PRTGB_DANRE
ID PRTGB_DANRE Reviewed; 1069 AA.
AC Q2EY13;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Protogenin B;
DE Flags: Precursor; Fragment;
GN Name=prtgb {ECO:0000312|ZFIN:ZDB-GENE-060302-1};
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:ABC96183.1}
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: Initially expressed in the ventral forebrain and
CC ventral spinal cord. Later, also expressed in the midbrain and in parts
CC of the diencephalon and hindbrain. {ECO:0000269|PubMed:16881056}.
CC -!- DEVELOPMENTAL STAGE: Expression is detected between the 10 s and 48
CC hour post-fertilization stages. {ECO:0000269|PubMed:16881056}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. DCC family.
CC {ECO:0000255}.
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DR EMBL; DQ360116; ABC96183.1; -; mRNA.
DR AlphaFoldDB; Q2EY13; -.
DR SMR; Q2EY13; -.
DR STRING; 7955.ENSDARP00000059192; -.
DR PaxDb; Q2EY13; -.
DR PRIDE; Q2EY13; -.
DR ZFIN; ZDB-GENE-060302-1; prtgb.
DR eggNOG; KOG4221; Eukaryota.
DR InParanoid; Q2EY13; -.
DR PhylomeDB; Q2EY13; -.
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 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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1069
FT /note="Protogenin B"
FT /evidence="ECO:0000255"
FT /id="PRO_5000141194"
FT TOPO_DOM 27..936
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 937..957
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 958..1069
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..117
FT /note="Ig-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 122..208
FT /note="Ig-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 221..308
FT /note="Ig-like 3"
FT /evidence="ECO:0000255"
FT DOMAIN 312..396
FT /note="Ig-like 4"
FT /evidence="ECO:0000255"
FT DOMAIN 406..500
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 502..601
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 608..701
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..904
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 317..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 618
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 834
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 143..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 242..290
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 333..380
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT NON_TER 1069
FT /evidence="ECO:0000312|EMBL:ABC96183.1"
SQ SEQUENCE 1069 AA; 117548 MW; 9FE80370D7CAF40E CRC64;
MGSVRWKTHQ QWLIIFWILS FSGVFGFSEL WFSIEPQDVS VSAGQHVVLD CQAGGESPVS
VRWRENGVQI QESECVRLLS NGSLCVSNLT QQRDEGYYQC VANNQYGAII SHRARLTITG
VLVFSAHPVP LELRLGSVAR FSCAVNRSPA DISWEINQRS LPQDSDRITV LPNGVLQIRN
VTMRDAGKYR CVAANAASRV TSREAELVLI PVGGPRRLLK PLIIAGPQNI SVALHQPVVL
ECLAEGNPRP LVSWSRADSK PIDVSAASVL GNGNLMISAV KAHHSGTYVC RATTPGTRNY
TTAAGNVTVL PPSLVEKPES QTRPRAGTAR FSCQAEGTPT PQITWFKNGE VIRTNGRTKM
YNNKLVITQI IPEDDAFYQC LAENSQGSVV STSRLIVVQS ENRPSAPRNI HAETISSSAI
LLAWERPQYN ADKVIAYSIH YMKSEGLNNE EYQAVIGNDT TSHIVDDLEP ARNYTFYIVA
YMAMGASRMS EQVTRHTLED VPLRTPELSL TSRSPTDILV SWQPLPPKLS RGRVSAYRLS
YRTATDEQVN SVELPVSGEN GTQYLLQDLQ PDTIYLIRMS VSTRVGWSQP SAWSSHRTPK
TSSATVPPAP NLELEPLNCT SVSVRWFPAA SDVLIQGFKL SFHPDGQSED SITQLPPQDH
QHTITALNPR VKYHVKVLAF SANGDGYQAH QTVNTPGCPS TPNRRLAALP PPDHTHAKAN
SSSAVHLSWG RPAFSSGKPV TFSVRYGPAS PSEASSVRYI QTSEQTVMVT GLQPNTRYEF
AVRLHMDQMS SPWSATVYQR TLLEAPMSPP ESVKVTLIEA DTALVCWKQP NQPNLSVTHY
TVLYASQSSW LAGEWQVLQR EGTNTMALLE KLESGNVYLV KISASNLAGD GPFSNTVELA
VKGKPHHGKN PRHADSHAEK TAFIDGLYHI DEKSMSGIIV GVCIALSCII LCIFILLSKT
QTQKSASSKM IGSMRNEVMH NEASSANQQP AENAEVLLPM MRNHFIDAKG GSNLLINHAG
PINCGSQTKR KRWSIFNHSQ RSNESKNETE DPACLYEVGK TVLCYEDEA
