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TKN4_RAT
ID   TKN4_RAT                Reviewed;         170 AA.
AC   Q8CH01;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Tachykinin-4;
DE   AltName: Full=Preprotachykinin-C;
DE            Short=PPT-C;
DE   Contains:
DE     RecName: Full=Hemokinin;
DE     AltName: Full=HK1;
DE     AltName: Full=Hemokinin-1;
DE     AltName: Full=Hemokinin-I;
DE              Short=HK-I;
DE   Flags: Precursor;
GN   Name=Tac4 {ECO:0000312|EMBL:AAS46597.1, ECO:0000312|RGD:628842};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000312|EMBL:AAN77129.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT MET-66.
RC   STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAN77129.1};
RX   PubMed=12383518; DOI=10.1016/s0378-1119(02)00861-2;
RA   Kurtz M.M., Wang R., Clements M.K., Cascieri M.A., Austin C.P.,
RA   Cunningham B.R., Chicchi G.G., Liu Q.;
RT   "Identification, localization and receptor characterization of novel
RT   mammalian substance P-like peptides.";
RL   Gene 296:205-212(2002).
RN   [2] {ECO:0000312|EMBL:AAS46597.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New England Deaconess Hospital {ECO:0000312|EMBL:AAS46597.1};
RA   Page N.M.;
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305}
RP   SYNTHESIS, AND FUNCTION.
RX   PubMed=11786503; DOI=10.1038/sj.bjp.0704443;
RA   Bellucci F., Carini F., Catalani C., Cucchi P., Lecci A., Meini S.,
RA   Patacchini R., Quartara L., Ricci R., Tramontana M., Giuliani S.,
RA   Maggi C.A.;
RT   "Pharmacological profile of the novel mammalian tachykinin, hemokinin 1.";
RL   Br. J. Pharmacol. 135:266-274(2002).
RN   [4] {ECO:0000305}
RP   SYNTHESIS, AND FUNCTION.
RX   PubMed=12044836; DOI=10.1016/s0024-3205(02)01682-x;
RA   Camarda V., Rizzi A., Calo G., Guerrini R., Salvadori S., Regoli D.;
RT   "Pharmacological profile of hemokinin 1: a novel member of the tachykinin
RT   family.";
RL   Life Sci. 71:363-370(2002).
RN   [5] {ECO:0000305}
RP   SYNTHESIS, AND FUNCTION.
RX   PubMed=16102736; DOI=10.1016/j.brainres.2005.07.020;
RA   Fu C.-Y., Kong Z.-Q., Wang K.-R., Yang Q., Zhai K., Chen Q., Wang R.;
RT   "Effects and mechanisms of supraspinal administration of rat/mouse
RT   hemokinin-1, a mammalian tachykinin peptide, on nociception in mice.";
RL   Brain Res. 1056:51-58(2005).
RN   [6] {ECO:0000305}
RP   SYNTHESIS, AND FUNCTION.
RX   PubMed=17628523; DOI=10.1016/j.ejphar.2007.06.014;
RA   Fu C.-Y., Kong Z.-Q., Long Y., Chen Q., Wang R.;
RT   "Cardiovascular responses to rat/mouse hemokinin-1, a mammalian tachykinin
RT   peptide: systemic study in anesthetized rats.";
RL   Eur. J. Pharmacol. 572:175-181(2007).
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. Hemokinin
CC       induces plasma extravasation, mast cell degranulation, muscle
CC       contraction, salivary secretion and scratching behavior. Increases
CC       sperm motility. Induces potent analgesic effects and may play a role in
CC       pain modulation. Promotes survival of bone marrow B lineage cells and
CC       of cultured LPS-stimulated pre-B cells and may act as an autocrine
CC       factor required for B-cell survival and proliferation. Lowers systemic
CC       arterial pressure following intravenous injection. Induces interferon-
CC       gamma production and may play a role in the inflammatory response.
CC       Shows potent affinity and specificity for the NK-1 receptor.
CC       {ECO:0000269|PubMed:11786503, ECO:0000269|PubMed:12044836,
CC       ECO:0000269|PubMed:16102736, ECO:0000269|PubMed:17628523}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the tachykinin family. {ECO:0000255}.
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DR   EMBL; AF521561; AAN77129.1; -; mRNA.
DR   EMBL; AY471575; AAS46597.1; -; mRNA.
DR   RefSeq; NP_758831.1; NM_172328.2.
DR   AlphaFoldDB; Q8CH01; -.
DR   STRING; 10116.ENSRNOP00000029541; -.
DR   PaxDb; Q8CH01; -.
DR   Ensembl; ENSRNOT00000035023; ENSRNOP00000029541; ENSRNOG00000004404.
DR   GeneID; 282829; -.
DR   KEGG; rno:282829; -.
DR   UCSC; RGD:628842; rat.
DR   CTD; 255061; -.
DR   RGD; 628842; Tac4.
DR   eggNOG; ENOG502TEEE; Eukaryota.
DR   GeneTree; ENSGT00390000015220; -.
DR   HOGENOM; CLU_133899_0_0_1; -.
DR   InParanoid; Q8CH01; -.
DR   OMA; YQLGRIV; -.
DR   OrthoDB; 1512743at2759; -.
DR   TreeFam; TF338519; -.
DR   PRO; PR:Q8CH01; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000004404; Expressed in esophagus and 11 other tissues.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0048018; F:receptor ligand activity; ISO:RGD.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR   GO; GO:0031837; F:substance K receptor binding; ISO:RGD.
DR   GO; GO:0031835; F:substance P receptor binding; ISO:RGD.
DR   GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IDA:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR   GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
DR   GO; GO:1904057; P:negative regulation of sensory perception of pain; ISO:RGD.
DR   GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; ISO:RGD.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:RGD.
DR   GO; GO:1902093; P:positive regulation of flagellated sperm motility; ISO:RGD.
DR   GO; GO:0046878; P:positive regulation of saliva secretion; ISO:RGD.
DR   GO; GO:1904058; P:positive regulation of sensory perception of pain; IDA:UniProtKB.
DR   GO; GO:0051930; P:regulation of sensory perception of pain; ISO:RGD.
DR   GO; GO:0007217; P:tachykinin receptor signaling pathway; ISO:RGD.
DR   InterPro; IPR013055; Tachy_Neuro_lke_CS.
DR   PROSITE; PS00267; TACHYKININ; 1.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Hypotensive agent;
KW   Mast cell degranulation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..54
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000320019"
FT   PEPTIDE         57..66
FT                   /note="Hemokinin"
FT                   /evidence="ECO:0000269|PubMed:12383518"
FT                   /id="PRO_0000320020"
FT   PROPEP          67..170
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000320021"
FT   REGION          107..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..147
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         66
FT                   /note="Methionine amide"
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:12383518"
SQ   SEQUENCE   170 AA;  18751 MW;  036845638A845567 CRC64;
     MLPLLALFLL IGPAVSTTTR DREDLTFGAE AESWVTVNLK GIPVPSIELK LQELKRSRTR
     QFYGLMGKRV EGVHPIQSAE RTGYQLGRIV QDLLGTRGLS IEGSCRQETN HQSAGPGAVA
     RESLQSQRGR SEPPNHQQHV ALSLGTEEDD QSSERAPRDA SQMMPRPSRP
 
 
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