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FARX_LYMST
ID   FARX_LYMST              Reviewed;         360 AA.
AC   P42565;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=FMRFamide-related neuropeptides;
DE   Contains:
DE     RecName: Full=EFFPL-amide;
DE   Contains:
DE     RecName: Full=GDPFLRF-amide 1;
DE   Contains:
DE     RecName: Full=GDPFLRF-amide 2;
DE   Contains:
DE     RecName: Full=GDPFLRF-amide 3;
DE   Contains:
DE     RecName: Full=GDPFLRF-amide 4;
DE   Contains:
DE     RecName: Full=GDPFLRF-amide 5;
DE   Contains:
DE     RecName: Full=GDPFLRF-amide 6;
DE   Contains:
DE     RecName: Full=GDPFLRF-amide 7;
DE   Contains:
DE     RecName: Full=SDPFLRF-amide 1;
DE   Contains:
DE     RecName: Full=SDPFLRF-amide 2;
DE   Contains:
DE     RecName: Full=SDPFLRF-amide 3;
DE   Contains:
DE     RecName: Full=SDPFLRF-amide 4;
DE   Contains:
DE     RecName: Full=SDPFLRF-amide 5;
DE   Contains:
DE     RecName: Full=SDPFLRF-amide 6;
DE   Contains:
DE     RecName: Full=SDPYLRF-amide;
DE   Contains:
DE     RecName: Full=SDPFFRF-amide;
DE   Contains:
DE     RecName: Full=SKPYMRF-amide;
DE   Contains:
DE     RecName: Full=SSFPRY-amide;
DE   Contains:
DE     RecName: Full=HDYMRF-amide;
DE   Flags: Precursor;
OS   Lymnaea stagnalis (Great pond snail) (Helix stagnalis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Lymnaeidae; Lymnaea.
OX   NCBI_TaxID=6523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT PHE-77; PHE-86; PHE-95;
RP   PHE-104; PHE-113; PHE-122; PHE-131; PHE-140; PHE-149; PHE-158; PHE-167;
RP   PHE-176; PHE-185; PHE-194; PHE-203; PHE-282; TYR-323 AND PHE-336.
RC   TISSUE=CNS;
RX   PubMed=7965060; DOI=10.1523/jneurosci.14-11-06564.1994;
RA   Kellett E., Saunders S.E., Li K.W., Staddon J.W., Benjamin P.R.,
RA   Burke J.F.;
RT   "Genomic organization of the FMRFamide gene in Lymnaea: multiple exons
RT   encoding novel neuropeptides.";
RL   J. Neurosci. 14:6564-6570(1994).
RN   [2]
RP   PARTIAL NUCLEOTIDE SEQUENCE.
RX   PubMed=2002360; DOI=10.1523/jneurosci.11-03-00740.1991;
RA   Saunders S.E., Bright K., Kellett E., Benjamin P.R., Burke J.F.;
RT   "Neuropeptides Gly-Asp-Pro-Phe-Leu-Arg-Phe-amide (GDPFLRFamide) and Ser-
RT   Asp-Pro-Phe-Leu-Arg-Phe-amide (SDPFLRFamide) are encoded by an exon 3' to
RT   Phe-Met-Arg-Phe-NH2 (FMRFamide) in the snail Lymnaea stagnalis.";
RL   J. Neurosci. 11:740-745(1991).
RN   [3]
RP   PARTIAL NUCLEOTIDE SEQUENCE.
RC   TISSUE=CNS;
RX   PubMed=1347559; DOI=10.1523/jneurosci.12-03-01033.1992;
RA   Saunders S.E., Kellett E., Bright K., Benjamin P.R., Burke J.F.;
RT   "Cell-specific alternative RNA splicing of an FMRFamide gene transcript in
RT   the brain.";
RL   J. Neurosci. 12:1033-1039(1992).
RN   [4]
RP   PROTEIN SEQUENCE OF 276-282 (SKPYMRF-AMIDE), AND AMIDATION AT PHE-203.
RX   PubMed=1421117; DOI=10.1097/00001756-199207000-00017;
RA   de With N.D., van der Schors R.C.;
RT   "SKPYMRFamide, a novel FMRFamide-related peptide in the snail Lymnaea
RT   stagnalis.";
RL   NeuroReport 3:612-614(1992).
CC   -!- FUNCTION: SDPFLRF-amide inhibits neurons.
CC   -!- FUNCTION: SKPYMRF-amide excites neurons.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Isoform 1 and isoform 2 only share the N-terminal signal
CC         sequence.;
CC       Name=2; Synonyms=FMRFamide-related;
CC         IsoId=P42565-1; Sequence=Displayed;
CC       Name=1; Synonyms=FMRFamide;
CC         IsoId=P19802-1; Sequence=External;
CC       Name=3;
CC         IsoId=P19802-2; Sequence=External;
CC   -!- TISSUE SPECIFICITY: Expressed in 57 cells including a cardiorespiratory
CC       cell and the visceral white interneuron (VWI).
CC   -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC       {ECO:0000305}.
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DR   EMBL; U03137; AAA62864.1; -; mRNA.
DR   EMBL; S38684; AAB21765.1; -; mRNA.
DR   PIR; G44840; G44840.
DR   AlphaFoldDB; P42565; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR002544; FMRFamid-related_peptide-like.
DR   InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR   Pfam; PF01581; FARP; 17.
DR   SUPFAM; SSF51120; SSF51120; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Amidation; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Neuropeptide; Repeat; Secreted; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   PROPEP          36..43
FT                   /id="PRO_0000009695"
FT   PEPTIDE         44..48
FT                   /note="EFFPL-amide"
FT                   /id="PRO_0000009696"
FT   PROPEP          49..70
FT                   /id="PRO_0000009697"
FT   PEPTIDE         71..77
FT                   /note="GDPFLRF-amide 1"
FT                   /id="PRO_0000009698"
FT   PEPTIDE         80..86
FT                   /note="GDPFLRF-amide 2"
FT                   /id="PRO_0000009699"
FT   PEPTIDE         89..95
FT                   /note="GDPFLRF-amide 3"
FT                   /id="PRO_0000009700"
FT   PEPTIDE         98..104
FT                   /note="GDPFLRF-amide 4"
FT                   /id="PRO_0000009701"
FT   PROPEP          106
FT                   /id="PRO_0000009702"
FT   PEPTIDE         107..113
FT                   /note="SDPFLRF-amide 1"
FT                   /id="PRO_0000009703"
FT   PEPTIDE         116..122
FT                   /note="GDPFLRF-amide 5"
FT                   /id="PRO_0000009704"
FT   PEPTIDE         125..131
FT                   /note="GDPFLRF-amide 6"
FT                   /id="PRO_0000009705"
FT   PEPTIDE         134..140
FT                   /note="SDPFLRF-amide 2"
FT                   /id="PRO_0000009706"
FT   PEPTIDE         143..149
FT                   /note="SDPFLRF-amide 3"
FT                   /id="PRO_0000009707"
FT   PEPTIDE         152..158
FT                   /note="SDPFLRF-amide 4"
FT                   /id="PRO_0000009708"
FT   PEPTIDE         161..167
FT                   /note="SDPFLRF-amide 5"
FT                   /id="PRO_0000009709"
FT   PEPTIDE         170..176
FT                   /note="SDPFLRF-amide 6"
FT                   /id="PRO_0000009710"
FT   PEPTIDE         179..185
FT                   /note="SDPYLRF-amide"
FT                   /id="PRO_0000009711"
FT   PEPTIDE         188..194
FT                   /note="GDPFLRF-amide 7"
FT                   /id="PRO_0000009712"
FT   PEPTIDE         197..203
FT                   /note="SDPFFRF-amide"
FT                   /id="PRO_0000009713"
FT   PROPEP          205..275
FT                   /evidence="ECO:0000269|PubMed:1421117"
FT                   /id="PRO_0000009714"
FT   PEPTIDE         276..282
FT                   /note="SKPYMRF-amide"
FT                   /id="PRO_0000009715"
FT   PROPEP          284..317
FT                   /id="PRO_0000009716"
FT   PEPTIDE         318..323
FT                   /note="SSFPRY-amide"
FT                   /id="PRO_0000009717"
FT   PROPEP          327..330
FT                   /id="PRO_0000009718"
FT   PEPTIDE         331..336
FT                   /note="HDYMRF-amide"
FT                   /id="PRO_0000009719"
FT   PROPEP          338..360
FT                   /id="PRO_0000009720"
FT   REGION          227..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          312..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..337
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         77
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:7965060"
FT   MOD_RES         86
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:7965060"
FT   MOD_RES         95
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:7965060"
FT   MOD_RES         104
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:7965060"
FT   MOD_RES         113
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:7965060"
FT   MOD_RES         122
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:7965060"
FT   MOD_RES         131
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:7965060"
FT   MOD_RES         140
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:7965060"
FT   MOD_RES         149
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:7965060"
FT   MOD_RES         158
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:7965060"
FT   MOD_RES         167
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:7965060"
FT   MOD_RES         176
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:7965060"
FT   MOD_RES         185
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:7965060"
FT   MOD_RES         194
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:7965060"
FT   MOD_RES         203
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:1421117,
FT                   ECO:0000269|PubMed:7965060"
FT   MOD_RES         282
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:7965060"
FT   MOD_RES         323
FT                   /note="Tyrosine amide"
FT                   /evidence="ECO:0000269|PubMed:7965060"
FT   MOD_RES         336
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:7965060"
SQ   SEQUENCE   360 AA;  41785 MW;  1593084FAE6542D2 CRC64;
     MKTWSHVALL ACLSIKWLTC VMADSIYCDD PDMCSNSVDL DRKEFFPLGR HDGVYQTPEE
     DGDLEDRQTR GDPFLRFGRG DPFLRFGRGD PFLRFGRGDP FLRFGQSDPF LRFGRGDPFL
     RFGRGDPFLR FGKSDPFLRF GRSDPFLRFG RSDPFLRFGK SDPFLRFGKS DPFLRFGKSD
     PYLRFGRGDP FLRFGRSDPF FRFGKQQVAT DDSGELDDEI LSRVSDDDKN IRRKRSTDSA
     ENAHTRHERE ASAPRAKGKV GEVKSSDDFQ SREIRSKPYM RFGRNNLNNY ALEDEDCKLT
     SDIIDDQFQR YQRGPSRSSF PRYGKRQDKR HDYMRFGRTS GGDFMGYDKS PENVGAEQSR
 
 
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