ID   APMAP_BOVIN             Reviewed;         412 AA.
AC   Q3T0E5;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Adipocyte plasma membrane-associated protein;
GN   Name=APMAP;
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].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Exhibits strong arylesterase activity with beta-naphthyl
CC       acetate and phenyl acetate. May play a role in adipocyte
CC       differentiation (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the strictosidine synthase family.
CC       {ECO:0000305}.
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DR   EMBL; BC102429; AAI02430.1; -; mRNA.
DR   RefSeq; NP_001030490.1; NM_001035413.2.
DR   AlphaFoldDB; Q3T0E5; -.
DR   SMR; Q3T0E5; -.
DR   STRING; 9913.ENSBTAP00000005603; -.
DR   PaxDb; Q3T0E5; -.
DR   PRIDE; Q3T0E5; -.
DR   GeneID; 535740; -.
DR   KEGG; bta:535740; -.
DR   CTD; 57136; -.
DR   eggNOG; KOG1520; Eukaryota.
DR   HOGENOM; CLU_023267_0_0_1; -.
DR   InParanoid; Q3T0E5; -.
DR   OrthoDB; 757814at2759; -.
DR   TreeFam; TF316475; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016844; F:strictosidine synthase activity; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 2.120.10.30; -; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR018119; Strictosidine_synth_cons-reg.
DR   Pfam; PF03088; Str_synth; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..412
FT                   /note="Adipocyte plasma membrane-associated protein"
FT                   /id="PRO_0000370857"
FT   TOPO_DOM        1..39
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        61..412
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         19
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HDC9"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   412 AA;  46091 MW;  4E92FA39D2074432 CRC64;
     MTEADGLRQR RPLRPQVVTD DNRTPEAKGG SSFSGRVFRA TFLMLAAFLT IPLLGALVLL
     DSPIDPEPLS FKEPPLFLGV LQPNTKLQQA ERLFENQLVG PESIANIGDV MFTGTADGRV
     VKLENGEVET IARFGSGPCK TRDDEPACGR PLGIRAGPNG TLFVVDAYKG LFEVNPWKRE
     VKLLLSSETP IEGRKMSFLN DLTVTRDGRK IYFTDSSSKW QRRDYLLLLM EGTDDGRLLE
     YDTQTKEVKV LLDHLRFPNG VQLSPAEDFV LVVELAMVRI RRFYVSGLMK GGADVFVENL
     PGFPDNIRAS SSGGYWVSMA AIRANPGFSM LDFLSERPFL KKVIFKLFSQ ETVMKFVPRY
     SLVLELSDSG TFLRSLHDPE GQVVTYVSEA HEHSGHLYLG SFRAPYLCRL RL