ID A0A452J1F8_9SAUR Unreviewed; 138 AA.
AC A0A452J1F8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Calcitonin peptide-like domain-containing protein {ECO:0000259|SMART:SM00113};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000034215.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000034215.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the calcitonin family.
CC {ECO:0000256|ARBA:ARBA00009222}.
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DR AlphaFoldDB; A0A452J1F8; -.
DR Ensembl; ENSGAGT00000038742.1; ENSGAGP00000034215.1; ENSGAGG00000024303.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR InterPro; IPR021118; Calcitonin.
DR InterPro; IPR021117; Calcitonin-like.
DR InterPro; IPR021116; Calcitonin/adrenomedullin.
DR InterPro; IPR018360; Calcitonin_CS.
DR InterPro; IPR001693; Calcitonin_peptide-like.
DR PANTHER; PTHR10505:SF16; CALCITONIN; 1.
DR PANTHER; PTHR10505; CALCITONIN-RELATED; 1.
DR Pfam; PF00214; Calc_CGRP_IAPP; 1.
DR PRINTS; PR00270; CALCITONINA.
DR SMART; SM00113; CALCITONIN; 1.
DR PROSITE; PS00258; CALCITONIN; 1.
PE 3: Inferred from homology;
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR621116-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..138
FT /note="Calcitonin peptide-like domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019317906"
FT DOMAIN 80..117
FT /note="Calcitonin peptide-like"
FT /evidence="ECO:0000259|SMART:SM00113"
FT DISULFID 82..88
FT /evidence="ECO:0000256|PIRSR:PIRSR621116-50"
SQ SEQUENCE 138 AA; 15369 MW; DFC54F50252B3072 CRC64;
MVMLKISPFL AVYALVMCQM DSSQATPLRP GLDSITDRVT LSDYEARRLL NALVKEFVQM
RAEDVEQETE GNSLDKPISK RCASLSTCVL GKLSQELHKL QTYPRTDVGA GTPGKKRNVL
NDLENERYAN YGESLGNN
//
