P41260 (GLB1_PHAPT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Hemoglobin-1 Alternative name(s): Hemoglobin I Short name=Hb I Short name=HbI Sulfide-reactive hemoglobin
Organism	Phacoides pectinatus (Thick lucine) (Lucina pectinata)
Taxonomic identifier	244486 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Lophotrochozoa › Mollusca › Bivalvia › Heteroconchia › Veneroida › Lucinoidea › Lucinidae › Phacoides

Protein attributes

Sequence length	143 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serves to transport hydrogen sulfide to autotrophic bacteria.
Subunit structure	Monomer.
Subcellular location	Cytoplasm.
Miscellaneous	This molluscan globin lacks one of the heme-binding histidine residues found in most other globins.
Sequence similarities	Belongs to the globin family.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cytoplasm
Ligand	Heme Iron Metal-binding
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	oxygen transport Inferred from electronic annotation. Source: InterPro
Cellular_component	extracellular region Inferred from electronic annotation. Source: InterPro hemoglobin complex Inferred from electronic annotation. Source: InterPro
Molecular_function	heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro oxygen binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 143

142

Hemoglobin-1

PRO_0000052492

Sites

Metal binding

97

1

Iron (heme proximal ligand)

Amino acid modifications

Modified residue

2

1

N-acetylserine

Experimental info

Sequence conflict

49

1

K → S AA sequence Ref.3

Secondary structure

1

.

.

.

.

.

.

.

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.

.

.

.

.

.

.

.

.

.

.

143

Helix Strand Turn

Details...

Helix

5 – 36

32

Helix

38 – 42

5

Turn

43 – 50

8

Helix

53 – 55

3

Helix

60 – 77

18

Turn

78 – 81

4

Helix

83 – 99

17

Helix

104 – 117

14

Helix

118 – 121

4

Helix

125 – 139

15

Helix

140 – 142

3

Sequences

	Sequence		Length	Mass (Da)
	P41260 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 0DFB3A709E97BED5	FASTA	143	14,944
	10 20 30 40 50 60 MSLSAAQKDN VKSSWAKASA AWGTAGPEFF MALFDAHDDV FAKFSGLFKG AAKGTVKNTP 70 80 90 100 110 120 EMAAQAQSFK GLVSNWVDNL DNAGALEGQC KTFAANHKAR GISAGQLEAA FKVLAGFMKS 130 140 YGGDEGAWTA VAGALMGMIR PNM

References

[1]	"The cDNA-derived amino acid sequence of hemoglobin I from Lucina pectinata." Antommattei-Perez F.M., Rosado-Ruiz T., Cadilla C.L., Lopez-Garriga J. J. Protein Chem. 18:831-836(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Hemoglobins of the Lucina pectinata/bacteria symbiosis. I. Molecular properties, kinetics and equilibria of reactions with ligands." Kraus D.W., Wittenberg J.B. J. Biol. Chem. 265:16043-16053(1990) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[3]	"Structure of the sulfide-reactive hemoglobin from the clam Lucina pectinata. Crystallographic analysis at 1.5-A resolution." Rizzi M., Wittenberg J.B., Coda A., Ascenzi P., Fasano M., Bolognesi M. J. Mol. Biol. 244:86-99(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS). Tissue: Gill.
[4]	"Structural bases for sulfide recognition in Lucina pectinata hemoglobin I." Rizzi M., Wittenberg J.B., Coda A., Ascenzi P., Bolognesi M. J. Mol. Biol. 258:1-5(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[5]	"Cyanide binding to Lucina pectinata hemoglobin I and to sperm whale myoglobin: an X-ray crystallographic study." Bolognesi M., Rosano C., Losso R., Borassi A., Rizzi M., Wittenberg J.B., Boffi A., Ascenzi P. Biophys. J. 77:1093-1099(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS), SEQUENCE REVISION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF187049 mRNA. Translation: AAG01380.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B0B	X-ray	1.43	A	2-141	[»]
1EBT	X-ray	1.90	A	2-143	[»]
1FLP	X-ray	1.50	A	2-137	[»]
1MOH	X-ray	1.90	A	2-137	[»]

ProteinModelPortal

P41260.

SMR

P41260. Positions 3-143.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

1.10.490.10. 1 hit.

InterPro

IPR002336. Erythrocruorin.
IPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
[Graphical view]

Pfam

PF00042. Globin. 1 hit.
[Graphical view]

PRINTS

PR00611. ERYTHCRUORIN.

SUPFAM

SSF46458. Globin_like. 1 hit.

PROSITE

PS01033. GLOBIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P41260.

Entry information

Entry name

GLB1_PHAPT

Accession

Primary (citable) accession number: P41260
Secondary accession number(s): Q9GV87

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 74 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)