Q9Y6R1 (S4A4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Electrogenic sodium bicarbonate cotransporter 1
Short name=Sodium bicarbonate cotransporter

Alternative name(s):
Na(+)/HCO3(-) cotransporter
Solute carrier family 4 member 4
kNBC1

Gene names

Name:	SLC4A4
Synonyms:	NBC, NBC1, NBCE1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1079 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Electrogenic sodium/bicarbonate cotransporter with a Na+:HCO3- stoichiometry varying from 1:2 to 1:3. May regulate bicarbonate influx/efflux at the basolateral membrane of cells and regulate intracellular pH. Ref.1 Ref.2 Ref.3 Ref.4
Enzyme regulation	Inhibited by stilbene derivatives and regulated by cyclic AMP.
Subunit structure	Interacts with CA2/carbonic anhydrase 2 and CA4/carbonic anhydrase 4 which may regulate transporter activity. Ref.12 Ref.16 Ref.20 Ref.21
Subcellular location	Basolateral cell membrane; Multi-pass membrane protein Ref.4 Ref.19.
Tissue specificity	Isoform 1 is expressed in pancreas and to a lower extent in heart, skeletal muscle, liver, parotid salivary glands, prostate, colon, stomach, thyroid, brain and spinal chord. Corneal endothelium cells express only isoform 1 (at protein level). Isoform 2 is specifically expressed in kidney at the level of proximal tubules. Ref.1 Ref.2 Ref.3 Ref.4 Ref.11 Ref.14 Ref.18
Post-translational modification	Phosphorylation of Ser-1026 by PKA increases the binding of CA2 and changes the Na+:HCO3- stoichiometry of the transporter from 3:1 to 2:1. Phosphorylation of Thr-49 regulates isoform 1 conductance. N-glycosylation is not necessary for the transporter basic functions.
Involvement in disease	Renal tubular acidosis, proximal, with ocular abnormalities and mental retardation (pRTA-OA) [MIM:604278]: An extremely rare autosomal recessive syndrome characterized by short stature, profound proximal renal tubular acidosis, mental retardation, bilateral glaucoma, cataracts and bandkeratopathy. pRTA is due to a failure of the proximal tubular cells to reabsorb filtered bicarbonate from the urine, leading to urinary bicarbonate wasting and subsequent acidemia. Note: The disease is caused by mutations affecting the gene represented in this entry. Loss of interaction with and stimulation by CA4 is the cause of retinitis pigmentosa type 17 (RP17).
Sequence similarities	Belongs to the anion exchanger (TC 2.A.31) family. [View classification]

Ontologies

Keywords
Biological process	Ion transport Sodium transport Symport Transport
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Retinitis pigmentosa
Domain	Transmembrane Transmembrane helix
Ligand	Sodium
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	basolateral plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	inorganic anion exchanger activity Inferred from electronic annotation. Source: InterPro sodium:bicarbonate symporter activity Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9Y6R1-1)

Also known as: hcNBC; hhNBC; hNBC1; pNBC; pNCB1; pNBC-1; NBC1b;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9Y6R1-2)

Also known as: hkNBC; hkNBCe1; kNBC; kNBC1; kNBC-1; NBC1a;

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: Missing.
     45-85: HKRKTGHKEK...SSSSILKPLI → MSTENVEGKP...FNHSIFTSAV

Isoform 3 (identifier: Q9Y6R1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: Missing.
     45-85: HKRKTGHKEK...SSSSILKPLI → MSTENVEGKP...FNHSIFTSAV
     635-690: ANISISNDTT...LVGNNCNFVP → GEGITLCVYA...EFDVSLPEVF
     691-1079: Missing.

Isoform 4 (identifier: Q9Y6R1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     813-896: Missing.

Isoform 5 (identifier: Q9Y6R1-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1034-1079: SDCPYSEKVP...PTFLERHTSC → EKDHQHSLNA...WRSKGTETTL

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1079	1079	Electrogenic sodium bicarbonate cotransporter 1		PRO_0000079227
Regions
	Topological domain	1 – 468	468	Cytoplasmic Potential
	Transmembrane	469 – 488	20	Helical; Potential
	Topological domain	489 – 504	16	Extracellular Potential
	Transmembrane	505 – 526	22	Helical; Potential
	Topological domain	527 – 554	28	Cytoplasmic Potential
	Transmembrane	555 – 580	26	Helical; Potential
	Topological domain	581 – 691	111	Extracellular Potential
	Transmembrane	692 – 710	19	Helical; Potential
	Topological domain	711 – 725	15	Cytoplasmic Potential
	Transmembrane	726 – 748	23	Helical; Potential
	Topological domain	749 – 777	29	Extracellular Potential
	Transmembrane	778 – 797	20	Helical; Potential
	Topological domain	798 – 822	25	Cytoplasmic Potential
	Transmembrane	823 – 847	25	Helical; Potential
	Topological domain	848 – 881	34	Extracellular Potential
	Transmembrane	882 – 901	20	Helical; Potential
	Topological domain	902 – 949	48	Cytoplasmic Potential
	Transmembrane	950 – 967	18	Helical; Potential
	Topological domain	968 – 970	3	Extracellular Potential
	Transmembrane	971 – 986	16	Helical; Potential
	Topological domain	987 – 1079	93	Cytoplasmic Potential
	Region	748 – 779	32	Interaction with CA4
	Region	1002 – 1004	3	CA2-binding
	Region	1030 – 1033	4	CA2-binding
	Region	1057 – 1059	3	Required for basolateral targeting
	Compositional bias	1009 – 1024	16	Lys-rich
Amino acid modifications
	Modified residue	30	1	Phosphotyrosine By similarity
	Modified residue	49	1	Phosphothreonine; by PKA Ref.17
	Modified residue	254	1	Phosphothreonine By similarity
	Modified residue	255	1	Phosphoserine By similarity
	Modified residue	257	1	Phosphoserine By similarity
	Modified residue	262	1	Phosphoserine By similarity
	Modified residue	1026	1	Phosphoserine; by PKA Ref.9
	Modified residue	1029	1	Phosphoserine By similarity
	Modified residue	1034	1	Phosphoserine By similarity
	Glycosylation	641	1	N-linked (GlcNAc...) By similarity
	Glycosylation	661	1	N-linked (GlcNAc...) By similarity
Natural variations
	Alternative sequence	1 – 44	44	Missing in isoform 2 and isoform 3.		VSP_016704
	Alternative sequence	45 – 85	41	HKRKT…LKPLI → MSTENVEGKPSNLGERGRAR SSTFLRVVQPMFNHSIFTSA V in isoform 2 and isoform 3.		VSP_016705
	Alternative sequence	635 – 690	56	ANISI…CNFVP → GEGITLCVYARFVFGGRCRL HACKFSTCCHGPQELVLFFS LKNSATEFDVSLPEVF in isoform 3.		VSP_016706
	Alternative sequence	691 – 1079	389	Missing in isoform 3.		VSP_016707
	Alternative sequence	813 – 896	84	Missing in isoform 4.		VSP_016708
	Alternative sequence	1034 – 1079	46	SDCPY…RHTSC → EKDHQHSLNATHHADKIPFL QSLGMPSPPRTPVKVVPQIR IELEPEDNDYFWRSKGTETT L in isoform 5.		VSP_041003
	Natural variant	342	1	R → S in pRTA-OA; mistargeting and altered function. Ref.23 Ref.25 Ref.26		VAR_024751
	Natural variant	471	1	S → L in pRTA-OA; mistargeting to the apical membrane and altered function. Ref.24 Ref.25		VAR_024752
	Natural variant	529	1	T → S in pRTA-OA; mistargeting and altered function. Ref.26		VAR_024753
	Natural variant	554	1	R → H in pRTA-OA; mistargeting and altered function. Ref.23 Ref.25 Ref.26		VAR_024754
	Natural variant	843	1	A → V in pRTA-OA; altered function. Ref.26		VAR_024755
	Natural variant	925	1	R → C in pRTA-OA; altered function. Ref.26		VAR_024756
Experimental info
	Mutagenesis	49	1	T → A: Loss of conductance regulation by cAMP; isoform 1. Ref.17
	Mutagenesis	49	1	T → D: Loss of conductance regulation by cAMP; isoform 1. Ref.17
	Mutagenesis	135	1	E → R: Mistargeting and altered function. Ref.25
	Mutagenesis	477	1	Y → F: Moderate reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	493	1	D → N: Prevents membrane targeting. Ref.22
	Mutagenesis	494	1	A → K: Prevents membrane targeting. Ref.22
	Mutagenesis	503	1	E → Q: Strong reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	504	1	S → L: Prevents membrane targeting. Ref.22
	Mutagenesis	536	1	E → Q: Prevents membrane targeting. Ref.22
	Mutagenesis	552	1	E → N: Prevents membrane targeting. Ref.22
	Mutagenesis	554	1	R → D: Prevents membrane targeting. Ref.22
	Mutagenesis	582	1	R → N: Moderate reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	582	1	R → Q: Strong reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	586	1	E → Q: Moderate reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	599	1	D → N: Moderate reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	600	1	A → T: Strong reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	602	1	K → Q: Moderate reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	603	1	K → Q: Strong reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	691	1	D → R: Strong reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	700	1	F → M: Strong reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	711	1	K → E, N or Q: Strong reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	711	1	K → R: No effect on the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	712	1	K → N: Strong reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	714	1	K → Q: Moderate reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	715	1	T → N: Strong reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	721	1	T → G: Moderate reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	724	1	R → E: Strong reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	725	1	K → N: Strong reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	728	1	S → G: Strong reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	729	1	D → N or R: Strong reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	743	1	D → K or N: Prevents membrane targeting. Ref.22
	Mutagenesis	749	1	D → N: Moderate reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	752	1	K → Q: Prevents membrane targeting. Ref.22
	Mutagenesis	766	1	R → Q: Moderate reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	767	1	G → T: Alters interaction with CA4. Ref.16
	Mutagenesis	775	1	E → N: Moderate reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	798	1	D → E, N or R: Strong reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	808 – 809	2	RK → NN: Strong reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	814 – 815	2	KK → NN: Moderate reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	820	1	H → D, N, S or R: Moderate reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	822	1	D → N: Moderate reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	851	1	H → N: Prevents membrane targeting. Ref.22
	Mutagenesis	853	1	D → N: Moderate reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	858 – 860	3	ETE → MSK: Moderate reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	875 – 877	3	EQR → QQQ: Prevents membrane targeting. Ref.22
	Mutagenesis	875	1	E → Q: Strong reduction of the sodium-dependent ion transport activity.
	Mutagenesis	898	1	K → E: Strong reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	925 – 927	3	RLK → NLN: Prevents membrane targeting. Ref.22
	Mutagenesis	948	1	R → E: Strong reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	949	1	R → E: Moderate reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	951	1	H → D: Moderate reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	951	1	H → N or R: Prevents membrane targeting. Ref.22
	Mutagenesis	968	1	K → Q: Moderate reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	987	1	R → E or N: Moderate reduction of the sodium-dependent ion transport activity. Ref.22
	Mutagenesis	1002	1	L → N: Partial loss of interaction with CA2.
	Mutagenesis	1003	1	D → N: Abolishes interaction with CA2.
	Mutagenesis	1004	1	D → N: Partial loss of interaction with CA2.
	Mutagenesis	1026	1	S → A: Prevents phosphorylation by PKA. Loss of regulation by cAMP of the transporter stoichiometry. Ref.9 Ref.17
	Mutagenesis	1026	1	S → D: Loss of regulation by cAMP of the transporter stoichiometry. Shifts transporter stoichiometry from 3:1 to 2:1. Ref.9 Ref.17
	Mutagenesis	1030 – 1033	4	DNDD → NNNN: Abolishes interaction with CA2. Ref.12 Ref.20
	Mutagenesis	1030	1	D → N: Loss of regulation by cAMP of the transporter stoichiometry. Abolishes interaction with CA2. Ref.12
	Mutagenesis	1032	1	D → N: Loss of regulation by cAMP of the transporter stoichiometry. Partial loss of interaction with CA2. Ref.12
	Mutagenesis	1033	1	D → N: No effect on regulation by cAMP of the transporter stoichiometry. Partial loss of interaction with CA2. Ref.12
	Mutagenesis	1057	1	F → A: Targeting to apical membrane. Ref.19
	Sequence conflict	6	1	V → A in AAG47773. Ref.4
	Sequence conflict	49	1	T → A in BAH58226. Ref.6
	Sequence conflict	78	1	S → G in AAF21718. Ref.3
	Sequence conflict	256	1	S → F in AAD42020. Ref.3
	Sequence conflict	263	1	D → E in AAF21718. Ref.3
	Sequence conflict	298	1	P → H in BAH58226. Ref.6
	Sequence conflict	364	1	H → R in AAF21719. Ref.3
	Sequence conflict	605	1	I → V in AAF21718. Ref.3
	Sequence conflict	654	1	S → P in AAF21718. Ref.3
	Sequence conflict	749	1	D → G in AAF21719. Ref.3
	Sequence conflict	799	1	Q → R in AAG47773. Ref.4
	Sequence conflict	856	1	K → R in AAG47773. Ref.4
	Sequence conflict	912	1	M → R in AAF21718. Ref.3
	Sequence conflict	913	1	G → R in AAF21719. Ref.3
	Sequence conflict	940	1	I → V in AAF21718. Ref.3
	Sequence conflict	1007	1	P → S in AAF21719. Ref.3
	Sequence conflict	1069	1	S → P in AAF21719. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (hcNBC) (hhNBC) (hNBC1) (pNBC) (pNCB1) (pNBC-1) (NBC1b) [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 14B981A94DD64293	FASTA	1,079	121,461
	10 20 30 40 50 60 MEDEAVLDRG ASFLKHVCDE EEVEGHHTIY IGVHVPKSYR RRRRHKRKTG HKEKKEKERI 70 80 90 100 110 120 SENYSDKSDI ENADESSSSI LKPLISPAAE RIRFILGEED DSPAPPQLFT ELDELLAVDG 130 140 150 160 170 180 QEMEWKETAR WIKFEEKVEQ GGERWSKPHV ATLSLHSLFE LRTCMEKGSI MLDREASSLP 190 200 210 220 230 240 QLVEMIVDHQ IETGLLKPEL KDKVTYTLLR KHRHQTKKSN LRSLADIGKT VSSASRMFTN 250 260 270 280 290 300 PDNGSPAMTH RNLTSSSLND ISDKPEKDQL KNKFMKKLPR DAEASNVLVG EVDFLDTPFI 310 320 330 340 350 360 AFVRLQQAVM LGALTEVPVP TRFLFILLGP KGKAKSYHEI GRAIATLMSD EVFHDIAYKA 370 380 390 400 410 420 KDRHDLIAGI DEFLDEVIVL PPGEWDPAIR IEPPKSLPSS DKRKNMYSGG ENVQMNGDTP 430 440 450 460 470 480 HDGGHGGGGH GDCEELQRTG RFCGGLIKDI KRKAPFFASD FYDALNIQAL SAILFIYLAT 490 500 510 520 530 540 VTNAITFGGL LGDATDNMQG VLESFLGTAV SGAIFCLFAG QPLTILSSTG PVLVFERLLF 550 560 570 580 590 600 NFSKDNNFDY LEFRLWIGLW SAFLCLILVA TDASFLVQYF TRFTEEGFSS LISFIFIYDA 610 620 630 640 650 660 FKKMIKLADY YPINSNFKVG YNTLFSCTCV PPDPANISIS NDTTLAPEYL PTMSSTDMYH 670 680 690 700 710 720 NTTFDWAFLS KKECSKYGGN LVGNNCNFVP DITLMSFILF LGTYTSSMAL KKFKTSPYFP 730 740 750 760 770 780 TTARKLISDF AIILSILIFC VIDALVGVDT PKLIVPSEFK PTSPNRGWFV PPFGENPWWV 790 800 810 820 830 840 CLAAAIPALL VTILIFMDQQ ITAVIVNRKE HKLKKGAGYH LDLFWVAILM VICSLMALPW 850 860 870 880 890 900 YVAATVISIA HIDSLKMETE TSAPGEQPKF LGVREQRVTG TLVFILTGLS VFMAPILKFI 910 920 930 940 950 960 PMPVLYGVFL YMGVASLNGV QFMDRLKLLL MPLKHQPDFI YLRHVPLRRV HLFTFLQVLC 970 980 990 1000 1010 1020 LALLWILKST VAAIIFPVMI LALVAVRKGM DYLFSQHDLS FLDDVIPEKD KKKKEDEKKK 1030 1040 1050 1060 1070 KKKKGSLDSD NDDSDCPYSE KVPSIKIPMD IMEQQPFLSD SKPSDRERSP TFLERHTSC
	Isoform 2 (hkNBC) (hkNBCe1) (kNBC) (kNBC1) (kNBC-1) (NBC1a) [UniParc]. Checksum: 122096381B33D776	FASTA	1,035	116,040
	10 20 30 40 50 60 MSTENVEGKP SNLGERGRAR SSTFLRVVQP MFNHSIFTSA VSPAAERIRF ILGEEDDSPA 70 80 90 100 110 120 PPQLFTELDE LLAVDGQEME WKETARWIKF EEKVEQGGER WSKPHVATLS LHSLFELRTC 130 140 150 160 170 180 MEKGSIMLDR EASSLPQLVE MIVDHQIETG LLKPELKDKV TYTLLRKHRH QTKKSNLRSL 190 200 210 220 230 240 ADIGKTVSSA SRMFTNPDNG SPAMTHRNLT SSSLNDISDK PEKDQLKNKF MKKLPRDAEA 250 260 270 280 290 300 SNVLVGEVDF LDTPFIAFVR LQQAVMLGAL TEVPVPTRFL FILLGPKGKA KSYHEIGRAI 310 320 330 340 350 360 ATLMSDEVFH DIAYKAKDRH DLIAGIDEFL DEVIVLPPGE WDPAIRIEPP KSLPSSDKRK 370 380 390 400 410 420 NMYSGGENVQ MNGDTPHDGG HGGGGHGDCE ELQRTGRFCG GLIKDIKRKA PFFASDFYDA 430 440 450 460 470 480 LNIQALSAIL FIYLATVTNA ITFGGLLGDA TDNMQGVLES FLGTAVSGAI FCLFAGQPLT 490 500 510 520 530 540 ILSSTGPVLV FERLLFNFSK DNNFDYLEFR LWIGLWSAFL CLILVATDAS FLVQYFTRFT 550 560 570 580 590 600 EEGFSSLISF IFIYDAFKKM IKLADYYPIN SNFKVGYNTL FSCTCVPPDP ANISISNDTT 610 620 630 640 650 660 LAPEYLPTMS STDMYHNTTF DWAFLSKKEC SKYGGNLVGN NCNFVPDITL MSFILFLGTY 670 680 690 700 710 720 TSSMALKKFK TSPYFPTTAR KLISDFAIIL SILIFCVIDA LVGVDTPKLI VPSEFKPTSP 730 740 750 760 770 780 NRGWFVPPFG ENPWWVCLAA AIPALLVTIL IFMDQQITAV IVNRKEHKLK KGAGYHLDLF 790 800 810 820 830 840 WVAILMVICS LMALPWYVAA TVISIAHIDS LKMETETSAP GEQPKFLGVR EQRVTGTLVF 850 860 870 880 890 900 ILTGLSVFMA PILKFIPMPV LYGVFLYMGV ASLNGVQFMD RLKLLLMPLK HQPDFIYLRH 910 920 930 940 950 960 VPLRRVHLFT FLQVLCLALL WILKSTVAAI IFPVMILALV AVRKGMDYLF SQHDLSFLDD 970 980 990 1000 1010 1020 VIPEKDKKKK EDEKKKKKKK GSLDSDNDDS DCPYSEKVPS IKIPMDIMEQ QPFLSDSKPS 1030 DRERSPTFLE RHTSC
	Isoform 3 [UniParc]. Checksum: 285D5E23C540A516	FASTA	646	72,049
	10 20 30 40 50 60 MSTENVEGKP SNLGERGRAR SSTFLRVVQP MFNHSIFTSA VSPAAERIRF ILGEEDDSPA 70 80 90 100 110 120 PPQLFTELDE LLAVDGQEME WKETARWIKF EEKVEQGGER WSKPHVATLS LHSLFELRTC 130 140 150 160 170 180 MEKGSIMLDR EASSLPQLVE MIVDHQIETG LLKPELKDKV TYTLLRKHRH QTKKSNLRSL 190 200 210 220 230 240 ADIGKTVSSA SRMFTNPDNG SPAMTHRNLT SSSLNDISDK PEKDQLKNKF MKKLPRDAEA 250 260 270 280 290 300 SNVLVGEVDF LDTPFIAFVR LQQAVMLGAL TEVPVPTRFL FILLGPKGKA KSYHEIGRAI 310 320 330 340 350 360 ATLMSDEVFH DIAYKAKDRH DLIAGIDEFL DEVIVLPPGE WDPAIRIEPP KSLPSSDKRK 370 380 390 400 410 420 NMYSGGENVQ MNGDTPHDGG HGGGGHGDCE ELQRTGRFCG GLIKDIKRKA PFFASDFYDA 430 440 450 460 470 480 LNIQALSAIL FIYLATVTNA ITFGGLLGDA TDNMQGVLES FLGTAVSGAI FCLFAGQPLT 490 500 510 520 530 540 ILSSTGPVLV FERLLFNFSK DNNFDYLEFR LWIGLWSAFL CLILVATDAS FLVQYFTRFT 550 560 570 580 590 600 EEGFSSLISF IFIYDAFKKM IKLADYYPIN SNFKVGYNTL FSCTCVPPDP GEGITLCVYA 610 620 630 640 RFVFGGRCRL HACKFSTCCH GPQELVLFFS LKNSATEFDV SLPEVF
	Isoform 4 [UniParc]. Checksum: 38B4A37EA047E9AC	FASTA	995	112,272
	10 20 30 40 50 60 MEDEAVLDRG ASFLKHVCDE EEVEGHHTIY IGVHVPKSYR RRRRHKRKTG HKEKKEKERI 70 80 90 100 110 120 SENYSDKSDI ENADESSSSI LKPLISPAAE RIRFILGEED DSPAPPQLFT ELDELLAVDG 130 140 150 160 170 180 QEMEWKETAR WIKFEEKVEQ GGERWSKPHV ATLSLHSLFE LRTCMEKGSI MLDREASSLP 190 200 210 220 230 240 QLVEMIVDHQ IETGLLKPEL KDKVTYTLLR KHRHQTKKSN LRSLADIGKT VSSASRMFTN 250 260 270 280 290 300 PDNGSPAMTH RNLTSSSLND ISDKPEKDQL KNKFMKKLPR DAEASNVLVG EVDFLDTPFI 310 320 330 340 350 360 AFVRLQQAVM LGALTEVPVP TRFLFILLGP KGKAKSYHEI GRAIATLMSD EVFHDIAYKA 370 380 390 400 410 420 KDRHDLIAGI DEFLDEVIVL PPGEWDPAIR IEPPKSLPSS DKRKNMYSGG ENVQMNGDTP 430 440 450 460 470 480 HDGGHGGGGH GDCEELQRTG RFCGGLIKDI KRKAPFFASD FYDALNIQAL SAILFIYLAT 490 500 510 520 530 540 VTNAITFGGL LGDATDNMQG VLESFLGTAV SGAIFCLFAG QPLTILSSTG PVLVFERLLF 550 560 570 580 590 600 NFSKDNNFDY LEFRLWIGLW SAFLCLILVA TDASFLVQYF TRFTEEGFSS LISFIFIYDA 610 620 630 640 650 660 FKKMIKLADY YPINSNFKVG YNTLFSCTCV PPDPANISIS NDTTLAPEYL PTMSSTDMYH 670 680 690 700 710 720 NTTFDWAFLS KKECSKYGGN LVGNNCNFVP DITLMSFILF LGTYTSSMAL KKFKTSPYFP 730 740 750 760 770 780 TTARKLISDF AIILSILIFC VIDALVGVDT PKLIVPSEFK PTSPNRGWFV PPFGENPWWV 790 800 810 820 830 840 CLAAAIPALL VTILIFMDQQ ITAVIVNRKE HKLKFIPMPV LYGVFLYMGV ASLNGVQFMD 850 860 870 880 890 900 RLKLLLMPLK HQPDFIYLRH VPLRRVHLFT FLQVLCLALL WILKSTVAAI IFPVMILALV 910 920 930 940 950 960 AVRKGMDYLF SQHDLSFLDD VIPEKDKKKK EDEKKKKKKK GSLDSDNDDS DCPYSEKVPS 970 980 990 IKIPMDIMEQ QPFLSDSKPS DRERSPTFLE RHTSC
	Isoform 5 [UniParc]. Checksum: B02FF2193A5F95C9	FASTA	1,094	123,181
	10 20 30 40 50 60 MEDEAVLDRG ASFLKHVCDE EEVEGHHTIY IGVHVPKSYR RRRRHKRKTG HKEKKEKERI 70 80 90 100 110 120 SENYSDKSDI ENADESSSSI LKPLISPAAE RIRFILGEED DSPAPPQLFT ELDELLAVDG 130 140 150 160 170 180 QEMEWKETAR WIKFEEKVEQ GGERWSKPHV ATLSLHSLFE LRTCMEKGSI MLDREASSLP 190 200 210 220 230 240 QLVEMIVDHQ IETGLLKPEL KDKVTYTLLR KHRHQTKKSN LRSLADIGKT VSSASRMFTN 250 260 270 280 290 300 PDNGSPAMTH RNLTSSSLND ISDKPEKDQL KNKFMKKLPR DAEASNVLVG EVDFLDTPFI 310 320 330 340 350 360 AFVRLQQAVM LGALTEVPVP TRFLFILLGP KGKAKSYHEI GRAIATLMSD EVFHDIAYKA 370 380 390 400 410 420 KDRHDLIAGI DEFLDEVIVL PPGEWDPAIR IEPPKSLPSS DKRKNMYSGG ENVQMNGDTP 430 440 450 460 470 480 HDGGHGGGGH GDCEELQRTG RFCGGLIKDI KRKAPFFASD FYDALNIQAL SAILFIYLAT 490 500 510 520 530 540 VTNAITFGGL LGDATDNMQG VLESFLGTAV SGAIFCLFAG QPLTILSSTG PVLVFERLLF 550 560 570 580 590 600 NFSKDNNFDY LEFRLWIGLW SAFLCLILVA TDASFLVQYF TRFTEEGFSS LISFIFIYDA 610 620 630 640 650 660 FKKMIKLADY YPINSNFKVG YNTLFSCTCV PPDPANISIS NDTTLAPEYL PTMSSTDMYH 670 680 690 700 710 720 NTTFDWAFLS KKECSKYGGN LVGNNCNFVP DITLMSFILF LGTYTSSMAL KKFKTSPYFP 730 740 750 760 770 780 TTARKLISDF AIILSILIFC VIDALVGVDT PKLIVPSEFK PTSPNRGWFV PPFGENPWWV 790 800 810 820 830 840 CLAAAIPALL VTILIFMDQQ ITAVIVNRKE HKLKKGAGYH LDLFWVAILM VICSLMALPW 850 860 870 880 890 900 YVAATVISIA HIDSLKMETE TSAPGEQPKF LGVREQRVTG TLVFILTGLS VFMAPILKFI 910 920 930 940 950 960 PMPVLYGVFL YMGVASLNGV QFMDRLKLLL MPLKHQPDFI YLRHVPLRRV HLFTFLQVLC 970 980 990 1000 1010 1020 LALLWILKST VAAIIFPVMI LALVAVRKGM DYLFSQHDLS FLDDVIPEKD KKKKEDEKKK 1030 1040 1050 1060 1070 1080 KKKKGSLDSD NDDEKDHQHS LNATHHADKI PFLQSLGMPS PPRTPVKVVP QIRIELEPED 1090 NDYFWRSKGT ETTL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and functional expression of a human kidney Na+:HCO3-cotransporter." Burnham C.E., Amlal H., Wang Z., Shull G.E., Soleimani M. J. Biol. Chem. 272:19111-19114(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY. Tissue: Kidney.
[2]	"Molecular cloning, chromosomal localization, tissue distribution, and functional expression of the human pancreatic sodium bicarbonate cotransporter." Abuladze N., Lee I., Newman D., Hwang J., Boorer K., Pushkin A., Kurtz I. J. Biol. Chem. 273:17689-17695(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY. Tissue: Pancreas.
[3]	"Cloning and characterization of a human electrogenic Na+-HCO-3 cotransporter isoform (hhNBC)." Choi I., Romero M.F., Khandoudi N., Bril A., Boron W.F. Am. J. Physiol. 276:C576-C584(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY. Tissue: Heart, Kidney and Prostate.
[4]	"Identification and cloning of the Na/HCO3- cotransporter (NBC) in human corneal endothelium." Sun X.C., Bonanno J.A. Exp. Eye Res. 77:287-295(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN CORNEAL ENDOTHELIAL CELLS, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. Tissue: Corneal endothelium.
[5]	"Homo sapiens sodium bicarbonate cotransporter NBC1 splice variant." Pushkin A., Abuladze N., Kurtz I. Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4). Tissue: Skeletal muscle.
[6]	"cDNA cloning and characterization of human sodium bicarbonate cotransporter, bNBC, a brain type splicing variant of SLC4A4 gene." Yamada H., Nagayoshi A., Kuroda Y., Mizutani A., Ando H., Seki G., Mikoshiba K. Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
[7]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Kidney.
[9]	"Phosphorylation of Ser(982) in the sodium bicarbonate cotransporter kNBC1 shifts the HCO(3)(-):Na(+) stoichiometry from 3:1 to 2:1 in murine proximal tubule cells." Gross E., Hawkins K., Pushkin A., Sassani P., Dukkipati R., Abuladze N., Hopfer U., Kurtz I. J. Physiol. (Lond.) 537:659-665(2001) [PubMed] [Europe PMC] [Abstract] Cited for: REGULATION, MUTAGENESIS OF SER-1026, PHOSPHORYLATION AT SER-1026.
[10]	Erratum Gross E., Hawkins K., Pushkin A., Sassani P., Dukkipati R., Abuladze N., Hopfer U., Kurtz I. J. Physiol. (Lond.) 538:1003-1003(2002)
[11]	"Expression of a sodium bicarbonate cotransporter in human parotid salivary glands." Park K., Hurley P.T., Roussa E., Cooper G.J., Smith C.P., Thevenod F., Steward M.C., Case R.M. Arch. Oral Biol. 47:1-9(2002) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[12]	"Regulation of the sodium bicarbonate cotransporter kNBC1 function: role of Asp(986), Asp(988) and kNBC1-carbonic anhydrase II binding." Gross E., Pushkin A., Abuladze N., Fedotoff O., Kurtz I. J. Physiol. (Lond.) 544:679-685(2002) [PubMed] [Europe PMC] [Abstract] Cited for: REGULATION, MUTAGENESIS OF ASP-1030; ASP-1032 AND ASP-1033, INTERACTION WITH CA2.
[13]	"Role of glycosylation in the renal electrogenic Na+-HCO3-cotransporter (NBCe1)." Choi I., Hu L., Rojas J.D., Schmitt B.M., Boron W.F. Am. J. Physiol. 284:F1199-F1206(2003) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION.
[14]	"Localization of NBC-1 variants in human kidney and renal cell carcinoma." Yamada H., Yamazaki S., Moriyama N., Hara C., Horita S., Enomoto Y., Kudo A., Kawakami H., Tanaka Y., Fujita T., Seki G. Biochem. Biophys. Res. Commun. 310:1213-1218(2003) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[15]	"Identification of membrane topography of the electrogenic sodium bicarbonate cotransporter pNBC1 by in vitro transcription/translation." Tatishchev S., Abuladze N., Pushkin A., Newman D., Liu W., Weeks D., Sachs G., Kurtz I. Biochemistry 42:755-765(2003) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY.
[16]	"Direct extracellular interaction between carbonic anhydrase IV and the human NBC1 sodium/bicarbonate co-transporter." Alvarez B.V., Loiselle F.B., Supuran C.T., Schwartz G.J., Casey J.R. Biochemistry 42:12321-12329(2003) [PubMed] [Europe PMC] [Abstract] Cited for: REGULATION, INTERACTION WITH CA2 AND CA4, MUTAGENESIS OF GLY-767.
[17]	"Phosphorylation-induced modulation of pNBC1 function: distinct roles for the amino- and carboxy-termini." Gross E., Fedotoff O., Pushkin A., Abuladze N., Newman D., Kurtz I. J. Physiol. (Lond.) 549:673-682(2003) [PubMed] [Europe PMC] [Abstract] Cited for: REGULATION, MUTAGENESIS OF THR-49 AND SER-1026, PHOSPHORYLATION AT THR-49.
[18]	"Expression of Na+/HCO3- co-transporter proteins (NBCs) in rat and human skeletal muscle." Kristensen J.M., Kristensen M., Juel C. Acta Physiol. Scand. 182:69-76(2004) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[19]	"Identification of a carboxyl-terminal motif essential for the targeting of Na+-HCO-3 cotransporter NBC1 to the basolateral membrane." Li H.C., Worrell R.T., Matthews J.B., Husseinzadeh H., Neumeier L., Petrovic S., Conforti L., Soleimani M. J. Biol. Chem. 279:43190-43197(2004) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF PHE-1057, SUBCELLULAR LOCATION.
[20]	"Molecular mechanism of kNBC1-carbonic anhydrase II interaction in proximal tubule cells." Pushkin A., Abuladze N., Gross E., Newman D., Tatishchev S., Lee I., Fedotoff O., Bondar G., Azimov R., Ngyuen M., Kurtz I. J. Physiol. (Lond.) 559:55-65(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CA2, MUTAGENESIS OF 1002-LEU--ASN-1004 AND 1030-ASP--ASP-1033.
[21]	"Mutant carbonic anhydrase 4 impairs pH regulation and causes retinal photoreceptor degeneration." Yang Z., Alvarez B.V., Chakarova C., Jiang L., Karan G., Frederick J.M., Zhao Y., Sauve Y., Li X., Zrenner E., Wissinger B., Den Hollander A.I., Katz B., Baehr W., Cremers F.P., Casey J.R., Bhattacharya S.S., Zhang K. Hum. Mol. Genet. 14:255-265(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CA4.
[22]	"Critical amino acid residues involved in the electrogenic sodium-bicarbonate cotransporter kNBC1-mediated transport." Abuladze N., Azimov R., Newman D., Sassani P., Liu W., Tatishchev S., Pushkin A., Kurtz I. J. Physiol. (Lond.) 565:717-730(2005) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF TYR-477; ASP-493; ALA-494; GLU-503; SER-504; GLU-536; GLU-552; ARG-554; ARG-582; GLU-586; ASP-599; ALA-600; LYS-602; LYS-603; ASP-691; PHE-700; LYS-711; LYS-712; LYS-714; THR-715; THR-721; ARG-724; LYS-725; SER-728; ASP-729; ASP-743; ASP-749; LYS-752; ARG-766; GLU-775; ASP-798; 808-ARG--LYS-809; 814-LYS--LYS-815; HIS-820; ASP-822; HIS-851; ASP-853; 858-GLU--GLU-860; 875-GLU--ARG-877; LYS-898; 925-ARG--LYS-927; ARG-948; ARG-949; HIS-951; LYS-968 AND ARG-987.
[23]	"Mutations in SLC4A4 cause permanent isolated proximal renal tubular acidosis with ocular abnormalities." Igarashi T., Inatomi J., Sekine T., Cha S.H., Kanai Y., Kunimi M., Tsukamoto K., Satoh H., Shimadzu M., Tozawa F., Mori T., Shiobara M., Seki G., Endou H. Nat. Genet. 23:264-266(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PRTA-OA SER-342 AND HIS-554.
[24]	"A novel missense mutation in the sodium bicarbonate cotransporter (NBCe1/SLC4A4) causes proximal tubular acidosis and glaucoma through ion transport defects." Dinour D., Chang M.-H., Satoh J., Smith B.L., Angle N., Knecht A., Serban I., Holtzman E.J., Romero M.F. J. Biol. Chem. 279:52238-52246(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PRTA-OA LEU-471.
[25]	"Missense mutations in Na+:HCO3- cotransporter NBC1 show abnormal trafficking in polarized kidney cells: a basis of proximal renal tubular acidosis." Li H.C., Szigligeti P., Worrell R.T., Matthews J.B., Conforti L., Soleimani M. Am. J. Physiol. 289:F61-F71(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PRTA-OA SER-342; LEU-471 AND HIS-554, MUTAGENESIS OF GLU-135.
[26]	"Functional analysis of NBC1 mutants associated with proximal renal tubular acidosis and ocular abnormalities." Horita S., Yamada H., Inatomi J., Moriyama N., Sekine T., Igarashi T., Endo Y., Dasouki M., Ekim M., Al-Gazali L., Shimadzu M., Seki G., Fujita T. J. Am. Soc. Nephrol. 16:2270-2278(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PRTA-OA SER-342; SER-529; HIS-554; VAL-843 AND CYS-925.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF007216 mRNA. Translation: AAC51645.1. AF011390 mRNA. Translation: AAC39840.1. AF053753 mRNA. Translation: AAF21718.1. AF053754 mRNA. Translation: AAF21719.1. AF069510 mRNA. Translation: AAD42020.1. AF310248 mRNA. Translation: AAG47773.1. AF157492 mRNA. Translation: AAF80343.1. AB470072 mRNA. Translation: BAH58226.1. AC019089 Genomic DNA. No translation available. AC079230 Genomic DNA. No translation available. AC096713 Genomic DNA. No translation available. AC110783 Genomic DNA. No translation available. AC112226 Genomic DNA. No translation available. BC030977 mRNA. Translation: AAH30977.1.
IPI	IPI00016949. IPI00410270. IPI00411338. IPI00658166. IPI00913897.
RefSeq	NP_001091954.1. NM_001098484.2. NP_003750.1. NM_003759.3.
UniGene	Hs.5462.
3D structure databases
ProteinModelPortal	Q9Y6R1.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-59373N.
IntAct	Q9Y6R1. 2 interactions.
STRING	9606.ENSP00000393557.
PTM databases
PhosphoSite	Q9Y6R1.
Polymorphism databases
DMDM	74721543.
Proteomic databases
PaxDb	Q9Y6R1.
PRIDE	Q9Y6R1.
Protocols and materials databases
DNASU	8671.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000264485; ENSP00000264485; ENSG00000080493. ENST00000340595; ENSP00000344272; ENSG00000080493. ENST00000351898; ENSP00000307349; ENSG00000080493. ENST00000425175; ENSP00000393557; ENSG00000080493. ENST00000512686; ENSP00000422400; ENSG00000080493.
GeneID	8671.
KEGG	hsa:8671.
UCSC	uc003hfy.3. human. uc003hga.2. human. uc003hgc.4. human. uc010iib.3. human.
Organism-specific databases
CTD	8671.
GeneCards	GC04P072017.
HGNC	HGNC:11030. SLC4A4.
HPA	CAB022493.
MIM	603345. gene. 604278. phenotype.
neXtProt	NX_Q9Y6R1.
Orphanet	93607. Proximal renal tubular acidosis with ocular abnormalities and intellectual deficit.
PharmGKB	PA35898.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG251607.
HOVERGEN	HBG004326.
InParanoid	Q9Y6R1.
KO	K13575.
OMA	DIMEQQP.
OrthoDB	EOG4320XB.
PhylomeDB	Q9Y6R1.
Enzyme and pathway databases
Reactome	REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
ArrayExpress	Q9Y6R1.
Bgee	Q9Y6R1.
CleanEx	HS_SLC4A4.
Genevestigator	Q9Y6R1.
GermOnline	ENSG00000080493. Homo sapiens.
Family and domain databases
Gene3D	3.40.1100.10. 1 hit.
InterPro	IPR013769. Band3_cytoplasmic_dom. IPR011531. HCO3_transpt_C. IPR003020. HCO3_transpt_euk. IPR003024. Na/HCO3_transpt. IPR016152. PTrfase/Anion_transptr. [Graphical view]
PANTHER	PTHR11453. PTHR11453. 1 hit.
Pfam	PF07565. Band_3_cyto. 1 hit. PF00955. HCO3_cotransp. 1 hit. [Graphical view]
PRINTS	PR01231. HCO3TRNSPORT. PR01232. NAHCO3TRSPRT.
SUPFAM	SSF55804. PTrfase/Anion_transptr. 1 hit.
TIGRFAMs	TIGR00834. ae. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	SLC4A4. human.
GenomeRNAi	8671.
NextBio	32523.
SOURCE	Search...

Entry information

Entry name

S4A4_HUMAN

Accession

Primary (citable) accession number: Q9Y6R1
Secondary accession number(s): C4B714 , O15153, Q8NEJ2, Q9H262, Q9NRZ1, Q9UIC0, Q9UIC1, Q9UP50

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.