CHHA_HOMAM
ID CHHA_HOMAM Reviewed; 134 AA.
AC P19806; Q25014; Q26415;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Crustacean hyperglycemic hormones isoform A;
DE Contains:
DE RecName: Full=CHH precursor-related peptide A;
DE Short=CPRP-A;
DE Contains:
DE RecName: Full=Crustacean hyperglycemic hormone A;
DE Short=CHH-A;
DE AltName: Full=Molt-inhibiting hormone;
DE Short=MIH;
DE Flags: Precursor;
OS Homarus americanus (American lobster).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC Nephropoidea; Nephropidae; Homarus.
OX NCBI_TaxID=6706;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7999796; DOI=10.1016/0167-4781(94)00173-z;
RA de Kleijn D.P.V., de Leeuw E.P.H., van den Berg M.C., Martens G.J.M.,
RA van Herp F.;
RT "Cloning and expression of two mRNAs encoding structurally different
RT crustacean hyperglycemic hormone precursors in the lobster Homarus
RT americanus.";
RL Biochim. Biophys. Acta 1260:62-66(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 61-133, AND AMIDATION AT VAL-132.
RC TISSUE=Eyestalk;
RX PubMed=1879416; DOI=10.1111/j.1432-1033.1991.tb21054.x;
RA Tensen C.P., de Kleijn D.P.V., van Herp F.;
RT "Cloning and sequence analysis of cDNA encoding two crustacean
RT hyperglycemic hormones from the lobster Homarus americanus.";
RL Eur. J. Biochem. 200:103-106(1991).
RN [3]
RP PROTEIN SEQUENCE OF 61-131.
RC TISSUE=Sinus gland;
RX PubMed=2169734; DOI=10.1016/0006-291x(90)91219-i;
RA Chang E.S., Prestwich G.D., Bruce M.J.;
RT "Amino acid sequence of a peptide with both molt-inhibiting and
RT hyperglycemic activities in the lobster, Homarus americanus.";
RL Biochem. Biophys. Res. Commun. 171:818-826(1990).
RN [4]
RP PROTEIN SEQUENCE OF 74-110.
RX PubMed=2384751; DOI=10.1111/j.1471-4159.1990.tb04561.x;
RA Pavloff M.S., Goy M.F.;
RT "Purification and chemical characterization of peptide G1, an invertebrate
RT neuropeptide that stimulates cyclic GMP metabolism.";
RL J. Neurochem. 55:788-797(1990).
RN [5]
RP PROTEIN SEQUENCE OF 61-68, PYROGLUTAMATE FORMATION AT GLN-61, AND D-AMINO
RP ACID AT PHE-63.
RX PubMed=8034574; DOI=10.1016/s0021-9258(17)32303-7;
RA Soyez D., van Herp F., Rossier J., Le Caer J.-P., Tensen C.P., Lafont R.;
RT "Evidence for a conformational polymorphism of invertebrate neurohormones.
RT D-amino acid residue in crustacean hyperglycemic peptides.";
RL J. Biol. Chem. 269:18295-18298(1994).
CC -!- FUNCTION: CHH is the most abundant hormone in the sinus gland of
CC isopods and decapods which controls the blood sugar level. Has a
CC secretagogue action over the amylase released from the midgut gland.
CC May act as a stress hormone.
CC -!- FUNCTION: MIH may inhibit Y-organs where molting hormone (ecdysteroid)
CC is secreted and a molting cycle is initiated when MIH secretion
CC diminishes or stops.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Produced by the medulla terminalis X-organ in the
CC eyestalks and transported to the sinus gland where they are stored and
CC released. Present also in the ventral nervous system.
CC -!- PTM: Stereoinversion of L-Phe (form CHH-A-I) to D-Phe (form CHH-A-II).
CC {ECO:0000269|PubMed:8034574}.
CC -!- SIMILARITY: Belongs to the arthropod CHH/MIH/GIH/VIH hormone family.
CC {ECO:0000305}.
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DR EMBL; S76846; AAB32871.1; -; mRNA.
DR EMBL; X54842; CAA38611.1; -; mRNA.
DR PIR; S52117; S52117.
DR AlphaFoldDB; P19806; -.
DR SMR; P19806; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005184; F:neuropeptide hormone activity; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.10.2010.10; -; 1.
DR InterPro; IPR018251; Crust_neurhormone_CS.
DR InterPro; IPR031098; Crust_neurohorm.
DR InterPro; IPR035957; Crust_neurohorm_sf.
DR InterPro; IPR001166; Hyperglycemic.
DR InterPro; IPR000346; Hyperglycemic1.
DR PANTHER; PTHR35981; PTHR35981; 1.
DR Pfam; PF01147; Crust_neurohorm; 1.
DR PRINTS; PR00548; HYPRGLYCEMC1.
DR PRINTS; PR00550; HYPRGLYCEMIC.
DR SUPFAM; SSF81778; SSF81778; 1.
DR PROSITE; PS01250; CHH_MIH_GIH; 1.
PE 1: Evidence at protein level;
KW Amidation; Carbohydrate metabolism; Cleavage on pair of basic residues;
KW D-amino acid; Direct protein sequencing; Disulfide bond;
KW Glucose metabolism; Hormone; Neuropeptide; Pyrrolidone carboxylic acid;
KW Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT PEPTIDE 25..58
FT /note="CHH precursor-related peptide A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000019039"
FT PEPTIDE 61..132
FT /note="Crustacean hyperglycemic hormone A"
FT /id="PRO_0000019040"
FT MOD_RES 61
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:8034574"
FT MOD_RES 63
FT /note="D-phenylalanine; in form CHH-A-II"
FT /evidence="ECO:0000269|PubMed:8034574"
FT MOD_RES 132
FT /note="Valine amide"
FT /evidence="ECO:0000269|PubMed:1879416"
FT DISULFID 67..103
FT /evidence="ECO:0000250"
FT DISULFID 83..99
FT /evidence="ECO:0000250"
FT DISULFID 86..112
FT /evidence="ECO:0000250"
FT CONFLICT 91
FT /note="R -> RR (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="W -> S (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="D -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="G -> P (in Ref. 2; CAA38611)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 134 AA; 14996 MW; 089A4491BE40DD70 CRC64;
MMACRTLCLV VVMVASLGTS GVGGRSVEGA SRMEKLLSSS NSPSSTPLGF LSQDHSVNKR
QVFDQACKGV YDRNLFKKLD RVCEDCYNLY RKPFVATTCR ENCYSNWVFR QCLDDLLLSD
VIDEYVSNVQ MVGK
