ID   TINAL_MOUSE             Reviewed;         466 AA.
AC   Q99JR5; Q9EQT9;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 161.
DE   RecName: Full=Tubulointerstitial nephritis antigen-like;
DE   AltName: Full=Adrenocortical zonation factor 1;
DE            Short=AZ-1;
DE   AltName: Full=Androgen-regulated gene 1 protein;
DE   AltName: Full=Tubulointerstitial nephritis antigen-related protein;
DE            Short=TARP;
DE   Flags: Precursor;
GN   Name=Tinagl1; Synonyms=Arg1, Lcn7, Tinagl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND TISSUE SPECIFICITY.
RX   PubMed=11377975; DOI=10.1016/s0960-0760(01)00039-5;
RA   Kobayashi M., Kinouchi T., Hakamata Y., Kamiakito T., Kuriki K., Suzuki K.,
RA   Tokue A., Fukayama M., Tanaka A.;
RT   "Isolation of an androgen-inducible novel lipocalin gene, Arg1, from
RT   androgen-dependent mouse mammary Shionogi carcinoma cells.";
RL   J. Steroid Biochem. Mol. Biol. 77:109-115(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND FUNCTION.
RC   TISSUE=Adrenal cortex;
RX   PubMed=12600995; DOI=10.1074/jbc.m301477200;
RA   Mukai K., Mitani F., Nagasawa H., Suzuki R., Suzuki T., Suematsu M.,
RA   Ishimura Y.;
RT   "An inverse correlation between expression of a preprocathepsin B-related
RT   protein with cysteine-rich sequences and steroid 11beta - hydroxylase in
RT   adrenocortical cells.";
RL   J. Biol. Chem. 278:17084-17092(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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).
CC   -!- FUNCTION: May be implicated in the adrenocortical zonation and in
CC       mechanisms for repressing the CYP11B1 gene expression in adrenocortical
CC       cells. This is a non catalytic peptidase C1 family protein.
CC       {ECO:0000269|PubMed:12600995}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Highly expressed in kidney, heart and
CC       adrenocortical cells of adrenal glands. Moderately expressed in spleen
CC       and liver. Also found in prostate, seminal vesicle, epididymis and
CC       testis in male reproductive organs. In adrenal glands is found in the
CC       outer cortical regions corresponding to the zona glomerulosa (zG) and
CC       the undifferentiated cell zone (zU) (at protein level).
CC       {ECO:0000269|PubMed:11377975, ECO:0000269|PubMed:12600995}.
CC   -!- INDUCTION: Down-regulated in prostate after castration.
CC       {ECO:0000269|PubMed:11377975}.
CC   -!- PTM: Glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10089}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB20596.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB047402; BAB20596.1; ALT_SEQ; mRNA.
DR   EMBL; AB050626; BAC76038.1; -; mRNA.
DR   EMBL; BC005738; AAH05738.1; -; mRNA.
DR   EMBL; BC018539; AAH18539.1; -; mRNA.
DR   CCDS; CCDS18708.2; -.
DR   RefSeq; NP_001161805.1; NM_001168333.1.
DR   RefSeq; NP_075965.2; NM_023476.3.
DR   AlphaFoldDB; Q99JR5; -.
DR   SMR; Q99JR5; -.
DR   BioGRID; 220489; 3.
DR   STRING; 10090.ENSMUSP00000101620; -.
DR   MEROPS; C01.975; -.
DR   GlyCosmos; Q99JR5; 2 sites, No reported glycans.
DR   GlyGen; Q99JR5; 2 sites.
DR   PhosphoSitePlus; Q99JR5; -.
DR   SwissPalm; Q99JR5; -.
DR   MaxQB; Q99JR5; -.
DR   PaxDb; 10090-ENSMUSP00000101620; -.
DR   PeptideAtlas; Q99JR5; -.
DR   ProteomicsDB; 259103; -.
DR   Pumba; Q99JR5; -.
DR   Antibodypedia; 31121; 213 antibodies from 26 providers.
DR   DNASU; 94242; -.
DR   Ensembl; ENSMUST00000030560.9; ENSMUSP00000030560.3; ENSMUSG00000028776.15.
DR   Ensembl; ENSMUST00000105998.8; ENSMUSP00000101620.2; ENSMUSG00000028776.15.
DR   Ensembl; ENSMUST00000105999.9; ENSMUSP00000101621.3; ENSMUSG00000028776.15.
DR   GeneID; 94242; -.
DR   KEGG; mmu:94242; -.
DR   UCSC; uc008uyz.2; mouse.
DR   AGR; MGI:2137617; -.
DR   CTD; 64129; -.
DR   MGI; MGI:2137617; Tinagl1.
DR   VEuPathDB; HostDB:ENSMUSG00000028776; -.
DR   eggNOG; KOG1544; Eukaryota.
DR   GeneTree; ENSGT00940000160023; -.
DR   InParanoid; Q99JR5; -.
DR   OMA; AEIYHSG; -.
DR   OrthoDB; 808912at2759; -.
DR   PhylomeDB; Q99JR5; -.
DR   TreeFam; TF313765; -.
DR   BioGRID-ORCS; 94242; 3 hits in 81 CRISPR screens.
DR   ChiTaRS; Tinagl1; mouse.
DR   PRO; PR:Q99JR5; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q99JR5; Protein.
DR   Bgee; ENSMUSG00000028776; Expressed in placenta labyrinth and 199 other cell types or tissues.
DR   ExpressionAtlas; Q99JR5; baseline and differential.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0043236; F:laminin binding; IPI:MGI.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd02620; Peptidase_C1A_CathepsinB; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR001212; Somatomedin_B_dom.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR   PANTHER; PTHR12411:SF270; TUBULOINTERSTITIAL NEPHRITIS ANTIGEN-LIKE; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00524; SMB_1; 1.
DR   PROSITE; PS50958; SMB_2; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
DR   Genevisible; Q99JR5; MM.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..466
FT                   /note="Tubulointerstitial nephritis antigen-like"
FT                   /id="PRO_0000026483"
FT   DOMAIN          49..96
FT                   /note="SMB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        160
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        53..72
FT                   /note="Alternate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT   DISULFID        70..84
FT                   /note="Alternate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT   DISULFID        70..72
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT   DISULFID        76..83
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT   DISULFID        84..91
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
SQ   SEQUENCE   466 AA;  52665 MW;  D12ABDCC8F63F36D CRC64;
     MWGCWLGLLL LLLAGQAALE ARRSRWRREL APGLHLRGIR DAGGRYCQEQ DMCCRGRADE
     CALPYLGATC YCDLFCNRTV SDCCPDFWDF CLGIPPPFPP VQGCMHGGRI YPVFGTYWDN
     CNRCTCHEGG HWECDQEPCL VDPDMIKAIN RGNYGWQAGN HSAFWGMTLD EGIRYRLGTI
     RPSSTVMNMN EIYTVLGQGE VLPTAFEASE KWPNLIHEPL DQGNCAGSWA FSTAAVASDR
     VSIHSLGHMT PILSPQNLLS CDTHHQQGCR GGRLDGAWWF LRRRGVVSDN CYPFSGREQN
     EASPTPRCMM HSRAMGRGKR QATSRCPNGQ VDSNDIYQVT PAYRLGSDEK EIMKELMENG
     PVQALMEVHE DFFLYQRGIY SHTPVSQGRP EQYRRHGTHS VKITGWGEET LPDGRTIKYW
     TAANSWGPWW GERGHFRIVR GTNECDIETF VLGVWGRVGM EDMGHH
//