SAS_DROME
ID SAS_DROME Reviewed; 1693 AA.
AC Q04164; Q960M6; Q9VI73;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Putative epidermal cell surface receptor;
DE AltName: Full=Stranded at second protein;
DE Flags: Precursor;
GN Name=sas; ORFNames=CG2507;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), FUNCTION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=1339334; DOI=10.1016/0012-1606(92)90183-h;
RA Schonbaum C.P., Organ E.L., Qu S., Cavener D.R.;
RT "The Drosophila melanogaster stranded at second (sas) gene encodes a
RT putative epidermal cell surface receptor required for larval development.";
RL Dev. Biol. 151:431-445(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=24718992; DOI=10.1242/dev.104166;
RA Chung S., Andrew D.J.;
RT "Cadherin 99C regulates apical expansion and cell rearrangement during
RT epithelial tube elongation.";
RL Development 141:1950-1960(2014).
CC -!- FUNCTION: Vital for larval development (PubMed:1339334). During
CC salivary tube elongation, possibly modulates cellular adhesion between
CC the apical surface and apical extracellular matrix, and acts as an
CC apical membrane determinant that functions in apical membrane expansion
CC independently of crb and Cad99C (PubMed:24718992).
CC {ECO:0000269|PubMed:1339334, ECO:0000269|PubMed:24718992}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:24718992}; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q04164-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q04164-2; Sequence=VSP_004071;
CC -!- TISSUE SPECIFICITY: Expressed in most, if not all, ectodermal tissues
CC which produce a cuticle. {ECO:0000269|PubMed:1339334}.
CC -!- DEVELOPMENTAL STAGE: Throughout development.
CC {ECO:0000269|PubMed:1339334}.
CC -!- DOMAIN: The extracellular domain is sufficent for conferring apical
CC characteristics on the salivary gland membrane.
CC {ECO:0000269|PubMed:24718992}.
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DR EMBL; M68866; AAA28879.1; -; mRNA.
DR EMBL; AE014297; AAN13346.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF54052.2; -; Genomic_DNA.
DR EMBL; AY051979; AAK93403.1; -; mRNA.
DR RefSeq; NP_001262336.1; NM_001275407.2. [Q04164-2]
DR RefSeq; NP_001262337.1; NM_001275408.2. [Q04164-1]
DR RefSeq; NP_476611.1; NM_057263.5. [Q04164-2]
DR RefSeq; NP_731141.1; NM_169177.3. [Q04164-1]
DR AlphaFoldDB; Q04164; -.
DR BioGRID; 66056; 5.
DR DIP; DIP-23080N; -.
DR STRING; 7227.FBpp0081089; -.
DR GlyGen; Q04164; 14 sites.
DR PaxDb; Q04164; -.
DR PRIDE; Q04164; -.
DR EnsemblMetazoa; FBtr0081570; FBpp0081089; FBgn0002306. [Q04164-1]
DR EnsemblMetazoa; FBtr0081571; FBpp0081090; FBgn0002306. [Q04164-2]
DR EnsemblMetazoa; FBtr0334884; FBpp0306905; FBgn0002306. [Q04164-2]
DR EnsemblMetazoa; FBtr0334885; FBpp0306906; FBgn0002306. [Q04164-1]
DR GeneID; 40861; -.
DR KEGG; dme:Dmel_CG2507; -.
DR CTD; 40861; -.
DR FlyBase; FBgn0002306; sas.
DR VEuPathDB; VectorBase:FBgn0002306; -.
DR eggNOG; ENOG502QPX6; Eukaryota.
DR InParanoid; Q04164; -.
DR OMA; HMNEPEN; -.
DR PhylomeDB; Q04164; -.
DR BioGRID-ORCS; 40861; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 40861; -.
DR PRO; PR:Q04164; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0002306; Expressed in wing disc and 30 other tissues.
DR ExpressionAtlas; Q04164; baseline and differential.
DR Genevisible; Q04164; DM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; NAS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0002168; P:instar larval development; IMP:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001007; VWF_dom.
DR Pfam; PF00041; fn3; 1.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00214; VWC; 4.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Developmental protein; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..41
FT /evidence="ECO:0000255"
FT CHAIN 42..1693
FT /note="Putative epidermal cell surface receptor"
FT /id="PRO_0000022281"
FT TOPO_DOM 42..1635
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1636..1656
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1657..1693
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 663..708
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 828..902
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 1281..1385
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1407..1506
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1512..1608
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 70..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1147..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1222..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 827
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 846
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 929
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 939
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 930..1274
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_004071"
FT CONFLICT 591
FT /note="V -> L (in Ref. 1; AAA28879)"
FT /evidence="ECO:0000305"
FT CONFLICT 1509
FT /note="V -> G (in Ref. 1; AAA28879)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1693 AA; 185254 MW; DA50F96677F41DC4 CRC64;
MQTCRRRKAS GGQSTIKWSR MCLATLCGLL LLGIQIERAA SAPAGEDAAA TTMPPLDTTT
DAPDAVAATT TPATTAAEQS SSISSITTEA ADGSTTSTTT TTEAANKSNA TETDFTTNVP
VASSLPEETS VRSTSIEPIT STEPTTTPRQ ETEGPDQHMV FSNTEPDQSH IQHIPLRDEH
AESSGADDAT TEMQRQREQD QQQNELNQIS NEQDDVVKDL NNFRHPATLI TASNSNSEEN
VEIESDKQVE TTTTAVPAAA TSTSTEATGT PPTGTPATST STVPNEREED PYHVHILSEN
HDRLAEHEDY QMLSTSTEES STTSTTSTTN STTESGIVAG IVVSQENKAT AEPSTATEST
SISTSTTTAA TAATSTTSRA RAMHMNDPED EAATTIMPDS ESVPVINIVE GQHMLQQEDQ
KDEEEEGVVK ESESSSTTEA STTTTEPSPF VAFAGEGRSA GGGNDIELFL HHNGSTHEQL
MDLSDVSMDG DQNEGSSKTE SSTTSTTTTT AQPETEMPKI VEITASGDTM QRECLANNKS
YKHGELMERD CDERCTCNRG DWMCEPRCRG LSYPRGSQRS MANPNCLEKM VEEDECCRVM
ECSEPQLEPT VVATEGAAPS TNGTGESAVT LPTTDDEATP KPRTDCHYNS GVYKFRERLE
IGCEQICHCA EGGVMDCRPR CPERNHTRLD KCVYVKDPKD VCCQLELCDV TLDDHEQQPT
PLQSNNNEDP EEIDPFRFQE QARDAGGAKP TCTFKGAEYD VGQQFRDGCD QLCICNEQGI
HCAKLECPSN FGLDVQDPHC IRWEPVPADF KPSPPNCCPE SMRCVDNGTC SYQGVQIENW
SPVPANLTGC DQHCYCENGR VECRAACPPV PALPPADLPC HPALARLLPI PDDECCKHWM
CAPQIPKIGG AGQDEETEAT STHSSIPANE TTTTTATANK STSIPSKVPQ IKKDEEKRPP
ASGAFYPTLD GKPPKSIGGL GIFEKPEKPE KAHKKVQHQQ QQHQQQEQQE QQQHQNDVIF
DGDRTEEQEE PLPPNGGFVP FQFGQQHPHQ PHLGPYGFYN PVKPVYEDYN PYEPYDINPN
GTPQGKPPPV PTSQSDLFNI LGAEQPGHPV HPGHGGPPRI HPGQTQKDNH NLGPQVRIEQ
ILQHLQQTVP GGPPPPPPHQ QHQSLTPQLH PQQQQISQQH PGHYVPIVHS GVPPPPPGHG
IAIVDGQTVA YESYPVIPGL GVPQHHPQQH QTTPQQHLQQ TILPSSSTTS GLSTQASEHS
LHQNQGKLAK QQQSGANNLQ PDIEVHTLEA IDPRSIRIVF TVPQVYVNLH GRVELRYSNG
PSNDTSTWEQ QIFAPPEDLI ATSQMEFDLP SLEPNSLYKV KITLILRDLN SQPTSSIYTV
KTPPERTITP PPPFPDYRPD FQDIFKNVED PELTVSETNA SWLQLTWKKL GDDQMEYVDG
VQLRYKELTG MIYSSTPLIH RTLTSYTIQN LQPDTGYEIG LYYIPLAGHG AELRAGHMIK
VRTAQKVDVY GFDVTVNVTK VKTQSVEISW NGVPYPEDKF VHIYRAIYQS DAGKEDSSVF
KVAKRDSTTG TLIMDLKPGT KYRLWLEMYL TNGNTKKSNV VNFITKPGGP ATPGKTGKLL
TAGTDQPVGD YYGPLVVVSV IAALAIMSTL ALLLIITRRR VHQTASITPP RKSDAAYDNP
SYKVEIQQET MNL
