SQT1_CAEEL
ID SQT1_CAEEL Reviewed; 324 AA.
AC P12114; Q17509;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cuticle collagen sqt-1;
DE AltName: Full=Protein roller-5;
DE AltName: Full=Protein squat-1;
GN Name=sqt-1; Synonyms=rol-5; ORFNames=B0491.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=3180220; DOI=10.1016/0092-8674(88)90214-0;
RA Kramer J.M., Johnson J.J., Edgar R.S., Basch C., Roberts S.;
RT "The sqt-1 gene of C. elegans encodes a collagen critical for organismal
RT morphogenesis.";
RL Cell 55:555-565(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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).
CC -!- FUNCTION: Nematode cuticles are composed largely of collagen-like
CC proteins. The cuticle functions both as an exoskeleton and as a barrier
CC to protect the worm from its environment. This is a collagen critical
CC for organismal morphogenesis. Mutations in sqt-1 can lengthen, shorten,
CC or helically twist the entire animal.
CC -!- SUBUNIT: Collagen polypeptide chains are complexed within the cuticle
CC by disulfide bonds and other types of covalent cross-links.
CC -!- SIMILARITY: Belongs to the cuticular collagen family. {ECO:0000305}.
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; J03146; AAA65468.1; -; Genomic_DNA.
DR EMBL; Z49907; CAA90084.1; -; Genomic_DNA.
DR PIR; A31920; A31920.
DR PIR; T18763; T18763.
DR RefSeq; NP_496421.1; NM_064020.5.
DR AlphaFoldDB; P12114; -.
DR SMR; P12114; -.
DR BioGRID; 40038; 2.
DR IntAct; P12114; 1.
DR STRING; 6239.B0491.2.1; -.
DR EPD; P12114; -.
DR PaxDb; P12114; -.
DR PeptideAtlas; P12114; -.
DR EnsemblMetazoa; B0491.2.1; B0491.2.1; WBGene00005016.
DR EnsemblMetazoa; B0491.2.2; B0491.2.2; WBGene00005016.
DR UCSC; B0491.2.1; c. elegans.
DR WormBase; B0491.2; CE02104; WBGene00005016; sqt-1.
DR eggNOG; KOG3544; Eukaryota.
DR HOGENOM; CLU_001074_4_4_1; -.
DR InParanoid; P12114; -.
DR OMA; EHPIGRP; -.
DR OrthoDB; 1351852at2759; -.
DR PhylomeDB; P12114; -.
DR PRO; PR:P12114; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00005016; Expressed in larva and 2 other tissues.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0042329; F:structural constituent of collagen and cuticulin-based cuticle; IMP:WormBase.
DR GO; GO:0040002; P:collagen and cuticulin-based cuticle development; IMP:WormBase.
DR GO; GO:0042338; P:cuticle development involved in collagen and cuticulin-based cuticle molting cycle; IMP:WormBase.
DR InterPro; IPR002486; Col_cuticle_N.
DR InterPro; IPR008160; Collagen.
DR Pfam; PF01484; Col_cuticle_N; 1.
DR Pfam; PF01391; Collagen; 1.
DR SMART; SM01088; Col_cuticle_N; 1.
PE 3: Inferred from homology;
KW Collagen; Cuticle; Disulfide bond; Reference proteome; Repeat.
FT CHAIN 1..324
FT /note="Cuticle collagen sqt-1"
FT /id="PRO_0000127596"
FT REGION 68..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..153
FT /note="Triple-helical region"
FT REGION 129..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..231
FT /note="Triple-helical region"
FT REGION 237..299
FT /note="Triple-helical region"
FT COMPBIAS 83..101
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 158
FT /note="A -> V (in Ref. 1; AAA65468)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="R -> G (in Ref. 1; AAA65468)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 32850 MW; 60A69FAD3F315DAC CRC64;
MSVKLACYVT ASVTVATLMV CFMTMSTIYS EVDGFREKLD TEMNVFRQST NGLWKDIVVI
GRSSKRVRRQ YEETNATPTP HADGSPSAPP GQPPAVPPVF NQPKTPNGAN GNGPTCNCNA
DNKCPAGPSG PKGVPGVPGL DGVPGLDGVP GVGADDIAPQ RESVGCFTCP QGPVGPPGAL
GRPGPRGLPG PRGQNGNPGR DGQPGHPGEQ GSSGQIGKIG EPGPPGEKGR DAEHPIGRPG
PKGPRGDQGP TGPAGQNGLH GPPGEPGTVG PEGPSGKQGR QGPDGTQGET GPDGRPGKDA
EYCQCPDKSP PSEAVNANRG YRNI
