SMAP2_CHICK
ID SMAP2_CHICK Reviewed; 428 AA.
AC Q5F413;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Stromal membrane-associated protein 2;
DE AltName: Full=Stromal membrane-associated protein 1-like;
GN Name=SMAP2; Synonyms=SMAP1L; ORFNames=RCJMB04_3n15;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: GTPase activating protein. May play a role in clathrin-
CC dependent retrograde transport from early endosomes to the trans-Golgi
CC network (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: May interact with clathrin heavy chains. {ECO:0000250}.
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DR EMBL; AJ851487; CAH65121.1; -; mRNA.
DR RefSeq; NP_001026073.1; NM_001030902.1.
DR AlphaFoldDB; Q5F413; -.
DR SMR; Q5F413; -.
DR STRING; 9031.ENSGALP00000039979; -.
DR Ensembl; ENSGALT00000050934; ENSGALP00000045717; ENSGALG00000029244.
DR GeneID; 419641; -.
DR KEGG; gga:419641; -.
DR CTD; 64744; -.
DR VEuPathDB; HostDB:geneid_419641; -.
DR eggNOG; KOG0703; Eukaryota.
DR GeneTree; ENSGT00940000158387; -.
DR InParanoid; Q5F413; -.
DR OMA; MMGYGQS; -.
DR OrthoDB; 1097163at2759; -.
DR PhylomeDB; Q5F413; -.
DR PRO; PR:Q5F413; -.
DR Proteomes; UP000000539; Chromosome 23.
DR Bgee; ENSGALG00000029244; Expressed in granulocyte and 13 other tissues.
DR ExpressionAtlas; Q5F413; baseline and differential.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.220.150; -; 1.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR Pfam; PF01412; ArfGap; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 2: Evidence at transcript level;
KW GTPase activation; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..428
FT /note="Stromal membrane-associated protein 2"
FT /id="PRO_0000235843"
FT DOMAIN 13..139
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT ZN_FING 28..51
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 161..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 46315 MW; 01903194C57985F3 CRC64;
MTGKSVRDVE RYQAVLGSLL SEEENKYCAD CQAKGPRWAS WNIGVFICIR CAGIHRNLGV
HISRVKSVNL DQWTQEQIQC MQEMGNGKAN RLYEAFLPEN FRRPQTDQAV EGFIRDKYEK
KKYMDRSIDI NTFRKEKDDK WKKSNEPVSE RKLEPIVFEK VKMPQKKEET QQSRKSSPKS
TEPVIDLLGL DAPVPSTLTN GRPCSLEKDL DLFASVGLNS DSRKVSGSMP TSGSAGSVPE
NLNLFPEPGG KGEEAGKKQL SKDSILSLYG SQTPQLPAQG AMFMAPAQMA YPAAAYTSFP
GVPPSSSMMG GMMAPSVGVM AQHGAAGMVT PMAIPAGYVG NVQAAVIGVP NGMMAAQQAG
YVAGMAAVPQ PVYGVQPAQQ LQWNITQMTQ QMAGMNFYGA NGVMGYGQSM GGGGAQGSNQ
SLSTQLWK