TKN1_CARAU
ID TKN1_CARAU Reviewed; 114 AA.
AC P25421; Q6LCG4;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 2.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Protachykinin;
DE AltName: Full=Gamma-preprotachykinin;
DE Short=Gamma-PPT;
DE Contains:
DE RecName: Full=Substance P;
DE Short=SP;
DE Contains:
DE RecName: Full=Neuropeptide gamma;
DE AltName: Full=Carassin;
DE Contains:
DE RecName: Full=Neurokinin A;
DE Short=NKA;
DE Contains:
DE RecName: Full=C-terminal-flanking peptide;
DE Flags: Precursor;
OS Carassius auratus (Goldfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Carassius.
OX NCBI_TaxID=7957;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9285930; DOI=10.1016/s0196-9781(97)00013-2;
RA Lin X.W., Peter R.E.;
RT "Goldfish gamma-preprotachykinin mRNA encodes the neuropeptides substance
RT P, carassin, and neurokinin A.";
RL Peptides 18:817-824(1997).
RN [2]
RP PROTEIN SEQUENCE OF 71-91, MASS SPECTROMETRY, AND AMIDATION AT MET-91.
RC TISSUE=Brain;
RX PubMed=2002352; DOI=10.1111/j.1471-4159.1991.tb11442.x;
RA Conlon J.M., O'Harte F., Peter R.E., Kah O.;
RT "Carassin: a tachykinin that is structurally related to neuropeptide-gamma
RT from the brain of the goldfish.";
RL J. Neurochem. 56:1432-1436(1991).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=2464008; DOI=10.1002/cne.902790109;
RA Sharma S.C., Berthoud V.M., Breckwoldt R.;
RT "Distribution of substance P-like immunoreactivity in the goldfish brain.";
RL J. Comp. Neurol. 279:104-116(1989).
RN [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=1381158; DOI=10.1007/bf00710401;
RA Vecino E., Sharma S.C.;
RT "The development of substance P-like immunoreactivity in the goldfish
RT brain.";
RL Anat. Embryol. (Berl.) 186:41-47(1992).
RN [5]
RP FUNCTION.
RX PubMed=1375097; DOI=10.1017/s0952523800005630;
RA Ayoub G.S., Matthews G.;
RT "Substance P modulates calcium current in retinal bipolar neurons.";
RL Vis. Neurosci. 8:539-544(1992).
RN [6]
RP FUNCTION.
RX PubMed=9095345; DOI=10.1016/s0166-4328(96)00166-0;
RA Mattioli R., Santangelo E.M., Costa A.C., Vasconcelos L.;
RT "Substance P facilitates memory in goldfish in an appetitively motivated
RT learning task.";
RL Behav. Brain Res. 85:117-120(1997).
RN [7]
RP FUNCTION.
RX PubMed=11486488; DOI=10.1155/np.2000.291;
RA Mattioli R., Huston J.P., Spieler R.E.;
RT "ACTH4-10, substance P, and dizolcipine (MK-801) accelerate functional
RT recovery after hemilabyrinthectomy in goldfish.";
RL Neural Plast. 7:291-301(2000).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=10764949; DOI=10.1016/s0196-9781(99)00190-4;
RA Peyon P., Saied H., Lin X., Peter R.E.;
RT "Preprotachykinin gene expression in goldfish brain: sexual, seasonal, and
RT postprandial variations.";
RL Peptides 21:225-231(2000).
RN [9]
RP FUNCTION.
RX PubMed=11311511; DOI=10.1016/s0304-3940(01)01698-6;
RA Santangelo E.M., Morato S., Mattioli R.;
RT "Facilitatory effect of substance P on learning and memory in the
RT inhibitory avoidance test for goldfish.";
RL Neurosci. Lett. 303:137-139(2001).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18445219; DOI=10.1111/j.1460-9568.2008.06210.x;
RA Thompson R.R., Walton J.C., Bhalla R., George K.C., Beth E.H.;
RT "A primitive social circuit: vasotocin-substance P interactions modulate
RT social behavior through a peripheral feedback mechanism in goldfish.";
RL Eur. J. Neurosci. 27:2285-2293(2008).
RN [11]
RP STRUCTURE BY NMR OF 71-91.
RX PubMed=12662361; DOI=10.1034/j.1399-3011.2003.00058.x;
RA Lee K., Lee S., Kim Y., Park N.G.;
RT "Structures of neuropeptide gamma from goldfish and mammalian neuropeptide
RT gamma, as determined by 1H NMR spectroscopy.";
RL J. Pept. Res. 61:274-285(2003).
CC -!- FUNCTION: Tachykinins are active peptides which excite neurons, evoke
CC behavioral responses, are potent vasodilators and secretagogues, and
CC contract (directly or indirectly) many smooth muscles.
CC -!- FUNCTION: Substance P produces a voltage-dependent inhibition of
CC calcium current in retinal bipolar cells. It can enhance learning and
CC memory, may regulate social approach and feeding behaviors, and can
CC accelerate the functional recovery in postural balance in response to
CC light after unilateral labyrinthectomy.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in all parts of the brain, with robust
CC expression in the olfactory bulbs and tracts, moderate expression in
CC the hypothalamus and posterior brain, and weak expression in the
CC telencephalon-preoptic region and optic tectum-thalamus. Also expressed
CC in nerve fibers, intestine, testes and pituitary gland. Not expressed
CC in the liver or kidneys. {ECO:0000269|PubMed:10764949,
CC ECO:0000269|PubMed:1381158, ECO:0000269|PubMed:18445219,
CC ECO:0000269|PubMed:2464008, ECO:0000269|PubMed:9285930}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the brain throughout development,
CC with expression first observable in the nascent diencephalon, olfactory
CC bulbs and hypothalamus shortly after fertilization.
CC {ECO:0000269|PubMed:1381158}.
CC -!- INDUCTION: Expression is induced in the hypothalamus and olfactory bulb
CC after feeding. {ECO:0000269|PubMed:10764949}.
CC -!- DOMAIN: Neuropeptide gamma contains alpha-helical structures at the C-
CC terminus which may be required for interaction with a cognate receptor.
CC -!- MASS SPECTROMETRY: [Neuropeptide gamma]: Mass=2384.2; Mass_error=2.4;
CC Method=Plasma desorption; Evidence={ECO:0000269|PubMed:2002352};
CC -!- SIMILARITY: Belongs to the tachykinin family. {ECO:0000305}.
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DR EMBL; U61272; AAB86991.1; -; mRNA.
DR PIR; JH0361; JH0361.
DR AlphaFoldDB; P25421; -.
DR Proteomes; UP000515129; Genome assembly.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:UniProtKB-KW.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0007217; P:tachykinin receptor signaling pathway; IEA:InterPro.
DR InterPro; IPR013055; Tachy_Neuro_lke_CS.
DR InterPro; IPR008215; Tachykinin_dom.
DR InterPro; IPR008216; Tachykinin_fam.
DR Pfam; PF02202; Tachykinin; 1.
DR PRINTS; PR01829; PROTACHYKNIN.
DR PROSITE; PS00267; TACHYKININ; 2.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Neuropeptide; Neurotransmitter; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..55
FT /evidence="ECO:0000255"
FT /id="PRO_0000391508"
FT PEPTIDE 57..67
FT /note="Substance P"
FT /id="PRO_5000145043"
FT PEPTIDE 71..91
FT /note="Neuropeptide gamma"
FT /id="PRO_5000145044"
FT PEPTIDE 82..91
FT /note="Neurokinin A"
FT /id="PRO_5000145045"
FT PEPTIDE 92..114
FT /note="C-terminal-flanking peptide"
FT /id="PRO_0000391509"
FT MOD_RES 67
FT /note="Methionine amide"
FT /evidence="ECO:0000255"
FT MOD_RES 91
FT /note="Methionine amide"
FT /evidence="ECO:0000269|PubMed:2002352"
SQ SEQUENCE 114 AA; 13495 MW; 6776134AAAA39541 CRC64;
MKFLLPSIVI FLVLCQVFGE ELGPKEDLDY WTGSNQVQDE WLQADPFREI IRRMTRKPRP
HQFIGLMGKR SPANAQITRK RHKINSFVGL MGKRSQEEPE SYEWGTVQIY DKRR
