SMA10_CAEEL
ID SMA10_CAEEL Reviewed; 881 AA.
AC Q965M2; H2L0D4;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Leucine-rich repeats and immunoglobulin-like domains protein sma-10 {ECO:0000305};
DE Flags: Precursor;
GN Name=sma-10 {ECO:0000312|WormBase:T21D12.9a};
GN ORFNames=T21D12.9 {ECO:0000312|WormBase:T21D12.9a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SMA-6 AND DAF-1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP LEU-102.
RX PubMed=20502686; DOI=10.1371/journal.pgen.1000963;
RA Gumienny T.L., Macneil L., Zimmerman C.M., Wang H., Chin L., Wrana J.L.,
RA Padgett R.W.;
RT "Caenorhabditis elegans SMA-10/LRIG is a conserved transmembrane protein
RT that enhances bone morphogenetic protein signaling.";
RL PLoS Genet. 6:E1000963-E1000963(2010).
CC -!- FUNCTION: Binds to the TGF-beta receptors sma-6 and daf-4, and enhances
CC TGF-beta signaling activity in vitro. Has a role in regulation of body
CC size. {ECO:0000269|PubMed:20502686}.
CC -!- SUBUNIT: Interacts with sma-6 and daf-1. {ECO:0000269|PubMed:20502686}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20502686};
CC Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle
CC membrane {ECO:0000305|PubMed:20502686}; Lipid-anchor, GPI-anchor
CC {ECO:0000305|PubMed:20502686}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:T21D12.9a};
CC IsoId=Q965M2-1; Sequence=Displayed;
CC Name=c {ECO:0000312|WormBase:T21D12.9c};
CC IsoId=Q965M2-2; Sequence=VSP_058387, VSP_058388;
CC -!- TISSUE SPECIFICITY: Expressed in the hypodermis.
CC {ECO:0000269|PubMed:20502686}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the pharynx from the embryonic stage
CC to adulthood. {ECO:0000269|PubMed:20502686}.
CC -!- DISRUPTION PHENOTYPE: Small body size phenotype.
CC {ECO:0000269|PubMed:20502686}.
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DR EMBL; BX284604; CCD72526.1; -; Genomic_DNA.
DR EMBL; BX284604; CCD72527.1; -; Genomic_DNA.
DR RefSeq; NP_499896.1; NM_067495.5. [Q965M2-1]
DR RefSeq; NP_499897.1; NM_067496.3.
DR AlphaFoldDB; Q965M2; -.
DR SMR; Q965M2; -.
DR STRING; 6239.T21D12.9a.2; -.
DR PaxDb; Q965M2; -.
DR EnsemblMetazoa; T21D12.9a.1; T21D12.9a.1; WBGene00020649. [Q965M2-1]
DR EnsemblMetazoa; T21D12.9a.2; T21D12.9a.2; WBGene00020649. [Q965M2-1]
DR EnsemblMetazoa; T21D12.9c.1; T21D12.9c.1; WBGene00020649. [Q965M2-2]
DR GeneID; 176849; -.
DR KEGG; cel:CELE_T21D12.9; -.
DR UCSC; T21D12.9c.1; c. elegans. [Q965M2-1]
DR CTD; 176849; -.
DR WormBase; T21D12.9a; CE28415; WBGene00020649; sma-10. [Q965M2-1]
DR WormBase; T21D12.9c; CE28417; WBGene00020649; sma-10. [Q965M2-2]
DR eggNOG; KOG4194; Eukaryota.
DR GeneTree; ENSGT00940000171544; -.
DR InParanoid; Q965M2; -.
DR OMA; EYSCELW; -.
DR OrthoDB; 161719at2759; -.
DR PhylomeDB; Q965M2; -.
DR PRO; PR:Q965M2; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00020649; Expressed in larva and 3 other tissues.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:WormBase.
DR GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IPI:WormBase.
DR GO; GO:0005114; F:type II transforming growth factor beta receptor binding; IPI:WormBase.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:WormBase.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IDA:WormBase.
DR GO; GO:0042661; P:regulation of mesodermal cell fate specification; IGI:UniProtKB.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IGI:WormBase.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
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; PF07679; I-set; 2.
DR Pfam; PF13855; LRR_8; 5.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00369; LRR_TYP; 13.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS51450; LRR; 16.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasmic vesicle; Disulfide bond;
KW Glycoprotein; GPI-anchor; Immunoglobulin domain; Leucine-rich repeat;
KW Lipoprotein; Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..881
FT /note="Leucine-rich repeats and immunoglobulin-like domains
FT protein sma-10"
FT /evidence="ECO:0000305"
FT /id="PRO_5004321473"
FT TOPO_DOM 21..840
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 841..861
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 862..881
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 24..50
FT /note="LRRNT"
FT REPEAT 51..74
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 75..98
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 99..122
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 124..145
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 146..169
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 170..193
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 195..217
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 218..241
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 242..265
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 267..289
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 290..313
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 314..337
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 339..361
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 362..388
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 390..413
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 415..437
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 440..465
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT DOMAIN 503..611
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 616..704
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 716..785
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 526..594
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 637..688
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 733..783
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 708..737
FT /note="NFFHYPESPDLSPMLIKKRDALKIDCSCDL -> LIYCSNSLSFTCLFSQTQ
FT VFRKLLPLPRKP (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_058387"
FT VAR_SEQ 738..881
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_058388"
FT MUTAGEN 102
FT /note="L->F: In wk26; small body phenotype."
FT /evidence="ECO:0000269|PubMed:20502686"
SQ SEQUENCE 881 AA; 99513 MW; 5854EDDA671E45C2 CRC64;
MIVYSLLLLI LYDFLPKVVT FDTVCIGLCH CVGNVVDCSS LDLSEIPTTI PNNTRILLLS
DNEIESIDKS RLKGFYFLQT LDISNNIIRH IDFEFFYNLP NLKILNIRKN RLARIPRGSH
ELGHLEKLDL RSNLISTVTS EELSYLAAVR SVDLSRNLIS YLPKPTTSAK VNIEKLDLAS
NSITDIGTDH FSSFNTLVTL KLARNHITTL NQFSFSRLRK LESLDLTRNM IREVRFLAFN
QLPSLQNVSL ARNDVYRLDD GMFYACEGLK HLNLSTNRVQ AVTEGWMFGL TSLEVLDLSY
NQIQSFHISS WSHTPKLKWL SLHSNRIQSL PSGSFRVLRQ LEELILSANS IDSLHKFALV
GMSSLHKLDL SSNTLAVCVE DGAVLYNTSM PFLRSLRFTN NQLRVIPKRA FERFPALEEL
DLTDNPIATI HPEAFEPLEL KRLVMNSSSI LCDCQISWLA SWIYRLKLDK SSIIAKCSYP
PPLADLYVVA IDTANLTCHN DSPRAKIVRQ PVEVSTLIGE KARFTCNVYG ASPLSIEWRV
MENGQPRVLV QDSATFLSIN RTAVVNGTFD ERELAAAELL LDNVAMTDNS EYQCVARNRF
GSDFSTHVKL QVYQAPKFTY TPEDMPLLVG QTAKFLCAAT GTPRPEIKWA FEQIPFPAAE
ARRLYVTPND DHIYIMNVTK EDQGAYTCHA TNVAGQTQAS ANLIVFENFF HYPESPDLSP
MLIKKRDALK IDCSCDLISS RQRMVWKRQQ QVILFLKKAK FSDNDQILTL TQTTFSDSGE
YSCELWVDDT ILMRKITMVK VVNEDEFVSS EATLTQRVQR IRAMASKLVD NIKSTGNGIY
LMASCSAFGL MILGVITSIC ICIAKCSCNQ NHVFNVLPVQ V
