UT1_HUMAN
ID UT1_HUMAN Reviewed; 389 AA.
AC Q13336; A8K0P3; B3KR62; B3KVX3; C9EHF2; Q86VM5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Urea transporter 1;
DE AltName: Full=Solute carrier family 14 member 1;
DE AltName: Full=Urea transporter, erythrocyte;
GN Name=SLC14A1; Synonyms=HUT11, JK, RACH1, UT1, UTE;
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 1), FUNCTION, TRANSPORTER ACTIVITY,
RP ACTIVITY REGULATION, TISSUE SPECIFICITY, AND VARIANT LYS-44.
RC TISSUE=Bone marrow;
RX PubMed=7989337; DOI=10.1016/s0021-9258(18)31744-7;
RA Olives B., Neau P., Bailly P., Hediger M.A., Rousselet G., Cartron J.-P.,
RA Ripoche P.;
RT "Cloning and functional expression of a urea transporter from human bone
RT marrow cells.";
RL J. Biol. Chem. 269:31649-31652(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8573795; DOI=10.1091/mbc.6.10.1411;
RA Davey S., Beach D.;
RT "RACH2, a novel human gene that complements a fission yeast cell cycle
RT checkpoint mutation.";
RL Mol. Biol. Cell 6:1411-1421(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), POLYMORPHISM, AND VARIANT JK(B)
RP ASN-280.
RX PubMed=9215669; DOI=10.1093/hmg/6.7.1017;
RA Olives B., Merriman M., Bailly P., Bain S., Barnett A., Todd T.,
RA Cartron J.-P., Merriman T.;
RT "The molecular basis of the Kidd blood group polymorphism and its lack of
RT association with type 1 diabetes susceptibility.";
RL Hum. Mol. Genet. 6:1017-1020(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY,
RP SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RC TISSUE=Blood;
RX PubMed=10514515; DOI=10.1074/jbc.274.42.30228;
RA Sidoux-Walter F., Lucien N., Olives B., Gobin R., Rousselet G.,
RA Kamsteeg E.J., Ripoche P., Deen P.M.T., Cartron J.-P., Bailly P.;
RT "At physiological expression levels, the Kidd blood group/urea transporter
RT protein is not a water channel.";
RL J. Biol. Chem. 274:30228-30235(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP LYS-44.
RC TISSUE=Artery smooth muscle, Brain cortex, and Caudate nucleus;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-44 AND ASN-280.
RG SeattleSNPs variation discovery resource;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS VAL-167
RP AND ASN-280.
RC TISSUE=Colon;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-381, AND VARIANT ASN-280.
RA Posadas J.B., Shnyreva M., Gaur P., Nakaya S., Devanaboina M., Teramura G.,
RA Haile A., Gaur L.K.;
RT "Missense mutations that result in serological JKnull phenotypes.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-113; 222-257 AND 317-332, AND
RP VARIANT JK(NULL) MET-319.
RX PubMed=18028269; DOI=10.1111/j.1537-2995.2007.01532.x;
RA Wester E.S., Johnson S.T., Copeland T., Malde R., Lee E., Storry J.R.,
RA Olsson M.L.;
RT "Erythroid urea transporter deficiency due to novel JKnull alleles.";
RL Transfusion 48:365-372(2008).
RN [10]
RP FUNCTION, TRANSPORTER ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=7797558; DOI=10.1074/jbc.270.26.15607;
RA Olives B., Mattei M.G., Huet M., Neau P., Martial S., Cartron J.P.,
RA Bailly P.;
RT "Kidd blood group and urea transport function of human erythrocytes are
RT carried by the same protein.";
RL J. Biol. Chem. 270:15607-15610(1995).
RN [11]
RP FUNCTION, TRANSPORTER ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=8997401; DOI=10.1152/ajprenal.1996.271.6.f1264;
RA Martial S., Olives B., Abrami L., Couriaud C., Bailly P., You G.,
RA Hediger M.A., Cartron J.P., Ripoche P., Rousselet G.;
RT "Functional differentiation of the human red blood cell and kidney urea
RT transporters.";
RL Am. J. Physiol. 271:F1264-F1268(1996).
RN [12]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION IN A COMPLEX
RP WITH STOM.
RX PubMed=23219802; DOI=10.1016/j.bbamem.2012.11.030;
RA Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R.;
RT "Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in
RT human erythrocyte membrane domains.";
RL Biochim. Biophys. Acta 1828:956-966(2013).
RN [13]
RP VARIANT JK(NULL) PRO-291.
RX PubMed=10942407;
RA Sidoux-Walter F., Lucien N., Nissinen R., Sistonen P., Henry S., Moulds J.,
RA Cartron J.-P., Bailly P.;
RT "Molecular heterogeneity of the Jk(null) phenotype: expression analysis of
RT the Jk(S291P) mutation found in Finns.";
RL Blood 96:1566-1573(2000).
RN [14]
RP VARIANT JK(NULL) PRO-291.
RX PubMed=10644814; DOI=10.1046/j.1537-2995.2000.40010069.x;
RA Irshaid N.M., Henry S.M., Olsson M.L.;
RT "Genomic characterization of the Kidd blood group gene: different molecular
RT basis of the Jk(a-b-) phenotype in Polynesians and Finns.";
RL Transfusion 40:69-74(2000).
RN [15]
RP VARIANTS JK(NULL) LYS-74; VAL-167 AND GLU-299.
RX PubMed=18980618; DOI=10.1111/j.1537-2995.2008.01958.x;
RA Liu H.M., Lin J.S., Chen P.S., Lyou J.Y., Chen Y.J., Tzeng C.H.;
RT "Two novel Jk(null) alleles derived from 222C>A in Exon 5 and 896G>A in
RT Exon 9 of the JK gene.";
RL Transfusion 49:259-264(2009).
CC -!- FUNCTION: Mediates the transport of urea driven by a concentration
CC gradient across the cell membrane of erythrocytes (PubMed:7989337,
CC PubMed:10514515, PubMed:7797558, PubMed:8997401). Also mediates the
CC transport of urea across the cell membrane of the renal inner medullary
CC collecting duct which is critical to the urinary concentrating
CC mechanism (By similarity). Facilitates water transport in erythrocytes
CC (By similarity). {ECO:0000250|UniProtKB:Q8VHL0,
CC ECO:0000269|PubMed:10514515, ECO:0000269|PubMed:7797558,
CC ECO:0000269|PubMed:7989337, ECO:0000269|PubMed:8997401}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=urea(in) = urea(out); Xref=Rhea:RHEA:32799, ChEBI:CHEBI:16199;
CC Evidence={ECO:0000269|PubMed:10514515, ECO:0000269|PubMed:7797558,
CC ECO:0000269|PubMed:7989337, ECO:0000269|PubMed:8997401};
CC -!- ACTIVITY REGULATION: Inhibited by phloretin and para-
CC chloromercuribenzene sulfonate. {ECO:0000269|PubMed:10514515,
CC ECO:0000269|PubMed:7989337, ECO:0000269|PubMed:8997401}.
CC -!- SUBUNIT: Homotrimer; each subunit contains a pore through which urea
CC permeates (By similarity). Identified in a complex with STOM
CC (PubMed:23219802). {ECO:0000250|UniProtKB:Q5QF96,
CC ECO:0000269|PubMed:23219802}.
CC -!- INTERACTION:
CC Q13336-2; Q8WVV5: BTN2A2; NbExp=3; IntAct=EBI-19141793, EBI-8648738;
CC Q13336-2; Q9Y3D6: FIS1; NbExp=3; IntAct=EBI-19141793, EBI-3385283;
CC Q13336-2; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-19141793, EBI-11991950;
CC Q13336-2; P30301: MIP; NbExp=3; IntAct=EBI-19141793, EBI-8449636;
CC Q13336-2; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-19141793, EBI-10244780;
CC Q13336-2; Q6UX34: SNORC; NbExp=3; IntAct=EBI-19141793, EBI-11957067;
CC Q13336-2; P0DN84: STRIT1; NbExp=3; IntAct=EBI-19141793, EBI-12200293;
CC Q13336-2; C9JKN6: THSD7B; NbExp=3; IntAct=EBI-19141793, EBI-17192156;
CC Q13336-2; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-19141793, EBI-12111910;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10514515,
CC ECO:0000269|PubMed:23219802, ECO:0000269|PubMed:7797558}; Multi-pass
CC membrane protein {ECO:0000255}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q8VHL0}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Restricted to the basolateral membrane in various
CC portions of the urothelium. {ECO:0000250|UniProtKB:Q8VHL0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13336-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13336-2; Sequence=VSP_041573;
CC -!- TISSUE SPECIFICITY: Detected in erythrocytes (at protein level)
CC (PubMed:23219802). Expressed in spleen erythroblasts and tumoral kidney
CC (PubMed:7989337). {ECO:0000269|PubMed:23219802,
CC ECO:0000269|PubMed:7989337}.
CC -!- POLYMORPHISM: SLC14A1 is responsible for the Kidd blood group system
CC (JK) [MIM:111000]. JK is defined by 2 alleles, JK*01 and JK*02 that
CC give rise to Jk(a) and Jk(b) antigens respectively. The molecular basis
CC of the Jk(a)/Jk(b) antigens is a single variation in position 280; Asp-
CC 280 corresponds to Jk(a) and Asn-280 to Jk(b). Some individuals carry
CC silenced JK*01 and JK*02 alleles, designated JK*01N or JK*02N. They
CC results in a Jk(null) phenotype associated with reduced urea
CC permeability of red blood cells. Jk(null) is not associated with any
CC obvious clinical syndrome except for a urine concentration defect.
CC -!- SIMILARITY: Belongs to the urea transporter family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation
CC database;
CC URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=kidd";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/slc14a1/";
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DR EMBL; L36121; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; U35735; AAB00181.1; -; mRNA.
DR EMBL; Y19039; CAB60834.1; -; mRNA.
DR EMBL; AK091064; BAG52274.1; -; mRNA.
DR EMBL; AK123681; BAG53935.1; -; mRNA.
DR EMBL; AK289608; BAF82297.1; -; mRNA.
DR EMBL; AY942197; AAX20112.1; -; Genomic_DNA.
DR EMBL; BC050539; AAH50539.1; -; mRNA.
DR EMBL; GQ502682; ACV91713.1; -; mRNA.
DR EMBL; EF571316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; EF571317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; EF571318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS11925.1; -. [Q13336-1]
DR CCDS; CCDS45860.1; -. [Q13336-2]
DR PIR; A55662; A55662.
DR RefSeq; NP_001122060.3; NM_001128588.3. [Q13336-2]
DR RefSeq; NP_001139508.2; NM_001146036.2. [Q13336-1]
DR RefSeq; NP_001139509.1; NM_001146037.1. [Q13336-2]
DR RefSeq; NP_056949.4; NM_015865.6. [Q13336-1]
DR PDB; 6QD5; X-ray; 2.40 A; A=31-389.
DR PDBsum; 6QD5; -.
DR AlphaFoldDB; Q13336; -.
DR SMR; Q13336; -.
DR BioGRID; 112451; 39.
DR DIP; DIP-60049N; -.
DR IntAct; Q13336; 12.
DR STRING; 9606.ENSP00000390637; -.
DR BindingDB; Q13336; -.
DR ChEMBL; CHEMBL2390814; -.
DR DrugBank; DB03904; Urea.
DR GuidetoPHARMACOLOGY; 982; -.
DR TCDB; 1.A.28.1.5; the urea transporter (ut) family.
DR GlyGen; Q13336; 1 site.
DR iPTMnet; Q13336; -.
DR PhosphoSitePlus; Q13336; -.
DR SwissPalm; Q13336; -.
DR BioMuta; SLC14A1; -.
DR DMDM; 4033779; -.
DR jPOST; Q13336; -.
DR MassIVE; Q13336; -.
DR PaxDb; Q13336; -.
DR PeptideAtlas; Q13336; -.
DR PRIDE; Q13336; -.
DR ProteomicsDB; 59327; -. [Q13336-1]
DR ProteomicsDB; 59328; -. [Q13336-2]
DR Antibodypedia; 22414; 167 antibodies from 25 providers.
DR DNASU; 6563; -.
DR Ensembl; ENST00000321925.9; ENSP00000318546.4; ENSG00000141469.18. [Q13336-1]
DR Ensembl; ENST00000415427.7; ENSP00000412309.2; ENSG00000141469.18. [Q13336-2]
DR Ensembl; ENST00000436407.7; ENSP00000390637.2; ENSG00000141469.18. [Q13336-2]
DR Ensembl; ENST00000586142.5; ENSP00000470476.1; ENSG00000141469.18. [Q13336-1]
DR Ensembl; ENST00000586951.6; ENSP00000465702.2; ENSG00000141469.18. [Q13336-1]
DR GeneID; 6563; -.
DR KEGG; hsa:6563; -.
DR MANE-Select; ENST00000321925.9; ENSP00000318546.4; NM_015865.7; NP_056949.4.
DR UCSC; uc002lbf.4; human. [Q13336-1]
DR CTD; 6563; -.
DR DisGeNET; 6563; -.
DR GeneCards; SLC14A1; -.
DR HGNC; HGNC:10918; SLC14A1.
DR HPA; ENSG00000141469; Group enriched (brain, prostate, urinary bladder).
DR MalaCards; SLC14A1; -.
DR MIM; 111000; phenotype.
DR MIM; 613868; gene.
DR neXtProt; NX_Q13336; -.
DR OpenTargets; ENSG00000141469; -.
DR PharmGKB; PA35810; -.
DR VEuPathDB; HostDB:ENSG00000141469; -.
DR eggNOG; ENOG502S2GD; Eukaryota.
DR GeneTree; ENSGT00390000018729; -.
DR InParanoid; Q13336; -.
DR OrthoDB; 1478665at2759; -.
DR PhylomeDB; Q13336; -.
DR TreeFam; TF332858; -.
DR PathwayCommons; Q13336; -.
DR Reactome; R-HSA-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
DR SignaLink; Q13336; -.
DR BioGRID-ORCS; 6563; 7 hits in 1055 CRISPR screens.
DR ChiTaRS; SLC14A1; human.
DR GeneWiki; SLC14A1; -.
DR GenomeRNAi; 6563; -.
DR Pharos; Q13336; Tchem.
DR PRO; PR:Q13336; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q13336; protein.
DR Bgee; ENSG00000141469; Expressed in tibia and 132 other tissues.
DR ExpressionAtlas; Q13336; baseline and differential.
DR Genevisible; Q13336; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0015265; F:urea channel activity; IDA:UniProtKB.
DR GO; GO:0015204; F:urea transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005372; F:water transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR GO; GO:0071918; P:urea transmembrane transport; IDA:UniProtKB.
DR GO; GO:0015840; P:urea transport; TAS:ProtInc.
DR Gene3D; 1.10.3430.10; -; 1.
DR InterPro; IPR029020; Ammonium/urea_transptr.
DR InterPro; IPR004937; Urea_transporter.
DR PANTHER; PTHR10464; PTHR10464; 1.
DR Pfam; PF03253; UT; 1.
DR PIRSF; PIRSF016502; Urea_transporter; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Blood group antigen; Cell membrane;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..389
FT /note="Urea transporter 1"
FT /id="PRO_0000065737"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 339
FT /note="Important for channel permeability"
FT /evidence="ECO:0000250|UniProtKB:Q5QF96"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1
FT /note="M -> MNGRSLIGGAGDARHGPVWKDPFGTKAGDAARRGIARLSLALADGSQ
FT EQEPEEEIAM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041573"
FT VARIANT 44
FT /note="E -> K (in dbSNP:rs2298720)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:7989337, ECO:0000269|Ref.6"
FT /id="VAR_022319"
FT VARIANT 74
FT /note="N -> K (in Jk(null); dbSNP:rs749037771)"
FT /evidence="ECO:0000269|PubMed:18980618"
FT /id="VAR_065466"
FT VARIANT 167
FT /note="M -> V (in Jk(null); dbSNP:rs2298719)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:18980618"
FT /id="VAR_051483"
FT VARIANT 171
FT /note="W -> R (in dbSNP:rs9948825)"
FT /id="VAR_051484"
FT VARIANT 280
FT /note="D -> N (in Jk(b); dbSNP:rs1058396)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9215669, ECO:0000269|Ref.6,
FT ECO:0000269|Ref.8"
FT /id="VAR_005669"
FT VARIANT 291
FT /note="S -> P (in Jk(null); dbSNP:rs78242949)"
FT /evidence="ECO:0000269|PubMed:10644814,
FT ECO:0000269|PubMed:10942407"
FT /id="VAR_013752"
FT VARIANT 299
FT /note="G -> E (in Jk(null); dbSNP:rs538368217)"
FT /evidence="ECO:0000269|PubMed:18980618"
FT /id="VAR_065467"
FT VARIANT 319
FT /note="T -> M (in Jk(null); dbSNP:rs565898944)"
FT /evidence="ECO:0000269|PubMed:18028269"
FT /id="VAR_065468"
FT CONFLICT 49
FT /note="L -> M (in Ref. 5; BAF82297)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="R -> Q (in Ref. 8; ACV91713)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="G -> GVG (in Ref. 1)"
FT /evidence="ECO:0000305"
FT HELIX 32..38
FT /evidence="ECO:0007829|PDB:6QD5"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:6QD5"
FT HELIX 54..67
FT /evidence="ECO:0007829|PDB:6QD5"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6QD5"
FT HELIX 75..88
FT /evidence="ECO:0007829|PDB:6QD5"
FT HELIX 90..109
FT /evidence="ECO:0007829|PDB:6QD5"
FT HELIX 114..118
FT /evidence="ECO:0007829|PDB:6QD5"
FT TURN 119..123
FT /evidence="ECO:0007829|PDB:6QD5"
FT HELIX 124..136
FT /evidence="ECO:0007829|PDB:6QD5"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:6QD5"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:6QD5"
FT HELIX 147..168
FT /evidence="ECO:0007829|PDB:6QD5"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:6QD5"
FT HELIX 178..191
FT /evidence="ECO:0007829|PDB:6QD5"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:6QD5"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:6QD5"
FT HELIX 219..231
FT /evidence="ECO:0007829|PDB:6QD5"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:6QD5"
FT HELIX 239..252
FT /evidence="ECO:0007829|PDB:6QD5"
FT HELIX 254..273
FT /evidence="ECO:0007829|PDB:6QD5"
FT HELIX 278..282
FT /evidence="ECO:0007829|PDB:6QD5"
FT TURN 283..287
FT /evidence="ECO:0007829|PDB:6QD5"
FT HELIX 288..297
FT /evidence="ECO:0007829|PDB:6QD5"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:6QD5"
FT HELIX 306..331
FT /evidence="ECO:0007829|PDB:6QD5"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:6QD5"
FT HELIX 340..351
FT /evidence="ECO:0007829|PDB:6QD5"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:6QD5"
FT HELIX 370..384
FT /evidence="ECO:0007829|PDB:6QD5"
SQ SEQUENCE 389 AA; 42528 MW; 08625B8B66C310F2 CRC64;
MEDSPTMVRV DSPTMVRGEN QVSPCQGRRC FPKALGYVTG DMKELANQLK DKPVVLQFID
WILRGISQVV FVNNPVSGIL ILVGLLVQNP WWALTGWLGT VVSTLMALLL SQDRSLIASG
LYGYNATLVG VLMAVFSDKG DYFWWLLLPV CAMSMTCPIF SSALNSMLSK WDLPVFTLPF
NMALSMYLSA TGHYNPFFPA KLVIPITTAP NISWSDLSAL ELLKSIPVGV GQIYGCDNPW
TGGIFLGAIL LSSPLMCLHA AIGSLLGIAA GLSLSAPFED IYFGLWGFNS SLACIAMGGM
FMALTWQTHL LALGCALFTA YLGVGMANFM AEVGLPACTW PFCLATLLFL IMTTKNSNIY
KMPLSKVTYP EENRIFYLQA KKRMVESPL
