SMAP1_MOUSE
ID SMAP1_MOUSE Reviewed; 440 AA.
AC Q91VZ6; Q497I6; Q68EF3;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Stromal membrane-associated protein 1;
GN Name=Smap1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, Jaw, Limb, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=9644265; DOI=10.1093/oxfordjournals.jbchem.a022082;
RA Sato Y., Hong H.N., Yanai N., Obinata M.;
RT "Involvement of stromal membrane-associated protein (SMAP-1) in
RT erythropoietic microenvironment.";
RL J. Biochem. 124:209-216(1998).
RN [3]
RP FUNCTION, INTERACTION WITH ARF6 AND CLATHRIN HEAVY CHAINS, AND MUTAGENESIS
RP OF ARG-61 AND 192-LEU--ASP-196.
RX PubMed=15659652; DOI=10.1091/mbc.e04-08-0683;
RA Tanabe K., Torii T., Natsume W., Braesch-Andersen S., Watanabe T.,
RA Satake M.;
RT "A novel GTPase-activating protein for ARF6 directly interacts with
RT clathrin and regulates clathrin-dependent endocytosis.";
RL Mol. Biol. Cell 16:1617-1628(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: GTPase activating protein that acts on ARF6. Plays a role in
CC clathrin-dependent endocytosis. May play a role in erythropoiesis.
CC {ECO:0000269|PubMed:15659652, ECO:0000269|PubMed:9644265}.
CC -!- SUBUNIT: Interacts with ARF6. Interacts with clathrin heavy chains via
CC the clathrin box-like motif. {ECO:0000269|PubMed:15659652}.
CC -!- INTERACTION:
CC Q91VZ6; Q7TN29: Smap2; NbExp=4; IntAct=EBI-8317690, EBI-11358641;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:9644265};
CC Peripheral membrane protein {ECO:0000305|PubMed:9644265}; Cytoplasmic
CC side {ECO:0000305|PubMed:9644265}.
CC -!- TISSUE SPECIFICITY: Detected in adult brain, lung, heart, liver, ovary
CC and bone marrow. Detected in stromal cells of the red pulp of adult
CC spleen. {ECO:0000269|PubMed:9644265}.
CC -!- DEVELOPMENTAL STAGE: Detected in stromal cells of fetal liver at 10.5
CC days. Expression was maximal after 14 days of development and decreased
CC thereafter. Detected at low levels after 18 days.
CC {ECO:0000269|PubMed:9644265}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI00538.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={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; BC006946; AAH06946.1; -; mRNA.
DR EMBL; BC080286; AAH80286.1; -; mRNA.
DR EMBL; BC100537; AAI00538.1; ALT_SEQ; mRNA.
DR CCDS; CCDS14851.1; -.
DR RefSeq; NP_001277612.1; NM_001290683.1.
DR RefSeq; NP_082810.1; NM_028534.3.
DR AlphaFoldDB; Q91VZ6; -.
DR SMR; Q91VZ6; -.
DR BioGRID; 221043; 12.
DR ELM; Q91VZ6; -.
DR IntAct; Q91VZ6; 13.
DR MINT; Q91VZ6; -.
DR STRING; 10090.ENSMUSP00000027339; -.
DR iPTMnet; Q91VZ6; -.
DR PhosphoSitePlus; Q91VZ6; -.
DR SwissPalm; Q91VZ6; -.
DR EPD; Q91VZ6; -.
DR jPOST; Q91VZ6; -.
DR MaxQB; Q91VZ6; -.
DR PaxDb; Q91VZ6; -.
DR PeptideAtlas; Q91VZ6; -.
DR PRIDE; Q91VZ6; -.
DR ProteomicsDB; 261256; -.
DR Antibodypedia; 31248; 148 antibodies from 23 providers.
DR DNASU; 98366; -.
DR Ensembl; ENSMUST00000027339; ENSMUSP00000027339; ENSMUSG00000026155.
DR GeneID; 98366; -.
DR KEGG; mmu:98366; -.
DR UCSC; uc007amg.2; mouse.
DR CTD; 60682; -.
DR MGI; MGI:2138261; Smap1.
DR VEuPathDB; HostDB:ENSMUSG00000026155; -.
DR eggNOG; KOG0703; Eukaryota.
DR GeneTree; ENSGT00940000155884; -.
DR HOGENOM; CLU_023062_5_0_1; -.
DR InParanoid; Q91VZ6; -.
DR OMA; NNGWSGM; -.
DR OrthoDB; 1097163at2759; -.
DR PhylomeDB; Q91VZ6; -.
DR TreeFam; TF313876; -.
DR BioGRID-ORCS; 98366; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Smap1; mouse.
DR PRO; PR:Q91VZ6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q91VZ6; protein.
DR Bgee; ENSMUSG00000026155; Expressed in blood and 260 other tissues.
DR ExpressionAtlas; Q91VZ6; baseline and differential.
DR Genevisible; Q91VZ6; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030276; F:clathrin binding; IDA:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IDA:MGI.
DR GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; IDA:MGI.
DR CDD; cd08839; ArfGap_SMAP; 1.
DR Gene3D; 1.10.220.150; -; 1.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR044732; ArfGAP_SMAP1-like.
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 1: Evidence at protein level;
KW Cell membrane; GTPase activation; Membrane; Metal-binding;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..440
FT /note="Stromal membrane-associated protein 1"
FT /id="PRO_0000235839"
FT DOMAIN 18..143
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT ZN_FING 33..56
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 140..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 192..196
FT /note="Interaction with clathrin heavy chains"
FT COMPBIAS 140..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 61
FT /note="R->Q: Loss of GTPase activation."
FT /evidence="ECO:0000269|PubMed:15659652"
FT MUTAGEN 192..196
FT /note="LLGLD->AAAAA: Loss of interaction with clathrin
FT heavy chains."
FT /evidence="ECO:0000269|PubMed:15659652"
SQ SEQUENCE 440 AA; 47660 MW; E1852548BAFBC229 CRC64;
MATRSCREKA QKLNEQHQLI LSKLLREEDN KYCADCEAKG PRWASWNIGV FICIRCAGIH
RNLGVHISRV KSVNLDQWTP EQIQCMQDMG NTKARLLYEA NLPENFRRPQ TDQAVEFFIR
DKYEKKKYYD KNAIAITNKE KEKKKDEKKR EKEPEKPAKP LTTEKLPKKE EQQLEPKKST
SPKNAAEPTI DLLGLDGPAE APVTNGNPAT APALSDDLDI FGPMISNPLP AAVMPPAQGT
ASVPAPATLS TVTSGDLDLF TEQTTKSEEV AKKQLSKDSI LSLYGTGAQQ STPGVFMGPT
NIPFTSQAPT AFQGFPSMGV PVPAAPGLIG NMMGQNTGMM VGMPMHNGFM GNAQTGVMPL
PQNVVGPQGG MVGQMGAPQS KFGLPQAQQP QWNLSQMNQQ MAAMNLSSAN ASAGFGQPPS
TTAGWSGSSS GQTLSTQLWK
