Q9UJW2 (TINAG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tubulointerstitial nephritis antigen
Short name=TIN-Ag

Gene names

Name:

TINAG

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	476 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Mediates adhesion of proximal tubule epithelial cells via integrins alpha3-beta1 and alphaV-beta3. This is a non catalytic peptidase C1 family protein. Ref.9
Subcellular location	Secreted › extracellular space › extracellular matrix › basement membrane Ref.2 Ref.7.
Tissue specificity	Expressed in the kidney cortex, small intestine and cornea. Ref.1 Ref.2 Ref.7
Developmental stage	Initially observed in the Bowman capsule during early glomerular capillary loop formation in the kidney. In more developmentally mature glomeruli, following transition from early to mid-capillary loop stage, expression is higher in the proximal tubular basement membrane than in the distal basement membrane and Bowman capsule. Ref.10
Post-translational modification	It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability, thus 2 alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both.
Miscellaneous	Antibodies against TINAG are found in sera of patients with tubulointerstitial nephritis, a rare autoimmune disorder that causes acute and chronic renal injury.
Sequence similarities	Belongs to the peptidase C1 family. Contains 1 SMB (somatomedin-B) domain.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Basement membrane Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from direct assay Ref.9. Source: UniProtKB immune response Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: InterPro
Cellular_component	basement membrane Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	cysteine-type endopeptidase activity Traceable author statement Ref.1. Source: ProtInc nucleotide binding Traceable author statement Ref.1. Source: ProtInc polysaccharide binding Inferred from electronic annotation. Source: InterPro scavenger receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q9UJW2-1)

Also known as: TIN1;

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.

Note: Major isoform.

Isoform 2 (identifier: Q9UJW2-2)

Also known as: TIN2;

The sequence of this isoform differs from the canonical sequence as follows:
     119-169: Missing.
     209-300: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 476	476	Tubulointerstitial nephritis antigen		PRO_0000050600
Regions
	Domain	59 – 107	49	SMB
Sites
	Site	49 – 50	2	Cleavage; by furin Potential Ref.2
Amino acid modifications
	Glycosylation	38	1	N-linked (GlcNAc...) Potential
	Glycosylation	175	1	N-linked (GlcNAc...) Potential
	Glycosylation	314	1	N-linked (GlcNAc...) Potential
	Glycosylation	360	1	N-linked (GlcNAc...) Potential
	Glycosylation	455	1	N-linked (GlcNAc...) Potential
	Disulfide bond	63 ↔ 70		Alternate By similarity
	Disulfide bond	70 ↔ 102		Alternate By similarity
	Disulfide bond	81 ↔ 95		Alternate By similarity
	Disulfide bond	81 ↔ 83		Alternate By similarity
	Disulfide bond	87 ↔ 94		By similarity
	Disulfide bond	95 ↔ 102		Alternate By similarity
Natural variations
	Alternative sequence	119 – 169	51	Missing in isoform 2. Ref.2		VSP_050567
	Alternative sequence	209 – 300	92	Missing in isoform 2. Ref.2		VSP_050568
	Natural variant	3	1	T → A. Corresponds to variant rs16885197 [ dbSNP | Ensembl ].		VAR_047091
	Natural variant	22	1	Q → R. Corresponds to variant rs2297980 [ dbSNP | Ensembl ].		VAR_047092
	Natural variant	158	1	S → P. Ref.1 Ref.2 Corresponds to variant rs1058768 [ dbSNP | Ensembl ].		VAR_047093
	Natural variant	413	1	V → I. Corresponds to variant rs34011963 [ dbSNP | Ensembl ].		VAR_047094
	Natural variant	433	1	I → L. Corresponds to variant rs3736352 [ dbSNP | Ensembl ].		VAR_047095
Experimental info
	Sequence conflict	7 – 8	2	IL → FS in AAF08931. Ref.2
	Sequence conflict	7 – 8	2	IL → FS in AAF08932. Ref.2
	Sequence conflict	175	1	N → I in AAF08932. Ref.2
	Sequence conflict	199	1	P → L in BAA84949. Ref.1
	Sequence conflict	333	1	H → D in AAF08931. Ref.2
	Sequence conflict	333	1	H → D in AAF08932. Ref.2
	Sequence conflict	381	1	R → H in BAA84949. Ref.1
	Sequence conflict	421	1	L → R in AAF08932. Ref.2
	Sequence conflict	437	1	S → F in AAF08931. Ref.2
	Sequence conflict	437	1	S → F in AAF08932. Ref.2
	Sequence conflict	463	1	I → V in AAF08931. Ref.2
	Sequence conflict	463	1	I → V in AAF08932. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (TIN1) [UniParc]. Last modified January 11, 2011. Version 3. Checksum: 6D90C734DAC3A5AE	FASTA	476	54,605
	10 20 30 40 50 60 MWTGYKILIF SYLTTEIWME KQYLSQREVD LEAYFTRNHT VLQGTRFKRA IFQGQYCRNF 70 80 90 100 110 120 GCCEDRDDGC VTEFYAANAL CYCDKFCDRE NSDCCPDYKS FCREEKEWPP HTQPWYPEGC 130 140 150 160 170 180 FKDGQHYEEG SVIKENCNSC TCSGQQWKCS QHVCLVRSEL IEQVNKGDYG WTAQNYSQFW 190 200 210 220 230 240 GMTLEDGFKF RLGTLPPSPM LLSMNEMTAS LPATTDLPEF FVASYKWPGW THGPLDQKNC 250 260 270 280 290 300 AASWAFSTAS VAADRIAIQS KGRYTANLSP QNLISCCAKN RHGCNSGSID RAWWYLRKRG 310 320 330 340 350 360 LVSHACYPLF KDQNATNNGC AMASRSDGRG KRHATKPCPN NVEKSNRIYQ CSPPYRVSSN 370 380 390 400 410 420 ETEIMKEIMQ NGPVQAIMQV REDFFHYKTG IYRHVTSTNK ESEKYRKLQT HAVKLTGWGT 430 440 450 460 470 LRGAQGQKEK FWIAANSWGK SWGENGYFRI LRGVNESDIE KLIIAAWGQL TSSDEP
	Isoform 2 (TIN2) [UniParc]. Checksum: E708C6B55D9DBF9A	FASTA	333	38,724
	10 20 30 40 50 60 MWTGYKILIF SYLTTEIWME KQYLSQREVD LEAYFTRNHT VLQGTRFKRA IFQGQYCRNF 70 80 90 100 110 120 GCCEDRDDGC VTEFYAANAL CYCDKFCDRE NSDCCPDYKS FCREEKEWPP HTQPWYPEGW 130 140 150 160 170 180 TAQNYSQFWG MTLEDGFKFR LGTLPPSPML LSMNEMTLVS HACYPLFKDQ NATNNGCAMA 190 200 210 220 230 240 SRSDGRGKRH ATKPCPNNVE KSNRIYQCSP PYRVSSNETE IMKEIMQNGP VQAIMQVRED 250 260 270 280 290 300 FFHYKTGIYR HVTSTNKESE KYRKLQTHAV KLTGWGTLRG AQGQKEKFWI AANSWGKSWG 310 320 330 ENGYFRILRG VNESDIEKLI IAAWGQLTSS DEP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, expression, and chromosomal localization of a human tubulointerstitial nephritis antigen." Ikeda M., Takemura T., Hino S., Yoshioka K. Biochem. Biophys. Res. Commun. 268:225-230(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT PRO-158. Tissue: Kidney.
[2]	"Identification of two alternatively spliced forms of human tubulointerstitial nephritis antigen (TIN-Ag)." Zhou B., Nelson T.R., Kashtan C., Gleason B., Michael A.F., Vlassi M., Charonis A.S. J. Am. Soc. Nephrol. 11:658-668(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT PRO-158. Tissue: Kidney.
[3]	"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] (ISOFORM 1). Tissue: Kidney.
[4]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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].
[6]	"Identification of a target antigen in human anti-tubular basement membrane nephritis." Fliger F.D., Wieslander J., Brentjens J.R., Andres G.A., Butkowski R.J. Kidney Int. 31:800-807(1987) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION, INVOLVEMENT IN TUBULOINTERSTITIAL NEPHRITIS. Tissue: Kidney.
[7]	"Distribution of tubulointerstitial nephritis antigen and evidence for multiple forms." Butkowski R.J., Kleppel M.M., Katz A., Michael A.F., Fish A.J. Kidney Int. 40:838-846(1991) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[8]	"Role of antibodies to tubulointerstitial nephritis antigen in human anti-tubular basement membrane nephritis associated with membranous nephropathy." Katz A., Fish A.J., Santamaria P., Nevins T.E., Kim Y., Butkowski R.J. Am. J. Med. 93:691-698(1992) [PubMed] [Europe PMC] [Abstract] Cited for: DISEASE.
[9]	"Receptors in proximal tubular epithelial cells for tubulointerstitial nephritis antigen." Chen Y., Krishnamurti U., Wayner E.A., Michael A.F., Charonis A.S. Kidney Int. 49:153-157(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"Tubulointerstitial nephritis antigen (TIN-ag) is expressed in distinct segments of the developing human nephron." Nelson T.R., Kim Y., Michael A.F., Butkowski R.J., Charonis A.S. Connect. Tissue Res. 37:53-60(1998) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB022277 mRNA. Translation: BAA84949.1. AF195116 mRNA. Translation: AAF08931.1. AF195117 mRNA. Translation: AAF08932.1. AK312918 mRNA. Translation: BAG35763.1. AL589946, AL359380 Genomic DNA. Translation: CAH70302.1. AL359380, AL589946 Genomic DNA. Translation: CAI16272.1. CH471081 Genomic DNA. Translation: EAX04437.1.
IPI	IPI00099386. IPI00478705.
PIR	JC7189.
RefSeq	NP_055279.3. NM_014464.3.
UniGene	Hs.127011.
3D structure databases
ProteinModelPortal	Q9UJW2.
SMR	Q9UJW2. Positions 216-466.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UJW2. 2 interactions.
STRING	9606.ENSP00000259782.
Protein family/group databases
MEROPS	C01.973.
PTM databases
PhosphoSite	Q9UJW2.
Polymorphism databases
DMDM	212276468.
Proteomic databases
PaxDb	Q9UJW2.
PRIDE	Q9UJW2.
Protocols and materials databases
DNASU	27283.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000259782; ENSP00000259782; ENSG00000137251.
GeneID	27283.
KEGG	hsa:27283.
UCSC	uc003pcj.2. human.
Organism-specific databases
CTD	27283.
GeneCards	GC06P054220.
H-InvDB	HIX0025004.
HGNC	HGNC:14599. TINAG.
HPA	HPA035427.
MIM	606749. gene.
neXtProt	NX_Q9UJW2.
PharmGKB	PA37905.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG310046.
HOGENOM	HOG000241342.
HOVERGEN	HBG053961.
InParanoid	Q9UJW2.
OMA	WGQLTSS.
PhylomeDB	Q9UJW2.
Gene expression databases
ArrayExpress	Q9UJW2.
Bgee	Q9UJW2.
CleanEx	HS_TINAG.
Genevestigator	Q9UJW2.
GermOnline	ENSG00000137251. Homo sapiens.
Family and domain databases
InterPro	IPR025661. Pept_asp_AS. IPR013128. Peptidase_C1A. IPR000668. Peptidase_C1A_C. IPR001212. Somatomedin_B_dom. [Graphical view]
PANTHER	PTHR12411. PTHR12411. 1 hit.
Pfam	PF00112. Peptidase_C1. 1 hit. PF01033. Somatomedin_B. 1 hit. [Graphical view]
SMART	SM00645. Pept_C1. 1 hit. SM00201. SO. 1 hit. [Graphical view]
PROSITE	PS00524. SMB_1. 1 hit. PS50958. SMB_2. 1 hit. PS00640. THIOL_PROTEASE_ASN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	27283.
NextBio	50212.
SOURCE	Search...

Entry information

Entry name

TINAG_HUMAN

Accession

Primary (citable) accession number: Q9UJW2
Secondary accession number(s): Q5T467, Q9UJW1, Q9ULZ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	January 11, 2011
Last modified:	May 1, 2013
This is version 106 of the entry and version 3 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.