ID G1TGI6_RABIT Unreviewed; 297 AA. AC G1TGI6; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAR-2024, entry version 73. DE RecName: Full=Small ribosomal subunit protein uS2 {ECO:0000256|HAMAP-Rule:MF_03016}; DE AltName: Full=37 kDa laminin receptor precursor {ECO:0000256|HAMAP-Rule:MF_03016}; DE Short=37LRP {ECO:0000256|HAMAP-Rule:MF_03016}; DE AltName: Full=37/67 kDa laminin receptor {ECO:0000256|HAMAP-Rule:MF_03016}; DE Short=LRP/LR {ECO:0000256|HAMAP-Rule:MF_03016}; DE AltName: Full=67 kDa laminin receptor {ECO:0000256|HAMAP-Rule:MF_03016}; DE Short=67LR {ECO:0000256|HAMAP-Rule:MF_03016}; DE AltName: Full=Laminin receptor 1 {ECO:0000256|HAMAP-Rule:MF_03016}; DE Short=LamR {ECO:0000256|HAMAP-Rule:MF_03016}; DE AltName: Full=Laminin-binding protein precursor p40 {ECO:0000256|HAMAP-Rule:MF_03016}; DE Short=LBP/p40 {ECO:0000256|HAMAP-Rule:MF_03016}; GN Name=RPSA {ECO:0000256|HAMAP-Rule:MF_03016}; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000016036.1, ECO:0000313|Proteomes:UP000001811}; RN [1] {ECO:0000313|Ensembl:ENSOCUP00000016036.1, ECO:0000313|Proteomes:UP000001811} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000016036.1, RC ECO:0000313|Proteomes:UP000001811}; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S., RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B., RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J., RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M., RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M., RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D., RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J., RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S., RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A., RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R., RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R., RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C., RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E., RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N., RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0007829|PDB:4KZX, ECO:0007829|PDB:4KZY} RP X-RAY CRYSTALLOGRAPHY (7.01 ANGSTROMS) OF 14-297. RX PubMed=23873042; DOI=10.1038/nature12355; RA Lomakin I.B., Steitz T.A.; RT "The initiation of mammalian protein synthesis and mRNA scanning RT mechanism."; RL Nature 500:307-311(2013). RN [3] {ECO:0000313|Ensembl:ENSOCUP00000016036.1} RP IDENTIFICATION. RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000016036.1}; RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- FUNCTION: Required for the assembly and/or stability of the 40S CC ribosomal subunit. Required for the processing of the 20S rRNA- CC precursor to mature 18S rRNA in a late step of the maturation of 40S CC ribosomal subunits. Also functions as a cell surface receptor for CC laminin. Plays a role in cell adhesion to the basement membrane and in CC the consequent activation of signaling transduction pathways. May play CC a role in cell fate determination and tissue morphogenesis. Also acts CC as a receptor for several other ligands, including the pathogenic prion CC protein, viruses, and bacteria. Acts as a PPP1R16B-dependent substrate CC of PPP1CA. {ECO:0000256|HAMAP-Rule:MF_03016}. CC -!- SUBUNIT: Monomer (37LRP) and homodimer (67LR). Component of the small CC ribosomal subunit. Mature ribosomes consist of a small (40S) and a CC large (60S) subunit. The 40S subunit contains about 33 different CC proteins and 1 molecule of RNA (18S). The 60S subunit contains about 49 CC different proteins and 3 molecules of RNA (28S, 5.8S and 5S). Interacts CC with RPS21. Interacts with several laminins including at least LAMB1. CC Interacts with MDK. The mature dimeric form interacts with PPP1R16B CC (via its fourth ankyrin repeat). Interacts with PPP1CA only in the CC presence of PPP1R16B. {ECO:0000256|HAMAP-Rule:MF_03016}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_03016}. CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|HAMAP- CC Rule:MF_03016}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03016}. Note=67LR is CC found at the surface of the plasma membrane, with its C-terminal CC laminin-binding domain accessible to extracellular ligands. 37LRP is CC found at the cell surface, in the cytoplasm and in the nucleus. Co- CC localizes with PPP1R16B in the cell membrane. {ECO:0000256|HAMAP- CC Rule:MF_03016}. CC -!- PTM: Acylated. Acylation may be a prerequisite for conversion of the CC monomeric 37 kDa laminin receptor precursor (37LRP) to the mature CC dimeric 67 kDa laminin receptor (67LR), and may provide a mechanism for CC membrane association. {ECO:0000256|HAMAP-Rule:MF_03016}. CC -!- PTM: Cleaved by stromelysin-3 (ST3) at the cell surface. Cleavage by CC stromelysin-3 may be a mechanism to alter cell-extracellular matrix CC interactions. {ECO:0000256|HAMAP-Rule:MF_03016}. CC -!- MISCELLANEOUS: This protein appears to have acquired a second function CC as a laminin receptor specifically in the vertebrate lineage. CC {ECO:0000256|HAMAP-Rule:MF_03016}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family. CC {ECO:0000256|ARBA:ARBA00006242, ECO:0000256|HAMAP-Rule:MF_03016, CC ECO:0000256|RuleBase:RU003631}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03016}. 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; AAGW02051613; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PDB; 4KZX; X-ray; 7.81 A; A=14-297. DR PDB; 4KZY; X-ray; 7.01 A; A=14-297. DR PDB; 4KZZ; X-ray; 7.03 A; A=14-297. DR PDBsum; 4KZX; -. DR PDBsum; 4KZY; -. DR PDBsum; 4KZZ; -. DR AlphaFoldDB; G1TGI6; -. DR SMR; G1TGI6; -. DR STRING; 9986.ENSOCUP00000016036; -. DR PaxDb; 9986-ENSOCUP00000016036; -. DR Ensembl; ENSOCUT00000027846.1; ENSOCUP00000016036.1; ENSOCUG00000022961.1. DR eggNOG; KOG0830; Eukaryota. DR GeneTree; ENSGT00950000183099; -. DR HOGENOM; CLU_058171_1_0_1; -. DR InParanoid; G1TGI6; -. DR OMA; QCHLGAK; -. DR TreeFam; TF300100; -. DR Proteomes; UP000001811; Chromosome 8. DR Bgee; ENSOCUG00000022961; Expressed in uterus and 15 other cell types or tissues. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:UniProtKB-UniRule. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043236; F:laminin binding; IEA:UniProtKB-UniRule. DR GO; GO:0005055; F:laminin receptor activity; IEA:UniProtKB-UniRule. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:UniProtKB-UniRule. DR GO; GO:0000028; P:ribosomal small subunit assembly; IEA:UniProtKB-UniRule. DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule. DR CDD; cd01425; RPS2; 1. DR HAMAP; MF_03015; Ribosomal_S2_euk; 1. DR HAMAP; MF_03016; Ribosomal_S2_laminin_receptor; 1. DR InterPro; IPR001865; Ribosomal_uS2. DR InterPro; IPR032281; Ribosomal_uS2_C. DR InterPro; IPR018130; Ribosomal_uS2_CS. DR InterPro; IPR027498; Ribosomal_uS2_euk. DR InterPro; IPR005707; Ribosomal_uS2_euk/arc. DR InterPro; IPR023591; Ribosomal_uS2_flav_dom_sf. DR InterPro; IPR027504; Ribosomal_uS2_vert. DR NCBIfam; TIGR01012; uS2_euk_arch; 1. DR PANTHER; PTHR11489; 40S RIBOSOMAL PROTEIN SA; 1. DR PANTHER; PTHR11489:SF32; 40S RIBOSOMAL PROTEIN SA-RELATED; 1. DR Pfam; PF16122; 40S_SA_C; 1. DR Pfam; PF00318; Ribosomal_S2; 2. DR PRINTS; PR00395; RIBOSOMALS2. DR SUPFAM; SSF52313; Ribosomal protein S2; 1. DR PROSITE; PS00962; RIBOSOMAL_S2_1; 1. DR PROSITE; PS00963; RIBOSOMAL_S2_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4KZX, ECO:0007829|PDB:4KZY}; KW Acetylation {ECO:0000256|ARBA:ARBA00022990}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_03016}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03016}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03016}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03016}; KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|HAMAP-Rule:MF_03016}; KW Reference proteome {ECO:0000313|Proteomes:UP000001811}; KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_03016}; KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP- KW Rule:MF_03016}; KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP- KW Rule:MF_03016}. FT DOMAIN 204..297 FT /note="Small ribosomal subunit protein uS2 C-terminal" FT /evidence="ECO:0000259|Pfam:PF16122" FT REPEAT 232..234 FT /note="[DE]-W-[ST] 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03016" FT REPEAT 249..251 FT /note="[DE]-W-[ST] 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03016" FT REPEAT 268..270 FT /note="[DE]-W-[ST] 3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03016" FT REPEAT 277..279 FT /note="[DE]-W-[ST] 4" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03016" FT REPEAT 295..297 FT /note="[DE]-W-[ST] 5" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03016" FT REGION 56..115 FT /note="Interaction with PPP1R16B" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03016" FT REGION 163..182 FT /note="Laminin-binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03016" FT REGION 207..231 FT /note="Laminin-binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03016" FT REGION 244..297 FT /note="Laminin-binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03016" FT REGION 268..297 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 117..118 FT /note="Cleavage; by ST3; site 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03016" FT SITE 135..136 FT /note="Cleavage; by ST3; site 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03016" SQ SEQUENCE 297 AA; 33136 MW; EF920874A51CE435 CRC64; HNPGLPAQIR SKLEEDVLKF LAAGTHLGGT NLDFQMEQYI YKRKSDGIYI INLKRTWEKL LLAARAIVAI ENPADVSVIS SRNTGQRAVL KFAAATGATP IAGRFTPGTF TNQIQAAFRE PRLLVVTDPR ADHQPLTEAS YVNLPTIALC NTDSPLRYVD IAIPCNNKGA HSVGLMWWML AREVLRMRGT ISREHPWEVM PDLYFYRDPE EIEKEEQAAA EKAVTKEEFQ GEWTAPAPEF TATQPEVADW SEGVQVPSVP IQQFPTEDWS AQPATEDWSA APTAQATEWV GTTTEWS //