SRBS1_CAEEL
ID SRBS1_CAEEL Reviewed; 1005 AA.
AC G5EC32; O62482;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Sorbin and SH3 domain-containing protein 1 homolog {ECO:0000305};
GN Name=sorb-1 {ECO:0000303|PubMed:28978740,
GN ECO:0000312|WormBase:Y45F10D.13a};
GN ORFNames=Y45F10D.13 {ECO:0000312|WormBase:Y45F10D.13a};
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 DEB-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 461-TRP--HIS-1005.
RX PubMed=28978740; DOI=10.1091/mbc.e16-06-0455;
RA Loveless T., Qadota H., Benian G.M., Hardin J.;
RT "Caenorhabditis elegans SORB-1 localizes to integrin adhesion sites and is
RT required for organization of sarcomeres and mitochondria in myocytes.";
RL Mol. Biol. Cell 28:3621-3633(2017).
CC -!- FUNCTION: Required for organization of sarcomeres in body wall muscles
CC and for maintaining normal mitochondrial position in myocytes.
CC {ECO:0000269|PubMed:28978740}.
CC -!- SUBUNIT: May interact with deb-1. {ECO:0000269|PubMed:28978740}.
CC -!- INTERACTION:
CC G5EC32; Q18605: athp-1; NbExp=4; IntAct=EBI-325337, EBI-331810;
CC G5EC32; B1Q247: B0507.3; NbExp=6; IntAct=EBI-325337, EBI-2316099;
CC G5EC32; O01481: C06A5.8; NbExp=8; IntAct=EBI-325337, EBI-2316191;
CC G5EC32; Q17865: C09G1.4; NbExp=5; IntAct=EBI-325337, EBI-317562;
CC G5EC32; G5EC89: ceh-17; NbExp=4; IntAct=EBI-325337, EBI-2316478;
CC G5EC32; Q17746: CELE_C06G3.6; NbExp=7; IntAct=EBI-325337, EBI-313792;
CC G5EC32; Q93231: CELE_C17E4.10; NbExp=5; IntAct=EBI-325337, EBI-326358;
CC G5EC32; Q966J6: CELE_F41B4.1; NbExp=7; IntAct=EBI-325337, EBI-327612;
CC G5EC32; O45522: CELE_F45B8.3; NbExp=3; IntAct=EBI-325337, EBI-326566;
CC G5EC32; Q20670: CELE_F52E10.4; NbExp=4; IntAct=EBI-325337, EBI-2316655;
CC G5EC32; Q22387: CELE_T11B7.1; NbExp=3; IntAct=EBI-325337, EBI-320525;
CC G5EC32; Q7JP75: cyk-1; NbExp=6; IntAct=EBI-325337, EBI-2003118;
CC G5EC32; O18195: ddl-2; NbExp=6; IntAct=EBI-325337, EBI-313368;
CC G5EC32; G5ED33: eps-8; NbExp=15; IntAct=EBI-325337, EBI-2315916;
CC G5EC32; Q9TYU9: exc-6; NbExp=4; IntAct=EBI-325337, EBI-2317613;
CC G5EC32; Q17744: F43B10.1; NbExp=6; IntAct=EBI-325337, EBI-2315966;
CC G5EC32; O16299: figl-1; NbExp=8; IntAct=EBI-325337, EBI-320880;
CC G5EC32; Q3Y407: grd-7; NbExp=4; IntAct=EBI-325337, EBI-2317687;
CC G5EC32; O45681: K10H10.4; NbExp=6; IntAct=EBI-325337, EBI-2316236;
CC G5EC32; P45962: klp-3; NbExp=3; IntAct=EBI-325337, EBI-311892;
CC G5EC32; O17583: lin-10; NbExp=6; IntAct=EBI-325337, EBI-313389;
CC G5EC32; Q9TYX9: M57.1; NbExp=10; IntAct=EBI-325337, EBI-2315745;
CC G5EC32; Q22002: mab-10; NbExp=4; IntAct=EBI-325337, EBI-2316177;
CC G5EC32; P34400: mig-10; NbExp=7; IntAct=EBI-325337, EBI-2315872;
CC G5EC32; Q03601: nhl-1; NbExp=7; IntAct=EBI-325337, EBI-314158;
CC G5EC32; Q95QA6: pat-12; NbExp=13; IntAct=EBI-325337, EBI-327642;
CC G5EC32; O62203: phm-2; NbExp=7; IntAct=EBI-325337, EBI-320780;
CC G5EC32; Q09442: sap-49; NbExp=16; IntAct=EBI-325337, EBI-2316106;
CC G5EC32; Q20010: sas-5; NbExp=3; IntAct=EBI-325337, EBI-327608;
CC G5EC32; Q19019: sli-1; NbExp=6; IntAct=EBI-325337, EBI-315356;
CC G5EC32; Q8MXU3: snn-1; NbExp=3; IntAct=EBI-325337, EBI-2316201;
CC G5EC32; Q1XFY2: tag-343; NbExp=3; IntAct=EBI-325337, EBI-2316564;
CC G5EC32; Q9U2Z0: ttx-1; NbExp=4; IntAct=EBI-325337, EBI-330989;
CC G5EC32; Q9XZI6: unc-11; NbExp=3; IntAct=EBI-325337, EBI-311866;
CC G5EC32; G5EDS1: vab-3; NbExp=14; IntAct=EBI-325337, EBI-319610;
CC G5EC32; Q17795: wsp-1; NbExp=12; IntAct=EBI-325337, EBI-2316131;
CC G5EC32; Q8MQE6: wsp-1; NbExp=5; IntAct=EBI-325337, EBI-2316008;
CC G5EC32; Q9XVK6: wve-1; NbExp=6; IntAct=EBI-325337, EBI-312105;
CC G5EC32; Q95Y58: Y50D4A.4; NbExp=4; IntAct=EBI-325337, EBI-2316345;
CC G5EC32; O02174: zfp-3; NbExp=4; IntAct=EBI-325337, EBI-2315779;
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000269|PubMed:28978740}. Cell membrane
CC {ECO:0000269|PubMed:28978740}. Cell junction, focal adhesion
CC {ECO:0000269|PubMed:28978740}. Note=Localizes to adhesion plaques and
CC dense bodies between myocytes (PubMed:28978740). Co-localizes with deb-
CC 1 and atn-1 at dense bodies (PubMed:28978740). Predominantly localizes
CC to the membrane-proximal region of dense bodies (PubMed:28978740).
CC {ECO:0000269|PubMed:28978740}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:Y45F10D.13a};
CC IsoId=G5EC32-1; Sequence=Displayed;
CC Name=c {ECO:0000312|WormBase:Y45F10D.13c};
CC IsoId=G5EC32-2; Sequence=VSP_060226;
CC -!- TISSUE SPECIFICITY: Expressed in body wall muscles, muscle arm
CC attachment sites at the nerve ring, all non-striated muscles, and
CC distal tip cells of the gonad (PubMed:28978740). Highly expressed in
CC the origins and insertions of the vulval and anal depressor muscles and
CC the spicule-associated and diagonal muscles of the male tail
CC (PubMed:28978740). Expressed in small puncta throughout the uterus,
CC stomatointestinal muscle and proximal gonadal sheath tissues
CC (PubMed:28978740). Not expressed in the pharynx (PubMed:28978740).
CC {ECO:0000269|PubMed:28978740}.
CC -!- DEVELOPMENTAL STAGE: Expressed from embryos to adults
CC (PubMed:28978740). First expressed at the twofold stage of embryonic
CC elongation (PubMed:28978740). Localizes to distal tip cells of the
CC gonad from the late L4 stage to adulthood (PubMed:28978740).
CC {ECO:0000269|PubMed:28978740}.
CC -!- DOMAIN: SH3 domains 1 and 2 are required for its localization to the
CC cell membrane of dense bodies. {ECO:0000269|PubMed:28978740}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in no defects in
CC brood size or locomotion compared to wild-type (PubMed:28978740). No
CC defects in cytoneme length of distal tip cells (PubMed:28978740).
CC {ECO:0000269|PubMed:28978740}.
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DR EMBL; BX284604; CAA16388.2; -; Genomic_DNA.
DR EMBL; BX284604; CBJ25342.1; -; Genomic_DNA.
DR PIR; T26940; T26940.
DR RefSeq; NP_001041035.2; NM_001047570.3. [G5EC32-1]
DR RefSeq; NP_001255756.1; NM_001268827.1. [G5EC32-2]
DR AlphaFoldDB; G5EC32; -.
DR SMR; G5EC32; -.
DR DIP; DIP-24971N; -.
DR IntAct; G5EC32; 72.
DR MINT; G5EC32; -.
DR STRING; 6239.Y45F10D.13a; -.
DR EPD; G5EC32; -.
DR PaxDb; G5EC32; -.
DR PeptideAtlas; G5EC32; -.
DR EnsemblMetazoa; Y45F10D.13a.1; Y45F10D.13a.1; WBGene00012891. [G5EC32-1]
DR EnsemblMetazoa; Y45F10D.13c.1; Y45F10D.13c.1; WBGene00012891. [G5EC32-2]
DR GeneID; 3565590; -.
DR UCSC; Y45F10D.13b; c. elegans.
DR CTD; 3565590; -.
DR WormBase; Y45F10D.13a; CE44448; WBGene00012891; sorb-1. [G5EC32-1]
DR WormBase; Y45F10D.13c; CE39436; WBGene00012891; sorb-1. [G5EC32-2]
DR eggNOG; KOG4225; Eukaryota.
DR GeneTree; ENSGT00940000172418; -.
DR HOGENOM; CLU_291067_0_0_1; -.
DR InParanoid; G5EC32; -.
DR OMA; KAPNPWP; -.
DR OrthoDB; 87641at2759; -.
DR SignaLink; G5EC32; -.
DR PRO; PR:G5EC32; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00012891; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; G5EC32; baseline and differential.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0097433; C:dense body; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IBA:GO_Central.
DR GO; GO:0051659; P:maintenance of mitochondrion location; IMP:UniProtKB.
DR GO; GO:0045214; P:sarcomere organization; IMP:UniProtKB.
DR GO; GO:0016191; P:synaptic vesicle uncoating; IBA:GO_Central.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR003127; SoHo_dom.
DR Pfam; PF14604; SH3_9; 3.
DR SMART; SM00326; SH3; 3.
DR SMART; SM00459; Sorb; 1.
DR SUPFAM; SSF50044; SSF50044; 3.
DR PROSITE; PS50002; SH3; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Coiled coil; Membrane;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..1005
FT /note="Sorbin and SH3 domain-containing protein 1 homolog"
FT /id="PRO_0000447668"
FT DOMAIN 499..567
FT /note="SoHo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00195"
FT DOMAIN 683..742
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 745..805
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 946..1005
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 610..642
FT /evidence="ECO:0000255"
FT COMPBIAS 9..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 2..604
FT /note="MHHPHPFGSNLANSSEPQQPSGQYLNPAADAYNFDTFEDSDKFSPKGNVAAL
FT RNVIHGQLDMKTPTGNSSRYQKPAPPPVDSTPSWAKNVKVYEPNGYVDPHLNKHNMGRV
FT LDGPVNPNKYFQGVPPASYSQVKHNESKPPVPPSTKPPHSAAQALQAQVLQSSKAPSQP
FT QQSQKTSYRIPYDVALDPRHHLGEFDIDDSASIISSCISTFGESSEIAGFSAAAEQRHL
FT YEQYRKKLMEEKNELKEGSETPCVSLSEKVMTSSTENLKNGNNQQNQQPEPQPPSSSIF
FT NSELTPFGHVAPVAKQFEPTNFPPFSPEKESEIKRSIDLESSQLLVKSKSPAPYSTSST
FT DHYGTIRRKHKPVAIDLSKSSPNLASQSPSNLFFGASFEEKQNRSPMTSTPSYKEQGFK
FT NDSLNDSLNQAFEIASSIETTKNAYEAPPTPKSASHDRSISDTYPVSSSTTSTWPSHTT
FT TPTTTTAAAPIAAVAPQTYTEQQPMSTSMSSSVMSTNMDEPIVVGSHQQIPQQSPDSSP
FT ERNEDMSQWYRKMFKQMHRKGEDGSNEGKEQHFINPSNVTDGIGRTTPTASNLGRSREN
FT LSFNQHRPDHPSSYFDSLEH -> CDLPKKDVEFKEIDAIYENMKIKNSQRQRSQNSLD
FT LIRITNNLDETTKSLNLYLQQIDATWKRSKSQPIMK (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_060226"
FT MUTAGEN 461..1005
FT /note="Missing: In gk769190; defects in sarcomere and
FT mitochondrial organization. No motility defects."
FT /evidence="ECO:0000269|PubMed:28978740"
SQ SEQUENCE 1005 AA; 112832 MW; 1EC17DAF276330BD CRC64;
MMHHPHPFGS NLANSSEPQQ PSGQYLNPAA DAYNFDTFED SDKFSPKGNV AALRNVIHGQ
LDMKTPTGNS SRYQKPAPPP VDSTPSWAKN VKVYEPNGYV DPHLNKHNMG RVLDGPVNPN
KYFQGVPPAS YSQVKHNESK PPVPPSTKPP HSAAQALQAQ VLQSSKAPSQ PQQSQKTSYR
IPYDVALDPR HHLGEFDIDD SASIISSCIS TFGESSEIAG FSAAAEQRHL YEQYRKKLME
EKNELKEGSE TPCVSLSEKV MTSSTENLKN GNNQQNQQPE PQPPSSSIFN SELTPFGHVA
PVAKQFEPTN FPPFSPEKES EIKRSIDLES SQLLVKSKSP APYSTSSTDH YGTIRRKHKP
VAIDLSKSSP NLASQSPSNL FFGASFEEKQ NRSPMTSTPS YKEQGFKNDS LNDSLNQAFE
IASSIETTKN AYEAPPTPKS ASHDRSISDT YPVSSSTTST WPSHTTTPTT TTAAAPIAAV
APQTYTEQQP MSTSMSSSVM STNMDEPIVV GSHQQIPQQS PDSSPERNED MSQWYRKMFK
QMHRKGEDGS NEGKEQHFIN PSNVTDGIGR TTPTASNLGR SRENLSFNQH RPDHPSSYFD
SLEHGPNDQY NNQERVKQSN EEELLRLKAE KLAEELRKEK ERKHSFIPSS APSLQNNMDR
LNSLLYDFSS DIQEPAHRDY TPQPVMTATA VYKFEPRSAR ELPLNRGDII RIIREVDGYW
MEGERNGRSG IFPTSYVQIN TGNQGDSQKM RAIYPFTARS DTELSLKRGE IITRRRQIDS
NWLEGSNQIG IVGIFPASYV EPIEQVEQHI PTIVPNRPKT PKIEDQVYNQ VYKPNETVIM
QSNQGYYDKA AVVPNNKVRF DLPSGSDSNL QMSLNPHQNQ FPPTHTQTST QQPSNYGMKK
IEYEREKVVE EVPPMHMDQY RKLNDEPKNP KKDTNILMNA ASLIPKGSEM YRAVYPYQPQ
KEDELQLYTN DIIFVVEKCD DGWFIGTSLR TGDFGIFPGN YVKRH
