ID TINAG_HUMAN Reviewed; 476 AA. AC Q9UJW2; Q9UJW1; Q9ULZ4; DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 23-JAN-2007, entry version 51. DE Tubulointerstitial nephritis antigen (TIN-Ag). GN Name=TINAG; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Kidney; RX MEDLINE=20119130; PubMed=10652240; DOI=10.1006/bbrc.2000.2103; RA Ikeda M., Takemura T., Hino S., Yoshioka K.; RT "Molecular cloning, expression, and chromosomal localization of a RT human tubulointerstitial nephritis antigen."; RL Biochem. Biophys. Res. Commun. 268:225-230(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND RP SUBCELLULAR LOCATION. RC TISSUE=Kidney; RX MEDLINE=20214190; PubMed=10752525; RA Zhou B., Nelson T.R., Kashtan C., Gleason B., Michael A.F., Vlassi M., RA Charonis A.S.; RT "Identification of two alternatively spliced forms of human RT tubulointerstitial nephritis antigen (TIN-Ag)."; RL J. Am. Soc. Nephrol. 11:658-668(2000). RN [3] RP IDENTIFICATION, AND DISEASE. RC TISSUE=Kidney; RX MEDLINE=87199690; PubMed=3553704; RA Fliger F.D., Wieslander J., Brentjens J.R., Andres G.A., RA Butkowski R.J.; RT "Identification of a target antigen in human anti-tubular basement RT membrane nephritis."; RL Kidney Int. 31:800-807(1987). RN [4] RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX MEDLINE=92106641; PubMed=1762287; RA Butkowski R.J., Kleppel M.M., Katz A., Michael A.F., Fish A.J.; RT "Distribution of tubulointerstitial nephritis antigen and evidence for RT multiple forms."; RL Kidney Int. 40:838-846(1991). RN [5] RP DISEASE. RX MEDLINE=93103006; PubMed=1466368; DOI=10.1016/0002-9343(92)90205-P; RA Katz A., Fish A.J., Santamaria P., Nevins T.E., Kim Y., RA Butkowski R.J.; RT "Role of antibodies to tubulointerstitial nephritis antigen in human RT anti-tubular basement membrane nephritis associated with membranous RT nephropathy."; RL Am. J. Med. 93:691-698(1992). RN [6] RP FUNCTION. RX MEDLINE=96366847; PubMed=8770961; RA Chen Y., Krishnamurti U., Wayner E.A., Michael A.F., Charonis A.S.; RT "Receptors in proximal tubular epithelial cells for tubulointerstitial RT nephritis antigen."; RL Kidney Int. 49:153-157(1996). RN [7] RP DEVELOPMENTAL STAGE. RX MEDLINE=98305799; PubMed=9643646; RA Nelson T.R., Kim Y., Michael A.F., Butkowski R.J., Charonis A.S.; RT "Tubulointerstitial nephritis antigen (TIN-ag) is expressed in RT distinct segments of the developing human nephron."; RL Connect. Tissue Res. 37:53-60(1998). CC -!- FUNCTION: Mediates adhesion of proximal tubule epithelial cells CC via integrins alpha3-beta1 and alphaV-beta3. CC -!- SUBCELLULAR LOCATION: Secreted protein; extracellular space; CC extracellular matrix; basement membrane. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=TIN1; CC IsoId=Q9UJW2-1; Sequence=Displayed; CC Note=Major isoform; CC Name=2; Synonyms=TIN2; CC IsoId=Q9UJW2-2; Sequence=VSP_050567, VSP_050568; CC -!- TISSUE SPECIFICITY: Expressed in the kidney cortex, small CC intestine and cornea. CC -!- DEVELOPMENTAL STAGE: Initially observed in the Bowman capsule CC during early glomerular capillary loop formation in the kidney. In CC more developmentally mature glomeruli, following transition from CC early to mid-capillary loop stage, expression is higher in the CC proximal tubular basement membrane than in the distal basement CC membrane and Bowman capsule. CC -!- PTM: It has been suggested that the active SMB domain may be CC permitted considerable disulfide bond heterogeneity or CC variability, thus 2 alternate disulfide patterns based on 3D CC structures are described with 1 disulfide bond conserved in both. CC -!- DISEASE: Antibodies against TINAG are found in sera of patients CC with tubulointerstitial nephritis, a rare autoimmune disorder that CC causes acute and chronic renal injury. CC -!- SIMILARITY: Belongs to the peptidase C1 family. CC -!- SIMILARITY: Contains 1 SMB (somatomedin B) domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB022277; BAA84949.1; -; mRNA. DR EMBL; AF195116; AAF08931.1; -; mRNA. DR EMBL; AF195117; AAF08932.1; -; mRNA. DR PIR; JC7189; JC7189. DR HSSP; P53634; 1K3B. DR MEROPS; C01.973; -. DR Ensembl; ENSG00000137251; Homo sapiens. DR KEGG; hsa:27283; -. DR HGNC; HGNC:14599; TINAG. DR MIM; 606749; gene. DR ArrayExpress; Q9UJW2; -. DR GermOnline; ENSG00000137251; Homo sapiens. DR RZPD-ProtExp; IOH40800; -. DR RZPD-ProtExp; W0583; -. DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:ProtInc. DR GO; GO:0000166; F:nucleotide binding; TAS:ProtInc. DR GO; GO:0005515; F:protein binding; IDA:UniProtKB. DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB. DR GO; GO:0007443; P:Malpighian tubule morphogenesis; TAS:ProtInc. DR InterPro; IPR013128; Peptidase_C1A. DR InterPro; IPR000668; Peptidase_C1A_C. DR InterPro; IPR009041; Prot_inh_PMP_SGC. DR InterPro; IPR001212; Somatomedin_B. DR PANTHER; PTHR12411; Peptidase_C1; 3. DR Pfam; PF00112; Peptidase_C1; 1. DR ProDom; PD000158; Peptidase_C1; 1. DR SMART; SM00645; Pept_C1; 1. DR SMART; SM00201; SO; 1. DR PROSITE; PS00524; SMB_1; 1. DR PROSITE; PS50958; SMB_2; 1. KW Alternative splicing; Basement membrane; Cell adhesion; KW Extracellular matrix; Glycoprotein. FT CHAIN 1 476 Tubulointerstitial nephritis antigen. FT /FTId=PRO_0000050600. FT DOMAIN 59 107 SMB. FT SITE 49 50 Cleavage (by furin) (Potential). FT CARBOHYD 38 38 N-linked (GlcNAc...) (Potential). FT CARBOHYD 175 175 N-linked (GlcNAc...) (Potential). FT CARBOHYD 314 314 N-linked (GlcNAc...) (Potential). FT CARBOHYD 360 360 N-linked (GlcNAc...) (Potential). FT CARBOHYD 455 455 N-linked (GlcNAc...) (Potential). FT DISULFID 63 70 Alternate (By similarity). FT DISULFID 70 102 Alternate (By similarity). FT DISULFID 81 95 Alternate (By similarity). FT DISULFID 81 83 Alternate (By similarity). FT DISULFID 87 94 By similarity. FT DISULFID 95 102 Alternate (By similarity). FT VAR_SEQ 119 169 Missing (in isoform 2). FT /FTId=VSP_050567. FT VAR_SEQ 209 300 Missing (in isoform 2). FT /FTId=VSP_050568. FT CONFLICT 7 8 FS -> IL (in Ref. 1). FT CONFLICT 175 175 N -> I (in Ref. 2; AAF08932). FT CONFLICT 199 199 P -> L (in Ref. 1). FT CONFLICT 333 333 D -> H (in Ref. 1). FT CONFLICT 381 381 R -> H (in Ref. 1). FT CONFLICT 421 421 L -> R (in Ref. 2; AAF08932). FT CONFLICT 437 437 F -> S (in Ref. 1). FT CONFLICT 463 463 V -> I (in Ref. 1). SQ SEQUENCE 476 AA; 54646 MW; 32DE88E3083C3077 CRC64; MWTGYKFSIF SYLTTEIWME KQYLSQREVD LEAYFTRNHT VLQGTRFKRA IFQGQYCRNF GCCEDRDDGC VTEFYAANAL CYCDKFCDRE NSDCCPDYKS FCREEKEWPP HTQPWYPEGC FKDGQHYEEG SVIKENCNSC TCSGQQWKCS QHVCLVRPEL IEQVNKGDYG WTAQNYSQFW GMTLEDGFKF RLGTLPPSPM LLSMNEMTAS LPATTDLPEF FVASYKWPGW THGPLDQKNC AASWAFSTAS VAADRIAIQS KGRYTANLSP QNLISCCAKN RHGCNSGSID RAWWYLRKRG LVSHACYPLF KDQNATNNGC AMASRSDGRG KRDATKPCPN NVEKSNRIYQ CSPPYRVSSN ETEIMKEIMQ NGPVQAIMQV REDFFHYKTG IYRHVTSTNK ESEKYRKLQT HAVKLTGWGT LRGAQGQKEK FWIAANFWGK SWGENGYFRI LRGVNESDIE KLVIAAWGQL TSSDEP //