ID A0A1U8HPR2_GOSHI Unreviewed; 583 AA.
AC A0A1U8HPR2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 28-JAN-2026, entry version 41.
DE SubName: Full=Patellin-3 isoform X1 {ECO:0000313|RefSeq:XP_016668040.1};
GN Name=LOC107888444 {ECO:0000313|RefSeq:XP_016668040.1};
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000818029, ECO:0000313|RefSeq:XP_016668040.1};
RN [1] {ECO:0000313|Proteomes:UP000818029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000818029};
RX PubMed=32313247; DOI=10.1038/s41588-020-0614-5;
RA Chen Z.J., Sreedasyam A., Ando A., Song Q., De Santiago L.M.,
RA Hulse-Kemp A.M., Ding M., Ye W., Kirkbride R.C., Jenkins J., Plott C.,
RA Lovell J., Lin Y.M., Vaughn R., Liu B., Simpson S., Scheffler B.E., Wen L.,
RA Saski C.A., Grover C.E., Hu G., Conover J.L., Carlson J.W., Shu S.,
RA Boston L.B., Williams M., Peterson D.G., McGee K., Jones D.C., Wendel J.F.,
RA Stelly D.M., Grimwood J., Schmutz J.;
RT "Genomic diversifications of five Gossypium allopolyploid species and their
RT impact on cotton improvement.";
RL Nat. Genet. 52:525-533(2020).
RN [2] {ECO:0000313|RefSeq:XP_016668040.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the patellin family.
CC {ECO:0000256|ARBA:ARBA00007155}.
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DR RefSeq; XP_016668040.1; XM_016812551.2.
DR AlphaFoldDB; A0A1U8HPR2; -.
DR SMR; A0A1U8HPR2; -.
DR STRING; 3635.A0A1U8HPR2; -.
DR PaxDb; 3635-A0A1U8HPR2; -.
DR GeneID; 107888444; -.
DR KEGG; ghi:107888444; -.
DR OMA; LAFNKMM; -.
DR OrthoDB; 75724at2759; -.
DR Proteomes; UP000818029; Chromosome D10.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 2.60.120.680; GOLD domain; 1.
DR Gene3D; 1.10.8.20; N-terminal domain of phosphatidylinositol transfer protein sec14p; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR011074; CRAL/TRIO_N_dom.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR InterPro; IPR009038; GOLD_dom.
DR InterPro; IPR036598; GOLD_dom_sf.
DR InterPro; IPR044834; PATL.
DR InterPro; IPR056794; PATL1-6_C_GOLD.
DR PANTHER; PTHR45932:SF17; CELLULAR RETINALDEHYDE-BINDING_TRIPLE FUNCTION DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45932; PATELLIN-1; 1.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF03765; CRAL_TRIO_N; 1.
DR Pfam; PF25099; GOLD_PATL1_C; 1.
DR PRINTS; PR00180; CRETINALDHBP.
DR SMART; SM01100; CRAL_TRIO_N; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 1.
DR SUPFAM; SSF101576; Supernatant protein factor (SPF), C-terminal domain; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000818029};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 298..473
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 477..578
FT /note="GOLD"
FT /evidence="ECO:0000259|PROSITE:PS50866"
FT REGION 29..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..136
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 583 AA; 65049 MW; CA3E5771903F5B1E CRC64;
MADQVQVGAP PADKVVVVPD VPLAEKPPVA AAAAAKEPPP VPESEEELVK QKQVEDAEAL
ETKISDAVAD GDDAEKVPQS GHYKEESTRV ADLLENEKKA VEELKVLVRE ALNKHEFGGF
AMPQQQQQQQ QQQQQQPKDD SAKEEPKPKA EAVTETVAET KEESIAQAET GDDEEKVATA
TIRSDAVEDD GAKTVEAIED TIVSVSASVQ PEQPPEAASK EPSDAKPNVE GKDAETVSNK
VLPQEVSIWG IPLLADERSD VILLKFLRAR DFKVKEAFTM LQNTIRWRKE FGIDELVEQD
FGNDLEKVVF MHGFDKEGHP VCYNVYGEFQ NKDLYQKTFS DEEKRQNFLR WRIQFLEKSI
RKLDFSPGGI CTIVQINDLK NSPGLTKWEL RQATKQALQL LQDNYPEFVA RQVFINVPWW
YLAVNKMISP FLTQRTRSKF VFAGPSKSAE NLFRYIAAEQ VPVRYGGLSK DGEFGNTDAV
TEITVKPAAK HTVEFPVTEA CLLTWEVRVV GWEVNYGAEF VPSGEDSYTI IIQKSKKVGC
SEGEVVCDNF KVGEPGKVVL TIHNPTSKKK KLLYRLKTMP ASA
//
