ID A0A2K1L342_PHYPA Unreviewed; 309 AA.
AC A0A2K1L342;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=ACB domain-containing protein {ECO:0000259|PROSITE:PS51228};
GN ORFNames=PHYPA_003238 {ECO:0000313|EMBL:PNR60445.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR60445.1};
RN [1] {ECO:0000313|EMBL:PNR60445.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c2_26770V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR60445.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c2_26770V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:Pp3c2_26770V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the ACBP family.
CC {ECO:0000256|ARBA:ARBA00005567}.
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DR EMBL; ABEU02000002; PNR60445.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1L342; -.
DR STRING; 3218.A0A2K1L342; -.
DR PaxDb; 3218-PP1S22_375V6-1; -.
DR EnsemblPlants; Pp3c2_26770V3.1; Pp3c2_26770V3.1; Pp3c2_26770.
DR EnsemblPlants; Pp3c2_26770V3.2; Pp3c2_26770V3.2; Pp3c2_26770.
DR Gramene; Pp3c2_26770V3.1; Pp3c2_26770V3.1; Pp3c2_26770.
DR Gramene; Pp3c2_26770V3.2; Pp3c2_26770V3.2; Pp3c2_26770.
DR InParanoid; A0A2K1L342; -.
DR OrthoDB; 473336at2759; -.
DR Proteomes; UP000006727; Chromosome 2.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IBA:GO_Central.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR Gene3D; 1.20.80.10; -; 1.
DR InterPro; IPR000582; Acyl-CoA-binding_protein.
DR InterPro; IPR035984; Acyl-CoA-binding_sf.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR PANTHER; PTHR23310; ACYL-COA-BINDING PROTEIN, ACBP; 1.
DR PANTHER; PTHR23310:SF77; LD25952P; 1.
DR Pfam; PF00887; ACBP; 1.
DR SUPFAM; SSF47027; Acyl-CoA binding protein; 1.
DR PROSITE; PS51228; ACB_2; 1.
PE 3: Inferred from homology;
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 197..286
FT /note="ACB"
FT /evidence="ECO:0000259|PROSITE:PS51228"
FT REGION 52..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 309 AA; 34123 MW; 0428E87812F1E2AB CRC64;
MGDWQEKMQT IIIGFVFTCM VVMLFSVISS FRAGNLRVAR ETDDEVPLLV PSEAAELSPA
HEQNTPLVAT DEETEADGDS ELEDSAHDFS SLSSPDSEVE TDATAACSPR EIDSAINPTV
SKVESKDNKV DATKDELAEF EKDEGAEDEN IETKHVSISG EHSLKSLNEQ ANGDVEDELE
VSRSATDDWE AIESTELEKR FGAASTYAST MVVSPNVKSS SEALLQLYAF YKIATEGPCS
NPQPSILQPT ARAKWNEWQK LGSMPQEEAM QKYIAVLTEV NSTCYETYQK SKEPARVVDQ
NDRDSSVRW
//
