LRC32_PONAB
ID LRC32_PONAB Reviewed; 662 AA.
AC Q5RF01;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Transforming growth factor beta activator LRRC32 {ECO:0000250|UniProtKB:Q14392};
DE AltName: Full=Leucine-rich repeat-containing protein 32 {ECO:0000250|UniProtKB:Q14392};
DE Flags: Precursor;
GN Name=LRRC32 {ECO:0000250|UniProtKB:Q14392};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Key regulator of transforming growth factor beta (TGFB1,
CC TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in
CC a latent state during storage in extracellular space. Associates
CC specifically via disulfide bonds with the Latency-associated peptide
CC (LAP), which is the regulatory chain of TGF-beta, and regulates
CC integrin-dependent activation of TGF-beta (By similarity). Able to
CC outcompete LTBP1 for binding to LAP regulatory chain of TGF-beta (By
CC similarity). Controls activation of TGF-beta-1 (TGFB1) on the surface
CC of activated regulatory T-cells (Tregs). Required for epithelial fusion
CC during palate development by regulating activation of TGF-beta-3
CC (TGFB3) (By similarity). {ECO:0000250|UniProtKB:G3XA59,
CC ECO:0000250|UniProtKB:Q14392}.
CC -!- SUBUNIT: Interacts with TGFB1; associates via disulfide bonds with the
CC Latency-associated peptide chain (LAP) regulatory chain of TGFB1,
CC leading to regulate activation of TGF-beta-1. Interacts with TGFB2 (By
CC similarity). Interacts with TGFB3; associates via disulfide bonds with
CC the Latency-associated peptide chain (LAP) regulatory chain of TGFB3,
CC leading to regulate activation of TGF-beta-3 (By similarity). Interacts
CC with LAPTM4B; decreases TGFB1 production in regulatory T-cells (By
CC similarity). {ECO:0000250|UniProtKB:G3XA59,
CC ECO:0000250|UniProtKB:Q14392}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14392};
CC Single-pass type I membrane protein {ECO:0000255}. Cell surface
CC {ECO:0000250|UniProtKB:Q14392}.
CC -!- SIMILARITY: Belongs to the LRRC32/LRRC33 family. {ECO:0000305}.
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DR EMBL; CR857361; CAH89656.1; -; mRNA.
DR RefSeq; NP_001124746.1; NM_001131274.1.
DR AlphaFoldDB; Q5RF01; -.
DR SMR; Q5RF01; -.
DR STRING; 9601.ENSPPYP00000004228; -.
DR Ensembl; ENSPPYT00000004400; ENSPPYP00000004228; ENSPPYG00000003700.
DR GeneID; 100171595; -.
DR KEGG; pon:100171595; -.
DR CTD; 2615; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000162288; -.
DR HOGENOM; CLU_024194_1_0_1; -.
DR InParanoid; Q5RF01; -.
DR OrthoDB; 826997at2759; -.
DR Proteomes; UP000001595; Chromosome 11.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050431; F:transforming growth factor beta binding; ISS:UniProtKB.
DR GO; GO:0046007; P:negative regulation of activated T cell proliferation; IEA:Ensembl.
DR GO; GO:0001818; P:negative regulation of cytokine production; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:1901388; P:regulation of transforming growth factor beta activation; ISS:UniProtKB.
DR GO; GO:1901398; P:regulation of transforming growth factor beta3 activation; IEA:Ensembl.
DR GO; GO:0062009; P:secondary palate development; ISS:UniProtKB.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF13855; LRR_8; 4.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00369; LRR_TYP; 14.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 20.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Growth factor binding;
KW Leucine-rich repeat; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..662
FT /note="Transforming growth factor beta activator LRRC32"
FT /id="PRO_0000042588"
FT TOPO_DOM 18..625
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 626..646
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 647..662
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..48
FT /note="LRRNT"
FT /evidence="ECO:0000255"
FT REPEAT 50..73
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 74..95
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 98..119
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 125..145
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 150..171
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 174..195
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 198..219
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 220..240
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 244..265
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 266..286
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 316..339
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 340..361
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 364..385
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 387..408
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 411..432
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 444..465
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 467..488
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 492..513
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 515..536
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 537..558
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT DOMAIN 571..620
FT /note="LRRCT"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 211
FT /note="Interchain (with C-33 in TGFB1); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q14392"
FT DISULFID 350
FT /note="Interchain (with C-33 in TGFB1); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q14392"
SQ SEQUENCE 662 AA; 72112 MW; 9D9753F9680C1F0A CRC64;
MRPQILLLLA LLTLGLAAQR QDKVPCKMVD KKVSCQGLGL LQVPSVLPPD TETLDLSGNQ
LRSILASPLG FYTALRHLDL STNEISFLQP GAFQALTHLE HLSLAHNRLA MATALSAGGL
GPLPRVTSLD LSGNSLYSGL LERLLGEAPS LHTLSLAENS LTRLTRHTFR DMPVLEQLDL
HSNVLMDIED GAFEGLPRLT HLNLSRNSLT CISDFSLQQL RVLDLSCNSI EAFQTASQPQ
AEFQLTWLDL RENKLLHFPD LAALPRLIYL NLSNNLIRLP TGPPQDSKGI HAPSEGWSAL
PLSTPSWNAS ARPLSQLLNL DLSYNEIELI PDSFLEHLTS LCFLNLSRNC LRTFEARRSG
SLPCLMLLDL SHNALETLEL GARALGSLRT LLLQGNALRD LPPYTFANLA SLQRLNLQGN
RVSPCGGPDE PGPSGCVAFS GITSLHSLSL VDNEIELLRA GAFLHTPLTE LDLSSNPGLE
VATGALGGLE ASLEVLALQG NGLTVLQVDL PCFICLKRLN LAENRLSHLP AWTQAVSLEV
LDLRNNSFSL LPGSAMGGLE TSLRRLYLQG NPLSCCGNGW LAAQLHQGRV DVDATQDLIC
RFSSQEEVSL SHVRPEDCEK GGLKNINLII ILTFILVSAI LLTTLATCCC VRRQKFNQQY
KA
