282; -.
DR DisGeNET; 57282; -.
DR GeneCards; SLC4A10; -.
DR HGNC; HGNC:13811; SLC4A10.
DR HPA; ENSG00000144290; Tissue enhanced (brain, choroid plexus, retina).
DR MIM; 605556; gene.
DR neXtProt; NX_Q6U841; -.
DR OpenTargets; ENSG00000144290; -.
DR PharmGKB; PA37810; -.
DR VEuPathDB; HostDB:ENSG00000144290; -.
DR eggNOG; KOG1172; Eukaryota.
DR GeneTree; ENSGT00940000156972; -.
DR InParanoid; Q6U841; -.
DR OMA; KTHQFKD; -.
DR OrthoDB; 265068at2759; -.
DR PhylomeDB; Q6U841; -.
DR TreeFam; TF313630; -.
DR PathwayCommons; Q6U841; -.
DR Reactome; R-HSA-425381; Bicarbonate transporters.
DR SignaLink; Q6U841; -.
DR SIGNOR; Q6U841; -.
DR BioGRID-ORCS; 57282; 5 hits in 1071 CRISPR screens.
DR ChiTaRS; SLC4A10; human.
DR GenomeRNAi; 57282; -.
DR Pharos; Q6U841; Tbio.
DR PRO; PR:Q6U841; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q6U841; protein.
DR Bgee; ENSG00000144290; Expressed in superior frontal gyrus and 84 other tissues.
DR ExpressionAtlas; Q6U841; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097440; C:apical dendrite; IEA:Ensembl.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
DR GO; GO:0097441; C:basal dendrite; IEA:Ensembl.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0097442; C:CA3 pyramidal cell dendrite; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0036477; C:somatodendritic compartment; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0015301; F:anion:anion antiporter activity; IEA:Ensembl.
DR GO; GO:0005452; F:inorganic anion exchanger activity; TAS:Reactome.
DR GO; GO:0008510; F:sodium:bicarbonate symporter activity; IDA:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015701; P:bicarbonate transport; IBA:GO_Central.
DR GO; GO:0048854; P:brain morphogenesis; IEA:Ensembl.
DR GO; GO:0006821; P:chloride transport; NAS:UniProtKB.
DR GO; GO:0050801; P:ion homeostasis; IBA:GO_Central.
DR GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:Ensembl.
DR GO; GO:0021860; P:pyramidal neuron development; IEA:Ensembl.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; ISS:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IEA:Ensembl.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; ISS:UniProtKB.
DR Gene3D; 3.40.930.10; -; 1.
DR InterPro; IPR013769; Band3_cytoplasmic_dom.
DR InterPro; IPR011531; HCO3_transpt-like_TM_dom.
DR InterPro; IPR003020; HCO3_transpt_euk.
DR InterPro; IPR003024; Na/HCO3_transpt.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR PANTHER; PTHR11453; PTHR11453; 1.
DR Pfam; PF07565; Band_3_cyto; 1.
DR Pfam; PF00955; HCO3_cotransp; 1.
DR PRINTS; PR01231; HCO3TRNSPORT.
DR PRINTS; PR01232; NAHCO3TRSPRT.
DR SUPFAM; SSF55804; SSF55804; 1.
DR TIGRFAMs; TIGR00834; ae; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiport; Cell membrane; Cell projection;
KW Glycoprotein; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Sodium; Sodium transport; Symport; Synapse; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1118
FT /note="Sodium-driven chloride bicarbonate exchanger"
FT /id="PRO_0000245240"
FT TOPO_DOM 1..509
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 531..538
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 539..559
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 560..562
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 563..583
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 584..596
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 597..617
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 618..626
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 627..647
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 648..720
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 721..741
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 742..762
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 763..783
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 784..809
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 810..830
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 831..855
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 856..876
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 877..912
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 913..933
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 934..935
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 936..956
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 957..998
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 999..1019
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1020..1118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..75
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DTL9"
FT MOD_RES 94
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5DTL9"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DTL9"
FT MOD_RES 1057
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DTL9"
FT MOD_RES 1085
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DTL9"
FT CARBOHYD 674
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18061361"
FT CARBOHYD 687
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18061361"
FT CARBOHYD 697
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18061361"
FT VAR_SEQ 1..16
FT /note="MEIKDQGAQMEPLLPT -> MQSLGVSGNRKVMQSGTCEPFQSLSHQ (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044993"
FT VAR_SEQ 287..316
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10993873,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_019653"
FT VAR_SEQ 370..408
FT /note="FLFILLGPLGKGQQYHEIGRSIATLMTDEVFHDVAYKAK -> YFMMLPIKL
FT KIVMTWYQELMSFWIRLLFSLLENGIQAFE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054471"
FT VAR_SEQ 409..1118
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054472"
FT MUTAGEN 677
FT /note="N->Q: Reduced glycosylation. Abolishes
FT glycosylation; when associated with Q-687 and Q-697."
FT /evidence="ECO:0000269|PubMed:18061361"
FT MUTAGEN 687
FT /note="N->Q: Reduced glycosylation. Abolishes
FT glycosylation; when associated with Q-677 and Q-697."
FT /evidence="ECO:0000269|PubMed:18061361"
FT MUTAGEN 697
FT /note="N->Q: Reduced glycosylation. Abolishes
FT glycosylation; when associated with Q-677 and Q-687."
FT /evidence="ECO:0000269|PubMed:18061361"
FT CONFLICT 336
FT /note="V -> L (in Ref. 1; BAB18301)"
FT /evidence="ECO:0000305"
FT CONFLICT 699
FT /note="T -> I (in Ref. 3; BAH11596)"
FT /evidence="ECO:0000305"
FT CONFLICT 1008
FT /note="V -> A (in Ref. 3; BAH11596)"
FT /evidence="ECO:0000305"
FT CONFLICT 1009
FT /note="F -> S (in Ref. 1; BAB18301)"
FT /evidence="ECO:0000305"
FT CONFLICT 1015
FT /note="A -> S (in Ref. 1; BAB18301)"
FT /evidence="ECO:0000305"
FT CONFLICT 1033
FT /note="S -> C (in Ref. 1; BAB18301)"
FT /evidence="ECO:0000305"
FT CONFLICT 1048
FT /note="E -> G (in Ref. 3; BAH11596)"
FT /evidence="ECO:0000305"
FT CONFLICT 1049
FT /note="D -> Y (in Ref. 1; BAB18301)"
FT /evidence="ECO:0000305"
FT CONFLICT 1057..1058
FT /note="SM -> CV (in Ref. 1; BAB18301)"
FT /evidence="ECO:0000305"
FT CONFLICT 1060
FT /note="A -> P (in Ref. 1; BAB18301)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1118 AA; 125946 MW; 2376529C2CBE04E2 CRC64;
MEIKDQGAQM EPLLPTRNDE EAVVDRGGTR SILKTHFEKE DLEGHRTLFI GVHVPLGGRK
SHRRHRHRGH KHRKRDRERD SGLEDGRESP SFDTPSQRVQ FILGTEDDDE EHIPHDLFTE
LDEICWREGE DAEWRETARW LKFEEDVEDG GERWSKPYVA TLSLHSLFEL RSCILNGTVL
LDMHANTLEE IADMVLDQQV SSGQLNEDVR HRVHEALMKQ HHHQNQKKLT NRIPIVRSFA
DIGKKQSEPN SMDKNAGQVV SPQSAPACVE NKNDVSRENS TVDFSKGLGG QQKGHTSPCG
MKQRHEKGPP HQQEREVDLH FMKKIPPGAE ASNILVGELE FLDRTVVAFV RLSPAVLLQG
LAEVPIPTRF LFILLGPLGK GQQYHEIGRS IATLMTDEVF HDVAYKAKDR NDLVSGIDEF
LDQVTVLPPG EWDPSIRIEP PKNVPSQEKR KIPAVPNGTA AHGEAEPHGG HSGPELQRTG
RIFGGLILDI KRKAPYFWSD FRDAFSLQCL ASFLFLYCAC MSPVITFGGL LGEATEGRIS
AIESLFGASM TGIAYSLFGG QPLTILGSTG PVLVFEKILF KFCKEYGLSY LSLRASIGLW
TATLCIILVA TDASSLVCYI TRFTEEAFAS LICIIFIYEA LEKLFELSEA YPINMHNDLE
LLTQYSCNCV EPHNPSNGTL KEWRESNISA SDIIWENLTV SECKSLHGEY VGRACGHDHP
YVPDVLFWSV ILFFSTVTLS ATLKQFKTSR YFPTKVRSIV SDFAVFLTIL CMVLIDYAIG
IPSPKLQVPS VFKPTRDDRG WFVTPLGPNP WWTVIAAIIP ALLCTILIFM DQQITAVIIN
RKEHKLKKGC GYHLDLLMVA VMLGVCSIMG LPWFVAATVL SITHVNSLKL ESECSAPGEQ
PKFLGIREQR VTGLMIFILM GSSVFMTSIL KFIPMPVLYG VFLYMGASSL KGIQFFDRIK
LFWMPAKHQP DFIYLRHVPL RKVHLFTIIQ MSCLGLLWII KVSRAAIVFP MMVLALVFVR
KLMDLLFTKR ELSWLDDLMP ESKKKKLEDA EKEEEQSMLA MEDEGTVQLP LEGHYRDDPS
VINISDEMSK TALWRNLLIT ADNSKDKESS FPSKSSPS
