ID   SMAP2_BOVIN             Reviewed;         429 AA.
AC   Q5EA00; Q08DF8;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Stromal membrane-associated protein 2;
DE   AltName: Full=Stromal membrane-associated protein 1-like;
GN   Name=SMAP2; Synonyms=SMAP1L;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal muscle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with ARF1. Interacts with PICALM and clathrin heavy
CC       chains (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Detected in multiple foci
CC       throughout the cytoplasm and in juxtanuclear structures. {ECO:0000250}.
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DR   EMBL; BT020769; AAX08786.1; -; mRNA.
DR   EMBL; BC123771; AAI23772.1; -; mRNA.
DR   RefSeq; NP_001069138.1; NM_001075670.2.
DR   AlphaFoldDB; Q5EA00; -.
DR   SMR; Q5EA00; -.
DR   STRING; 9913.ENSBTAP00000029227; -.
DR   PaxDb; Q5EA00; -.
DR   PRIDE; Q5EA00; -.
DR   Ensembl; ENSBTAT00000029227; ENSBTAP00000029227; ENSBTAG00000021922.
DR   GeneID; 514465; -.
DR   KEGG; bta:514465; -.
DR   CTD; 64744; -.
DR   VEuPathDB; HostDB:ENSBTAG00000021922; -.
DR   VGNC; VGNC:34984; SMAP2.
DR   eggNOG; KOG0703; Eukaryota.
DR   GeneTree; ENSGT00940000158387; -.
DR   HOGENOM; CLU_023062_5_0_1; -.
DR   InParanoid; Q5EA00; -.
DR   OMA; MMGYGQS; -.
DR   OrthoDB; 1097163at2759; -.
DR   TreeFam; TF313876; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000021922; Expressed in nasopharynx and 104 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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   Cytoplasm; GTPase activation; Metal-binding; Phosphoprotein;
KW   Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..429
FT                   /note="Stromal membrane-associated protein 2"
FT                   /id="PRO_0000235840"
FT   DOMAIN          13..137
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          138..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          163..232
FT                   /note="Interaction with clathrin heavy chains"
FT                   /evidence="ECO:0000250"
FT   REGION          217..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..429
FT                   /note="Interaction with PICALM"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        138..175
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         127
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WU79"
FT   MOD_RES         219
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WU79"
FT   MOD_RES         223
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WU79"
FT   MOD_RES         225
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WU79"
FT   MOD_RES         231
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WU79"
FT   MOD_RES         240
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WU79"
SQ   SEQUENCE   429 AA;  46900 MW;  985C0893E15BA853 CRC64;
     MTGKSVKDVD RYQAVLANLL LEEDNKFCAD CQSKGPRWAS WNIGVFICIR CAGIHRNLGV
     HISRVKSVNL DQWTQEQIQC MQEMGNGKAN RLYEAYLPET FRRPQIDHAV EGFIRDKYEK
     KKYMDRSLDI NAFRKEKDNK WKRGSEPAPE KKMEPVVFEK VKMPQKKEDP QLPRKTSPKS
     KAPVVDLLGL DAPVSCSIAN GKTSNTLEKD LDLLASVSSP SSSVSRKVVG SMPTPGSAGS
     VPENLNLFPE PGSKSEETSK KQLSKDSILS LYGSQTPQMP TQAMFMAPAQ MAYPTAYPSF
     PGVTPPNSLM GSMMPPPVGM VAQPGASGMV APMAMPAGYM GGMQASMMGV PNGMMTTQQA
     SYMAGMAAMP QTMYGVQPAQ QLQWNLTQMT QQMAGMNFCG TNGMLSYGQS MNGGNGQAAN
     QTLSPQMWK