ALB2_LATSA
ID ALB2_LATSA Reviewed; 227 AA.
AC D4AEP7; P86190;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Albumin-2 {ECO:0000250|UniProtKB:P08688};
DE AltName: Full=24 kDa albumin {ECO:0000303|PubMed:20147493};
DE Short=LS-24 {ECO:0000303|PubMed:20147493};
DE AltName: Full=PA2 {ECO:0000250|UniProtKB:P08688};
OS Lathyrus sativus (White vetchling).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Lathyrus.
OX NCBI_TaxID=3860;
RN [1] {ECO:0000305, ECO:0000312|PDB:3LP9}
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, HEME-BINDING, AND X-RAY
RP CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH CALCIUM.
RC TISSUE=Seed {ECO:0000269|PubMed:20147493};
RX PubMed=20147493; DOI=10.1104/pp.109.150680;
RA Gaur V., Qureshi I.A., Singh A., Chanana V., Salunke D.M.;
RT "Crystal structure and functional insights of hemopexin fold protein from
RT grass pea.";
RL Plant Physiol. 152:1842-1850(2010).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-40, CRYSTALLIZATION, AND PRELIMINARY X-RAY
RP CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RC TISSUE=Seed {ECO:0000269|PubMed:16946466};
RX PubMed=16946466; DOI=10.1107/s1744309106028077;
RA Qureshi I.A., Sethi D.K., Salunke D.M.;
RT "Purification, identification and preliminary crystallographic studies of
RT an allergenic protein from Lathyrus sativus.";
RL Acta Crystallogr. F 62:869-872(2006).
CC -!- FUNCTION: May play a role in response to oxidative stress and polyamine
CC biosynthesis. The monomeric form binds one hemin per monomer. In the
CC dimeric form, about half of the dimers bind one molecule of spermine
CC each under physiological conditions. Ligand binding is mutually
CC exclusive as binding of hemin leads to dissociation of the dimer.
CC {ECO:0000269|PubMed:20147493}.
CC -!- SUBUNIT: Monomer and homodimer. Dimers are prevalent in solution.
CC {ECO:0000269|PubMed:20147493}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P08688}.
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DR PDB; 3LP9; X-ray; 2.20 A; A/B/C/D=1-227.
DR PDBsum; 3LP9; -.
DR AlphaFoldDB; D4AEP7; -.
DR SMR; D4AEP7; -.
DR EvolutionaryTrace; D4AEP7; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR CDD; cd00094; HX; 1.
DR Gene3D; 2.110.10.10; -; 1.
DR InterPro; IPR000585; Hemopexin-like_dom.
DR InterPro; IPR036375; Hemopexin-like_dom_sf.
DR InterPro; IPR018487; Hemopexin-like_repeat.
DR Pfam; PF00045; Hemopexin; 3.
DR SMART; SM00120; HX; 3.
DR SUPFAM; SSF50923; SSF50923; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cytoplasm; Direct protein sequencing; Metal-binding;
KW Repeat; Seed storage protein; Storage protein.
FT CHAIN 1..227
FT /note="Albumin-2"
FT /id="PRO_0000408767"
FT REPEAT 3..46
FT /note="Hemopexin 1"
FT REPEAT 61..111
FT /note="Hemopexin 2"
FT REPEAT 117..165
FT /note="Hemopexin 3"
FT REPEAT 171..221
FT /note="Hemopexin 4"
FT BINDING 7
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:20147493"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:20147493"
FT BINDING 118
FT /ligand="spermine"
FT /ligand_id="ChEBI:CHEBI:45725"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:20147493"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:20147493"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:20147493"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:3LP9"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:3LP9"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:3LP9"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:3LP9"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:3LP9"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:3LP9"
FT HELIX 58..62
FT /evidence="ECO:0007829|PDB:3LP9"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:3LP9"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:3LP9"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:3LP9"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:3LP9"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:3LP9"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:3LP9"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:3LP9"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:3LP9"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:3LP9"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:3LP9"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:3LP9"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:3LP9"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:3LP9"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:3LP9"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:3LP9"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:3LP9"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:3LP9"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:3LP9"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:3LP9"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:3LP9"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:3LP9"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:3LP9"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:3LP9"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:3LP9"
SQ SEQUENCE 227 AA; 25621 MW; 9FAD69E8D9E7F8E7 CRC64;
TKPGYINAAF RSSKNNEAYF FINDKYVLLD YAPGSSRDKV LYGPTPVRDG FKSLNQTIFG
SYGIDCSFDT ENNEAFIFYE NFCALIDYAP HSKKDKIILG PKKIADVFPF FEGTVFESGI
DAAYRSTRGK EVYLFKGDQY ARIDYGSNSM VNKEIKSISS GYPCFRNTIF ESGADAAFAS
HKTNEVYFFK DDHYARVKVT PGGKLAIMDG VREIVDYWPS LKDIVPL
