SMAP2_MOUSE
ID SMAP2_MOUSE Reviewed; 428 AA.
AC Q7TN29; Q3U798;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Stromal membrane-associated protein 2;
DE AltName: Full=Stromal membrane-associated protein 1-like;
GN Name=Smap2; Synonyms=Smap1l;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Fetal brain;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP FUNCTION, INTERACTION WITH ARF1; PICALM AND CLATHRIN HEAVY CHAINS,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-56; 187-LEU--ASP-191 AND
RP 212-ASP--LEU-214.
RX PubMed=16571680; DOI=10.1091/mbc.e05-10-0909;
RA Natsume W., Tanabe K., Kon S., Yoshida N., Watanabe T., Torii T.,
RA Satake M.;
RT "SMAP2, a novel ARF GTPase-activating protein, interacts with clathrin and
RT clathrin assembly protein and functions on the AP-1-positive early
RT endosome/trans-Golgi network.";
RL Mol. Biol. Cell 17:2592-2603(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219 AND SER-239, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, 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 ARF1. Can also
CC activate ARF6 (in vitro). May play a role in clathrin-dependent
CC retrograde transport from early endosomes to the trans-Golgi network.
CC {ECO:0000269|PubMed:16571680}.
CC -!- SUBUNIT: Interacts with ARF1. Interacts with PICALM and clathrin heavy
CC chains. {ECO:0000269|PubMed:16571680}.
CC -!- INTERACTION:
CC Q7TN29; Q91VZ6: Smap1; NbExp=4; IntAct=EBI-11358641, EBI-8317690;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16571680}.
CC Note=Detected in multiple foci throughout the cytoplasm and in
CC juxtanuclear structures.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TN29-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TN29-2; Sequence=VSP_018505, VSP_018506;
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DR EMBL; AK152757; BAE31472.1; -; mRNA.
DR EMBL; BC052413; AAH52413.1; -; mRNA.
DR CCDS; CCDS18598.1; -. [Q7TN29-1]
DR RefSeq; NP_598477.2; NM_133716.3. [Q7TN29-1]
DR AlphaFoldDB; Q7TN29; -.
DR SMR; Q7TN29; -.
DR BioGRID; 213674; 2.
DR IntAct; Q7TN29; 1.
DR MINT; Q7TN29; -.
DR STRING; 10090.ENSMUSP00000035800; -.
DR iPTMnet; Q7TN29; -.
DR PhosphoSitePlus; Q7TN29; -.
DR EPD; Q7TN29; -.
DR jPOST; Q7TN29; -.
DR MaxQB; Q7TN29; -.
DR PaxDb; Q7TN29; -.
DR PeptideAtlas; Q7TN29; -.
DR PRIDE; Q7TN29; -.
DR ProteomicsDB; 257259; -. [Q7TN29-1]
DR ProteomicsDB; 257260; -. [Q7TN29-2]
DR Antibodypedia; 17974; 139 antibodies from 23 providers.
DR DNASU; 69780; -.
DR Ensembl; ENSMUST00000043200; ENSMUSP00000035800; ENSMUSG00000032870. [Q7TN29-1]
DR GeneID; 69780; -.
DR KEGG; mmu:69780; -.
DR UCSC; uc008unw.2; mouse. [Q7TN29-1]
DR CTD; 64744; -.
DR MGI; MGI:1917030; Smap2.
DR VEuPathDB; HostDB:ENSMUSG00000032870; -.
DR eggNOG; KOG0703; Eukaryota.
DR GeneTree; ENSGT00940000158387; -.
DR HOGENOM; CLU_023062_5_0_1; -.
DR InParanoid; Q7TN29; -.
DR OMA; MMGYGQS; -.
DR OrthoDB; 1097163at2759; -.
DR PhylomeDB; Q7TN29; -.
DR TreeFam; TF313876; -.
DR BioGRID-ORCS; 69780; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Smap2; mouse.
DR PRO; PR:Q7TN29; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q7TN29; protein.
DR Bgee; ENSMUSG00000032870; Expressed in saccule of membranous labyrinth and 245 other tissues.
DR Genevisible; Q7TN29; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; GTPase activation; Metal-binding;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..428
FT /note="Stromal membrane-associated protein 2"
FT /id="PRO_0000235842"
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 163..231
FT /note="Interaction with clathrin heavy chains"
FT REGION 218..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..428
FT /note="Interaction with PICALM"
FT /evidence="ECO:0000269|PubMed:16571680"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WU79"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WU79"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WU79"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 227..245
FT /note="AVGSMPTAGSAGSVPENLN -> SQGANQKKQARNSSPRTPS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018505"
FT VAR_SEQ 246..428
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018506"
FT MUTAGEN 56
FT /note="R->Q: Loss of GTPase activation."
FT /evidence="ECO:0000269|PubMed:16571680"
FT MUTAGEN 187..191
FT /note="LLGLD->AAAAA: Loss of interaction with clathrin
FT heavy chains; when associated with 212-AAA-214."
FT /evidence="ECO:0000269|PubMed:16571680"
FT MUTAGEN 212..214
FT /note="DLL->AAA: Loss of interaction with clathrin heavy
FT chains; when associated with 187-AAAAA-191."
FT /evidence="ECO:0000269|PubMed:16571680"
FT CONFLICT 89
FT /note="A -> V (in Ref. 2; AAH52413)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="K -> E (in Ref. 2; AAH52413)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 428 AA; 46578 MW; 5F27D6677C3B1AAF CRC64;
MTGKSVKDVD RYQAVLANLL LEEDNKFCAD CQSKGPRWAS WNIGVFICIR CAGIHRNLGV
HISRVKSVNL DQWTQEQIQC MQEMGNGKAN RLYEAYLPET FRRPQIDPAV EGFIRDKYEK
KKYMDRSLDI NVLRKEKDDK WKRGNEPAPE KKMEPVVFEK VKMPQKKEDA QLPRKSSPKS
AAPVMDLLGL DAPVACSIAN SKTSNALEKD LDLLASVPSP SSVSRKAVGS MPTAGSAGSV
PENLNLFPEP GSKSEETGKK QLSKDSILSL YGSQTPQMPA QAMFMAPAQM AYPTAYPSFP
GVTPPNSIMG GMVPPPVGMV AQPGASGMLT PMAMPAGYMG GMQASMMGVP NGMMTTQQAG
YMASMAAMPQ TVYGVQPAQQ LQWNLTQMTQ QMAGMNFYGA NGMMNYGQSM GGGNGQAANQ
TLSPQMWK
