PRTG_CHICK
ID PRTG_CHICK Reviewed; 1187 AA.
AC Q589G5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Protogenin;
DE Flags: Precursor;
GN Name=PRTG {ECO:0000250|UniProtKB:Q2EY15};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAD93619.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Midbrain {ECO:0000269|PubMed:15922677};
RX PubMed=15922677; DOI=10.1016/j.modgep.2005.04.001;
RA Toyoda R., Nakamura H., Watanabe Y.;
RT "Identification of protogenin, a novel immunoglobulin superfamily gene.";
RL Gene Expr. Patterns 5:778-785(2005).
RN [2] {ECO:0000305}
RP TISSUE SPECIFICITY.
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:0000250|UniProtKB:Q2EY15}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: In the embryo, expressed in early mesodermal cells,
CC the neuroepithelial layer of the brain and the trunk neural tube, the
CC neural layer of the retina and in the epithelial somite and
CC dermomyotome. From mid-gastrulation to early somite stages, restricted
CC to the posterior embryonic region but this posterior restriction is
CC progressively lost during somitogenesis. As development proceeds,
CC further restricted to the dorsal parts of the spinal cord and somites.
CC In parallel, expression progresses caudally during axis elongation.
CC {ECO:0000269|PubMed:15922677, ECO:0000269|PubMed:16881056}.
CC -!- DEVELOPMENTAL STAGE: Highest expression is found in E1-E3 embryos with
CC a significant decrease after E3.5. {ECO:0000269|PubMed:15922677}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. DCC family.
CC {ECO:0000255}.
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DR EMBL; AB185923; BAD93619.1; -; mRNA.
DR RefSeq; NP_001025719.1; NM_001030548.4.
DR AlphaFoldDB; Q589G5; -.
DR SMR; Q589G5; -.
DR STRING; 9031.ENSGALP00000006943; -.
DR PaxDb; Q589G5; -.
DR GeneID; 415407; -.
DR KEGG; gga:415407; -.
DR CTD; 283659; -.
DR VEuPathDB; HostDB:geneid_415407; -.
DR eggNOG; KOG4221; Eukaryota.
DR InParanoid; Q589G5; -.
DR OrthoDB; 1010015at2759; -.
DR PhylomeDB; Q589G5; -.
DR PRO; PR:Q589G5; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR CDD; cd00063; FN3; 5.
DR Gene3D; 2.60.40.10; -; 9.
DR InterPro; IPR043204; Basigin-like.
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 InterPro; IPR033011; Protogenin.
DR PANTHER; PTHR10075; PTHR10075; 1.
DR PANTHER; PTHR10075:SF75; PTHR10075:SF75; 1.
DR Pfam; PF00041; fn3; 5.
DR Pfam; PF07679; I-set; 2.
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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1187
FT /note="Protogenin"
FT /evidence="ECO:0000255"
FT /id="PRO_0000317049"
FT TOPO_DOM 28..941
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 942..962
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 963..1187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..122
FT /note="Ig-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 127..214
FT /note="Ig-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 227..314
FT /note="Ig-like 3"
FT /evidence="ECO:0000255"
FT DOMAIN 319..403
FT /note="Ig-like 4"
FT /evidence="ECO:0000255"
FT DOMAIN 413..507
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 509..605
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 610..709
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 716..809
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 814..909
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1103..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 725
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 746
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 758
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 148..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 248..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 340..387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1187 AA; 130515 MW; CA76A0587BD5041D CRC64;
MPAASRCMAL LRALLGALLL PMPGVWCFSE LFFVREPQDV TASRKDAVVL DCQARGEAPI
TVTWLKNGGK VSENERIYTL SNGSLYISEV EGRKGEQSDE GFYQCLALNK YGAILSQKSH
LTLATISAFE VQPLSTEVQE GGVARFTCKI AANPPAVVTW EVNRTTLPLS MDRITALPTG
VLQIYGVEQK DAGNYRCVAT TITSRRKSAE ATLNVIPASD LKPFHKPAII AGPQNVTASL
HQTVILECVA TGNPKPIISW SRLDHKSIDV FNTRVLGNGN LMISDVKVQH AGVYVCRATI
PGTRNFTVAM ATLTVLAPPS FVEWPESLTR PRAGTARFAC QAEGIPAPKI SWLKNGRRIH
SNGRIKMYNS KLVINQIIPE DDAIYQCMAE NSQGSVLSRA RLTVVMSEDR PSAPYNVHAE
TMSSSAILLA WERPLYNSDK VIAYSVHYMK AEGLNNEEYQ VVIGNDTTHY IIDDLEPASN
YTFYIVAYMP LGASQMSDHV TQHTLEDVPL RAPEISLTSR SPTDILISWL PIPAKYRRGQ
VVLYRLSFRL STDSKIQVLE LPGTSDEYLL EGLRPDSVYL VRITAATRIG WGEASLWTSH
RTPKATSVKA PKSPELRLEP INCTTITVQW QQDSDDTAAI QGYKLYYKEE GQQENGPILL
DASDLEYTVS GLDPRRKYHV RLLAYNNMEE GYQADQTVST PGCVSVRDRM VPPPPPPHHL
YAKANTSSSI YLHWGKPAFT SAQVINYTIR CNPVGLQNAS LVLYLQTSET HMLVQGLEPK
TMYEFAVRLH VDQLSSPWSP VVYHTTLPEA PSGPPVGVKV TLIEDDTALV SWKPPDGPET
VVTRYTILYA SRKSWIAGEW QVLHREGAMT MALLENLVAG NVYLVKIAAS NEVGEGPFSN
VVELAVLPKE TSESNQRPKR LDSGDSTAYS DYYHLDQKSM TGIVVGVCIA LTCILICILI
LIYRSKARKT SAPKPVQQST DQLSHTNISL ASANEVEKSI DGIAENAESL LPMIVGNSFI
DAKGGSDLII NSYGPVTKAN CKKRWLFFQD TKKMKTEEPQ RRFVQAVCLY QPGTTVLISE
DDSPSSPGQQ SNFQVPFSIA ADTEHSANSE GSHETGDSGR FSHESNDELH LSSVTSATPC
ATSHFVSSDL GKNVMNSTIS DSKESPLLFA TDQPATSPLQ IHSAVQN
