PRTGA_DANRE
ID PRTGA_DANRE Reviewed; 1149 AA.
AC Q2EY14;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Protogenin A;
DE Flags: Precursor;
GN Name=prtga {ECO:0000312|ZFIN:ZDB-GENE-061204-4};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABC96182.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16881056; DOI=10.1002/dvdy.20898;
RA Vesque C., Anselme I., Couve E., Charnay P., Schneider-Maunoury S.;
RT "Cloning of vertebrate protogenin (Prtg) and comparative expression
RT analysis during axis elongation.";
RL Dev. Dyn. 235:2836-2844(2006).
CC -!- FUNCTION: May play a role in anteroposterior axis elongation.
CC {ECO:0000269|PubMed:16881056}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expression begins in the posterior region of the
CC embryo and this posterior restriction persists at the 4 s stage. At
CC early somite stages, expressed along the neural tube with lower levels
CC in the lateral and paraxial mesoderm. Expression decreases caudally and
CC rostrally becomes restricted to the ventral part of the brain.
CC Widespread in the spinal cord at 30 hours post-fertilization (hpf) and
CC is also expressed in the lens from this time. At 40 hpf, expression is
CC restricted to the lens. {ECO:0000269|PubMed:16881056}.
CC -!- DEVELOPMENTAL STAGE: Expression begins at 80% epiboly and is
CC extinguished by 48 hours post-fertilization.
CC {ECO:0000269|PubMed:16881056}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. DCC family.
CC {ECO:0000255}.
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DR EMBL; DQ360115; ABC96182.1; -; mRNA.
DR RefSeq; NP_001038495.1; NM_001045030.1.
DR AlphaFoldDB; Q2EY14; -.
DR SMR; Q2EY14; -.
DR PeptideAtlas; Q2EY14; -.
DR PRIDE; Q2EY14; -.
DR GeneID; 563834; -.
DR KEGG; dre:563834; -.
DR CTD; 563834; -.
DR ZFIN; ZDB-GENE-061204-4; prtga.
DR InParanoid; Q2EY14; -.
DR OrthoDB; 1010015at2759; -.
DR PhylomeDB; Q2EY14; -.
DR PRO; PR:Q2EY14; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IMP:MGI.
DR CDD; cd00063; FN3; 5.
DR Gene3D; 2.60.40.10; -; 9.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF00041; fn3; 5.
DR Pfam; PF07679; I-set; 3.
DR SMART; SM00060; FN3; 5.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 4.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 5.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 2: Evidence at transcript level;
KW Developmental protein; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1149
FT /note="Protogenin A"
FT /evidence="ECO:0000255"
FT /id="PRO_5000141193"
FT TOPO_DOM 24..932
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 933..953
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 954..1149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..117
FT /note="Ig-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 122..209
FT /note="Ig-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 222..309
FT /note="Ig-like 3"
FT /evidence="ECO:0000255"
FT DOMAIN 314..399
FT /note="Ig-like 4"
FT /evidence="ECO:0000255"
FT DOMAIN 408..502
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 504..600
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 605..704
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 711..804
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 809..905
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 646..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1086
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 753
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 143..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 243..291
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 335..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1149 AA; 126296 MW; 7DDDF460C361053F CRC64;
MASFKRDLYL FLAVFLSISG VWSFSELFFI KEPHDVTAMR RDAVVLDCQA HGEAPIGIRW
LKNGVTITES ERVYSLSNGS LLISEVESRK DKSDEGFYQC LAQNKYGSIL SQRARLTIAS
LSTFTQQPAS IIVMEGSVAR FTCKITATPP PIITWEFNRV TLPLATERIT VLPSGVLQIQ
GVEQRDAGSY RCVAANIVSR RRSTEATLTV TPAMSPRAPQ RPRIIAGPQN LTVPAHSTAL
LECMASGNPR PLISWSRADH KSIDVHKTKV LGNGNLIISD VNPQHAGIYF CRATTPGTRN
YTIAAANITV LAPPSLVEWP ESVTRPRAGT ARFVCTAEGF PTPQITWLKN GEPVRSNGRI
KMYNSKLVIN QIIPEDDGIY QCEAENIQGS VLAMARLIVV MSDNRPSAPR NIRADTVSSS
AIVLAWDRPA YNSEKVIAYS VHYMKAEGLN NEEYQIVIGN DTTRYIIDDL EAGRNYTFYI
VAYMPMGASR MSDHVIQHTL EDVPLRAPEL SLTSRSPSDI QVSWQPLSHK LSRGRVSAYR
LSYRTSSDGT LTQLELSAHK THQLLEGLQP DTTYLLRIAA ATAVGWGEPS AWSSHRTPKA
SSTKVPLAPE LQLESLNCTT VTLRWHLPAG SSSGLQGFKL SYHEEGQSEA AQAQIPPHHR
QHTIGGLDPR KKYHIKLLAF SFMGDGYQAD QTISTPGCVS VRDRLVPPPP PPHHVYAHSN
SSSSVFLHWA RPAFTSAQTL NYTVRCNPVG LQNASLVLYL QTAAQSLLVT DLEPNTNYEF
AVRLHVDLLS SPWSPVVYQT TLPEAPSRAP VGVKVTLIEG DSALVSWKAP DDRSAAAVTH
YTVLYATRRA WAAGDWQMLQ REGSITMALL ENLQPGQVYL VQVSASNQMG DGPFSAAVEL
TIHTDGHAHR THGFSHATVF SDGFYHLDQR SMAGIAVGVC IALTCIIICI LILACRSKTR
KSCTTKSIRQ AGGQTPPTAV RLANESAAES VEVMMPMMRD HFIDAKGGTN LIINSYGPVK
PNIEKKRRKR WSFFKKNEKE VKKVSSPAYS YHPGTTLLCY TETSPENPPT TLQGLFGPSG
GDSEGSHSSE GSHETSDSGR YSHDDTEATN VSIRSRPASL QDDGNQTPVH EKQLETTLQE
QEMTDLHPV
