P13866 (SC5A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sodium/glucose cotransporter 1
Short name=Na(+)/glucose cotransporter 1

Alternative name(s):
High affinity sodium-glucose cotransporter
Solute carrier family 5 member 1

Gene names

Name:	SLC5A1
Synonyms:	NAGT, SGLT1

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	664 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Actively transports glucose into cells by Na+ cotransport with a Na+ to glucose coupling ratio of 2:1. Efficient substrate transport in mammalian kidney is provided by the concerted action of a low affinity high capacity and a high affinity low capacity Na+/glucose cotransporter arranged in series along kidney proximal tubules.
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Expressed mainly in intestine and kidney.
Post-translational modification	N-glycosylation is not necessary for the cotransporter function.
Involvement in disease	Congenital glucose/galactose malabsorption (GGM) [MIM:606824]: Intestinal monosaccharide transporter deficiency. It is an autosomal recessive disorder manifesting itself within the first weeks of life. It is characterized by severe diarrhea and dehydration which are usually fatal unless glucose and galactose are eliminated from the diet. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.8 Ref.9 Ref.10
Sequence similarities	Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family. [View classification]

Ontologies

Keywords
Biological process	Ion transport Sodium transport Sugar transport Symport Transport
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Transmembrane Transmembrane helix
Ligand	Sodium
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Traceable author statement. Source: Reactome intestinal absorption Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	apical plasma membrane Inferred from electronic annotation. Source: Compara brush border membrane Inferred from electronic annotation. Source: Compara cell-cell junction Inferred from electronic annotation. Source: Compara integral to plasma membrane Traceable author statement PubMed 8563765. Source: ProtInc
Molecular_function	glucose:sodium symporter activity Inferred from direct assay PubMed 8563765. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EGFR	P00533	3	EBI-1772443,EBI-297353

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P13866-1)

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: P13866-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-127: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 664	664	Sodium/glucose cotransporter 1		PRO_0000105366
Regions
	Topological domain	1 – 28	28	Extracellular Potential
	Transmembrane	29 – 49	21	Helical; Potential
	Topological domain	50 – 64	15	Cytoplasmic Potential
	Transmembrane	65 – 85	21	Helical; Potential
	Topological domain	86 – 105	20	Extracellular Potential
	Transmembrane	106 – 126	21	Helical; Potential
	Topological domain	127 – 142	16	Cytoplasmic Potential
	Transmembrane	143 – 163	21	Helical; Potential
	Topological domain	164 – 178	15	Extracellular Potential
	Transmembrane	179 – 201	23	Helical; Potential
	Topological domain	202 – 208	7	Cytoplasmic Potential
	Transmembrane	209 – 229	21	Helical; Potential
	Topological domain	230 – 277	48	Extracellular Potential
	Transmembrane	278 – 298	21	Helical; Potential
	Topological domain	299 – 313	15	Cytoplasmic Potential
	Transmembrane	314 – 334	21	Helical; Potential
	Topological domain	335 – 380	46	Extracellular Potential
	Transmembrane	381 – 401	21	Helical; Potential
	Topological domain	402 – 423	22	Cytoplasmic Potential
	Transmembrane	424 – 444	21	Helical; Potential
	Topological domain	445 – 455	11	Extracellular Potential
	Transmembrane	456 – 476	21	Helical; Potential
	Topological domain	477 – 484	8	Cytoplasmic Potential
	Transmembrane	485 – 505	21	Helical; Potential
	Topological domain	506 – 526	21	Extracellular Potential
	Transmembrane	527 – 547	21	Helical; Potential
	Topological domain	548 – 643	96	Cytoplasmic Potential
	Transmembrane	644 – 664	21	Helical; Potential
Sites
	Site	43	1	Implicated in sodium coupling By similarity
	Site	300	1	Implicated in sodium coupling By similarity
Amino acid modifications
	Glycosylation	248	1	N-linked (GlcNAc...) Ref.7
Natural variations
	Alternative sequence	1 – 127	127	Missing in isoform 2.		VSP_044782
	Natural variant	28	1	D → G in GGM. Ref.2		VAR_013630
	Natural variant	28	1	D → N in GGM. Ref.8		VAR_007168
	Natural variant	51	1	N → S. Corresponds to variant rs17683011 [ dbSNP | Ensembl ].		VAR_029147
	Natural variant	135	1	R → W in GGM; loss of activity. Ref.10		VAR_021502
	Natural variant	318	1	G → R in GGM. Ref.9		VAR_021503
	Natural variant	411	1	A → T. Corresponds to variant rs17683430 [ dbSNP | Ensembl ].		VAR_029148
	Natural variant	468	1	A → V in GGM. Ref.9		VAR_021504
Experimental info
	Mutagenesis	248	1	N → Q: Loss of N-glycosylation. Ref.7
	Sequence conflict	631	1	K → R in BAH14555. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 2B403376595EAB74	FASTA	664	73,498
	10 20 30 40 50 60 MDSSTWSPKT TAVTRPVETH ELIRNAADIS IIVIYFVVVM AVGLWAMFST NRGTVGGFFL 70 80 90 100 110 120 AGRSMVWWPI GASLFASNIG SGHFVGLAGT GAASGIAIGG FEWNALVLVV VLGWLFVPIY 130 140 150 160 170 180 IKAGVVTMPE YLRKRFGGQR IQVYLSLLSL LLYIFTKISA DIFSGAIFIN LALGLNLYLA 190 200 210 220 230 240 IFLLLAITAL YTITGGLAAV IYTDTLQTVI MLVGSLILTG FAFHEVGGYD AFMEKYMKAI 250 260 270 280 290 300 PTIVSDGNTT FQEKCYTPRA DSFHIFRDPL TGDLPWPGFI FGMSILTLWY WCTDQVIVQR 310 320 330 340 350 360 CLSAKNMSHV KGGCILCGYL KLMPMFIMVM PGMISRILYT EKIACVVPSE CEKYCGTKVG 370 380 390 400 410 420 CTNIAYPTLV VELMPNGLRG LMLSVMLASL MSSLTSIFNS ASTLFTMDIY AKVRKRASEK 430 440 450 460 470 480 ELMIAGRLFI LVLIGISIAW VPIVQSAQSG QLFDYIQSIT SYLGPPIAAV FLLAIFWKRV 490 500 510 520 530 540 NEPGAFWGLI LGLLIGISRM ITEFAYGTGS CMEPSNCPTI ICGVHYLYFA IILFAISFIT 550 560 570 580 590 600 IVVISLLTKP IPDVHLYRLC WSLRNSKEER IDLDAEEENI QEGPKETIEI ETQVPEKKKG 610 620 630 640 650 660 IFRRAYDLFC GLEQHGAPKM TEEEEKAMKM KMTDTSEKPL WRTVLNVNGI ILVTVAVFCH AYFA
	Isoform 2 [UniParc]. Checksum: F7B5A898E54C9476	FASTA	537	60,097
	10 20 30 40 50 60 MPEYLRKRFG GQRIQVYLSL LSLLLYIFTK ISADIFSGAI FINLALGLNL YLAIFLLLAI 70 80 90 100 110 120 TALYTITGGL AAVIYTDTLQ TVIMLVGSLI LTGFAFHEVG GYDAFMEKYM KAIPTIVSDG 130 140 150 160 170 180 NTTFQEKCYT PRADSFHIFR DPLTGDLPWP GFIFGMSILT LWYWCTDQVI VQRCLSAKNM 190 200 210 220 230 240 SHVKGGCILC GYLKLMPMFI MVMPGMISRI LYTEKIACVV PSECEKYCGT KVGCTNIAYP 250 260 270 280 290 300 TLVVELMPNG LRGLMLSVML ASLMSSLTSI FNSASTLFTM DIYAKVRKRA SEKELMIAGR 310 320 330 340 350 360 LFILVLIGIS IAWVPIVQSA QSGQLFDYIQ SITSYLGPPI AAVFLLAIFW KRVNEPGAFW 370 380 390 400 410 420 GLILGLLIGI SRMITEFAYG TGSCMEPSNC PTIICGVHYL YFAIILFAIS FITIVVISLL 430 440 450 460 470 480 TKPIPDVHLY RLCWSLRNSK EERIDLDAEE ENIQEGPKET IEIETQVPEK KKGIFRRAYD 490 500 510 520 530 LFCGLEQHGA PKMTEEEEKA MKMKMTDTSE KPLWRTVLNV NGIILVTVAV FCHAYFA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Homology of the human intestinal Na+/glucose and Escherichia coli Na+/proline cotransporters." Hediger M.A., Turk E., Wright E.M. Proc. Natl. Acad. Sci. U.S.A. 86:5748-5752(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Structure of the human Na+/glucose cotransporter gene SGLT1." Turk E., Martin M.G., Wright E.M. J. Biol. Chem. 269:15204-15209(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GGM GLY-28.
[3]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Heart and Trachea.
[5]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"Membrane topology of the human Na+/glucose cotransporter SGLT1." Turk E., Kerner C.J., Lostao M.P., Wright E.M. J. Biol. Chem. 271:1925-1934(1996) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY, MUTAGENESIS OF ASN-248, GLYCOSYLATION AT ASN-248.
[8]	"Glucose/galactose malabsorption caused by a defect in the Na+/glucose cotransporter." Turk E., Zabel B., Mundlos S., Dyer J., Wright E.M. Nature 350:354-356(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GGM ASN-28.
[9]	"Missense mutations in SGLT1 cause glucose-galactose malabsorption by trafficking defects." Lam J.T., Martin M.G., Turk E., Hirayama B.A., Bosshard N.U., Steinmann B., Wright E.M. Biochim. Biophys. Acta 1453:297-303(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GGM ARG-318 AND VAL-468.
[10]	"A missense mutation in the Na(+)/glucose cotransporter gene SGLT1 in a patient with congenital glucose-galactose malabsorption: normal trafficking but inactivation of the mutant protein." Kasahara M., Maeda M., Hayashi S., Mori Y., Abe T. Biochim. Biophys. Acta 1536:141-147(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GGM TRP-135.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M24847 mRNA. Translation: AAA60320.1. L29339 , L29328, L29330, L29329, L29331, L29332, L29333, L29334, L29335, L29336, L29337, L29338 Genomic DNA. Translation: AAB59448.1. CR456579 mRNA. Translation: CAG30465.1. AK297665 mRNA. Translation: BAH12645.1. AK312948 mRNA. Translation: BAG35789.1. AK316184 mRNA. Translation: BAH14555.1. AL022321 , Z74021, Z80998, Z83839, Z83849 Genomic DNA. Translation: CAI19810.1. Z74021 , AL022321, Z80998, Z83839, Z83849 Genomic DNA. Translation: CAI18756.1. Z80998 , AL022321, Z74021, Z83839, Z83849 Genomic DNA. Translation: CAI18759.1. Z83839 , AL022321, Z74021, Z80998, Z83849 Genomic DNA. Translation: CAB06087.1. Z83849 , AL022321, Z74021, Z80998, Z83839 Genomic DNA. Translation: CAI23589.1. CH471095 Genomic DNA. Translation: EAW60006.1.
IPI	IPI00010866. IPI01015369.
PIR	A33545.
RefSeq	NP_000334.1. NM_000343.3. NP_001243243.1. NM_001256314.1.
UniGene	Hs.1964.
3D structure databases
ProteinModelPortal	P13866.
ModBase	Search...
Protein-protein interaction databases
IntAct	P13866. 1 interaction.
STRING	9606.ENSP00000266088.
Protein family/group databases
TCDB	2.A.21.3.1. solute:sodium symporter (SSS) family.
PTM databases
PhosphoSite	P13866.
Polymorphism databases
DMDM	127803.
Proteomic databases
PaxDb	P13866.
PRIDE	P13866.
Protocols and materials databases
DNASU	6523.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000266088; ENSP00000266088; ENSG00000100170. ENST00000543737; ENSP00000444898; ENSG00000100170.
GeneID	6523.
KEGG	hsa:6523.
UCSC	uc003amc.3. human.
Organism-specific databases
CTD	6523.
GeneCards	GC22P032439.
HGNC	HGNC:11036. SLC5A1.
HPA	CAB015467.
MIM	182380. gene. 606824. phenotype.
neXtProt	NX_P13866.
Orphanet	35710. Glucose-galactose malabsorption.
PharmGKB	PA308.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG4146.
HOVERGEN	HBG052859.
InParanoid	P13866.
KO	K14158.
OMA	EHNGDAL.
OrthoDB	EOG4B5P4V.
PhylomeDB	P13866.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism. REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
ArrayExpress	P13866.
Bgee	P13866.
CleanEx	HS_SLC5A1.
Genevestigator	P13866.
GermOnline	ENSG00000100170. Homo sapiens.
Family and domain databases
InterPro	IPR001734. Na/solute_symporter. IPR018212. Na/solute_symporter_CS. IPR019900. Na/solute_symporter_subgr. [Graphical view]
PANTHER	PTHR11819. PTHR11819. 1 hit.
Pfam	PF00474. SSF. 1 hit. [Graphical view]
TIGRFAMs	TIGR00813. sss. 1 hit.
PROSITE	PS00456. NA_SOLUT_SYMP_1. 1 hit. PS00457. NA_SOLUT_SYMP_2. 1 hit. PS50283. NA_SOLUT_SYMP_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P13866.
ChEMBL	CHEMBL4979.
GenomeRNAi	6523.
NextBio	25375.
SOURCE	Search...

Entry information

Entry name

SC5A1_HUMAN

Accession

Primary (citable) accession number: P13866
Secondary accession number(s): B2R7E2, B7Z4Q9, B7ZA69

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	May 1, 2013
This is version 138 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.