ID   ILP_BRACL               Reviewed;         305 AA.
AC   P22334;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Insulin-like peptide;
DE   Contains:
DE     RecName: Full=Insulin-like peptide B chain;
DE   Contains:
DE     RecName: Full=Insulin-like peptide A chain;
DE   Flags: Precursor;
GN   Name=ILP;
OS   Branchiostoma californiense (California lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomidae; Branchiostoma.
OX   NCBI_TaxID=7738;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1701257; DOI=10.1073/pnas.87.23.9319;
RA   Chan S.J., Cao Q.-P., Steiner D.F.;
RT   "Evolution of the insulin superfamily: cloning of a hybrid insulin/insulin-
RT   like growth factor cDNA from amphioxus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:9319-9323(1990).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; M55302; AAA62720.1; -; mRNA.
DR   PIR; A38422; A38422.
DR   AlphaFoldDB; P22334; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd04367; IlGF_insulin_like; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR036438; Insulin-like_sf.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cleavage on pair of basic residues;
KW   Disulfide bond; Glucose metabolism; Hormone; Secreted; Signal.
FT   SIGNAL          1..22
FT   PEPTIDE         23..49
FT                   /note="Insulin-like peptide B chain"
FT                   /id="PRO_0000015734"
FT   PROPEP          52..76
FT                   /note="Connecting peptide"
FT                   /id="PRO_0000015735"
FT   PEPTIDE         81..101
FT                   /note="Insulin-like peptide A chain"
FT                   /id="PRO_0000015736"
FT   PROPEP          102..305
FT                   /note="D/E peptide"
FT                   /id="PRO_0000015737"
FT   REGION          102..114
FT                   /note="D"
FT   REGION          107..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..305
FT                   /note="E"
FT   REGION          236..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..305
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        28..87
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        40..100
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        86..91
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   305 AA;  34605 MW;  EE7864E7E9DAA5E8 CRC64;
     MNLSSVYVLA SLAVVCLLVK ETQAEYLCGS TLADVLSFVC GNRGYNSQPR RSVSKRAIDF
     ISEQQAKDYM GAMPHIRRRR GLVEECCYNV CDYSQLESYC NPYSTAPATA TPVRTTEPQP
     EEAEDDPLDG MVGDQAPLGS IENIENLVYH YDSDDITIDA AKMEPKKLKE ILGSFEDKKA
     NPVFPFIRQS KNIKPNKFPD SFAHQFPTDL VEEEPTNEIP ESPSQKPTLE RLGYKHNQTD
     KKEPTENNNN NNRARDNRTK SSTVEPHTVP DYISKQYTHK PLITLPRGTP RRIESRDSYH
     LTELR