HEM_DROME
ID HEM_DROME Reviewed; 1126 AA.
AC P55162; Q540Y5; Q9VNU8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Membrane-associated protein Hem;
DE AltName: Full=dHem-2;
GN Name=Hem; Synonyms=HEM2; ORFNames=CG5837;
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], FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S;
RX PubMed=7643388; DOI=10.1006/jmbi.1995.0414;
RA Baumgartner S., Martin D., Chiquet-Ehrismann R., Sutton J., Desai A.,
RA Huang I., Kato K., Hromas R.;
RT "The HEM proteins: a novel family of tissue-specific transmembrane proteins
RT expressed from invertebrates through mammals with an essential function in
RT oogenesis.";
RL J. Mol. Biol. 251:41-49(1995).
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.
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].
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 COMPONENT OF WAVE COMPLEX.
RX PubMed=15385157; DOI=10.1016/j.ydbio.2004.07.009;
RA Schenck A., Qurashi A., Carrera P., Bardoni B., Diebold C., Schejter E.,
RA Mandel J.-L., Giangrande A.;
RT "WAVE/SCAR, a multifunctional complex coordinating different aspects of
RT neuronal connectivity.";
RL Dev. Biol. 274:260-270(2004).
CC -!- FUNCTION: Plays a role during growth of the oocyte.
CC {ECO:0000269|PubMed:7643388}.
CC -!- SUBUNIT: Component of the WAVE complex composed of Hem/Kette, Scar/Wave
CC and Sra-1/Cyfip where it binds directly to the C-terminus of Sra-1.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally in the oocyte and shows
CC uniform expression during the first half of embryogenesis, but becomes
CC restricted to the brain and the nervous system during late
CC embryogenesis. {ECO:0000269|PubMed:7643388}.
CC -!- SIMILARITY: Belongs to the HEM-1/HEM-2 family. {ECO:0000305}.
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DR EMBL; X80028; CAA56332.1; -; mRNA.
DR EMBL; AE014296; AAF51820.1; -; Genomic_DNA.
DR EMBL; AY118579; AAM49948.1; -; mRNA.
DR PIR; S57832; S49208.
DR RefSeq; NP_524214.1; NM_079490.4.
DR AlphaFoldDB; P55162; -.
DR SMR; P55162; -.
DR BioGRID; 65698; 17.
DR ComplexPortal; CPX-2972; WAVE regulatory complex.
DR DIP; DIP-18694N; -.
DR IntAct; P55162; 5.
DR STRING; 7227.FBpp0078162; -.
DR iPTMnet; P55162; -.
DR PaxDb; P55162; -.
DR PRIDE; P55162; -.
DR EnsemblMetazoa; FBtr0078510; FBpp0078162; FBgn0011771.
DR GeneID; 40462; -.
DR KEGG; dme:Dmel_CG5837; -.
DR UCSC; CG5837-RA; d. melanogaster.
DR CTD; 40462; -.
DR FlyBase; FBgn0011771; Hem.
DR VEuPathDB; VectorBase:FBgn0011771; -.
DR eggNOG; KOG1917; Eukaryota.
DR GeneTree; ENSGT00390000016619; -.
DR HOGENOM; CLU_004450_0_0_1; -.
DR InParanoid; P55162; -.
DR OMA; VGMVMYN; -.
DR OrthoDB; 138196at2759; -.
DR PhylomeDB; P55162; -.
DR Reactome; R-DME-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-DME-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-DME-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-9013149; RAC1 GTPase cycle.
DR SignaLink; P55162; -.
DR BioGRID-ORCS; 40462; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 40462; -.
DR PRO; PR:P55162; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0011771; Expressed in embryonic/larval hemocyte (Drosophila) and 29 other tissues.
DR Genevisible; P55162; DM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031209; C:SCAR complex; IDA:FlyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0007409; P:axonogenesis; IMP:FlyBase.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IMP:FlyBase.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IMP:FlyBase.
DR GO; GO:0030031; P:cell projection assembly; IMP:FlyBase.
DR GO; GO:0007417; P:central nervous system development; IMP:FlyBase.
DR GO; GO:0008407; P:chaeta morphogenesis; IMP:FlyBase.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0007520; P:myoblast fusion; IMP:FlyBase.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:FlyBase.
DR GO; GO:0001764; P:neuron migration; IMP:FlyBase.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IMP:FlyBase.
DR GO; GO:0050807; P:regulation of synapse organization; IDA:SynGO.
DR InterPro; IPR019137; Nck-associated_protein-1.
DR PANTHER; PTHR12093; PTHR12093; 1.
DR Pfam; PF09735; Nckap1; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1126
FT /note="Membrane-associated protein Hem"
FT /id="PRO_0000216176"
FT TRANSMEM 989..1006
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1126 AA; 129380 MW; 125FE7177AECC0E5 CRC64;
MARPIFPNQQ KIAEKLIILN DRGLGILTRI YNIKKACGDT KSKPGFLSEK SLESSIKFIV
KRFPNIDVKG LNAIVNIKAE IIKSLSLYYH TFVDLLDFKD NVCELLTTMD ACQIHLDITL
NFELTKYYLD LVVTYVSLMI VLSRVEDRKA VLGLYNAAYE LQNNQADTGF PRLGQMILDY
EVPLKKLAEE FIPHQRLLTS ALRSLTSIYA LRNLPADKWR EMQKLSLVGN PAILLKAVRT
DTMSCEYISL EAMDRWIIFG LLLNHQMLGQ YPEVNKIWLS ALESSWVVAL FRDEVLQIHQ
YIQATFDGIK GYSKRIGEVK EAYNTAVQKA ALMHRERRKF LRTALKELAL IMTDQPGLLG
PKAIFIFIGL CLARDEILWL LRHNDNPPLL KNKGKSNEDL VDRQLPELLF HMEELRALVR
KYSQVMQRYY VQYLSGFDAT DLNIRMQSLQ MCPEDESIIF SSLYNTAAAL TVKQVEDNEL
FYFRPFRLDW FRLQTYMSVG KAALRIAEHA ELARLLDSMV FHTRVVDNLD EILVETSDLS
IFCFYNKMFD DQFHMCLEFP AQNRYIIAFP LICSHFQNCT HEMCPEERHH IRERSLSVVN
IFLEEMAKEA KNIITTICDE QCTMADALLP KHCAKILSVQ SARKKKDKSK SKHFDDIRKP
GDESYRKTRE DLTTMDKLHM ALTELCFAIN YCPTVNVWEF AFAPREYLCQ NLEHRFSRDL
VGMVMFNQET MEIAKPSELL ASVRAYMNVL QTVENYVHID ITRVFNNCLL QQTQALDSHG
EKTIAALYNT WYSEVLLRRV SAGNIVFSIN QKAFVPISPE GWVPFNPQEF SDLNELRALA
ELVGPYGIKT LNETLMWHIA NQVQELKSLV STNKEVLITL RTSFDKPEVM KEQFKRLQDV
DRVLQRMTII GVIICFRNLV HEALVDVLDK RIPFLLSSVK DFQEHLPGGD QIRVASEMAS
AAGLLCKVDP TLATTLKSKK PEFDEGEHLT ACLLMVFVAV SIPKLARNEN SFYRATIDGH
SNNTHCMAAA INNIFGALFT ICGQSDMEDR MKEFLALASS SLLRLGQESD KEATRNRESI
YLLLDEIVKQ SPFLTMDLLE SCFPYVLIRN AYHGVYKQEQ ILGLAL
