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PRTG_RAT
ID   PRTG_RAT                Reviewed;        1193 AA.
AC   Q2VWP9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Protogenin;
DE   AltName: Full=Protein Shen-Dan;
DE   Flags: Precursor;
GN   Name=Prtg {ECO:0000250|UniProtKB:Q2EY15};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000312|EMBL:AAU05739.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Neural tube {ECO:0000312|EMBL:AAU05739.1};
RA   Wong Y.-H., Chang C., Chen P.-H., Yu J.-Y., Wang Y.-C., Lee C.-M.,
RA   Lin W.-J., Tsai T.-F., Wang A.-G., Fann M.-J.;
RT   "Shen-Dan is a novel receptor for embryonic stem cells and developing
RT   neurons.";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. DCC family.
CC       {ECO:0000255}.
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DR   EMBL; AY630256; AAU05739.1; -; mRNA.
DR   RefSeq; NP_001032740.1; NM_001037651.1.
DR   AlphaFoldDB; Q2VWP9; -.
DR   SMR; Q2VWP9; -.
DR   STRING; 10116.ENSRNOP00000036541; -.
DR   GlyGen; Q2VWP9; 3 sites.
DR   PaxDb; Q2VWP9; -.
DR   GeneID; 315806; -.
DR   KEGG; rno:315806; -.
DR   UCSC; RGD:1307157; rat.
DR   CTD; 283659; -.
DR   RGD; 1307157; Prtg.
DR   eggNOG; KOG4221; Eukaryota.
DR   InParanoid; Q2VWP9; -.
DR   OrthoDB; 1010015at2759; -.
DR   PhylomeDB; Q2VWP9; -.
DR   PRO; PR:Q2VWP9; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0038023; F:signaling receptor activity; ISO:RGD.
DR   GO; GO:0007411; P:axon guidance; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0050768; P:negative regulation of neurogenesis; ISO:RGD.
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; 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..1193
FT                   /note="Protogenin"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000317048"
FT   TOPO_DOM        24..944
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        945..965
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        966..1193
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          24..124
FT                   /note="Ig-like 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          126..217
FT                   /note="Ig-like 2"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          230..317
FT                   /note="Ig-like 3"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          322..406
FT                   /note="Ig-like 4"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          416..510
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          512..608
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          613..712
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          719..812
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          817..912
FT                   /note="Fibronectin type-III 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          974..1018
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1078..1193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        974..991
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1078..1109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1110..1130
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1131..1152
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        238
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        625
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        54..107
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        150..200
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        251..299
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        343..390
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   1193 AA;  131080 MW;  8936A811894236C8 CRC64;
     MAPPVRPGML PLLLLLLLPP LGSVPGVWSF SELFFMKEPQ DATVTRKDPV FLDCQAHGEG
     PIKVTWLKNG AKLSENKRIQ VLSNGSLYIS EAEGRRGEQS DEGFYQCLAV NKYGAILSQK
     AHLTLSTISA FEVHPVSTEV PEGGVARFSC KISSTPPAVI TWEFNRTALP MTMDSRVTAL
     PSGVLQIYDA GPEDAGKYRC VAATHAHKRK SMEASLTIVP ANETRSFYMP TIIASPQNVT
     ASLHQTVVLE CMATGYPKPI ISWSRLDHKS IDVFNTRVLG NGNLIISDVK LQHAGVYVCR
     ATTPGTRNFT VAMATLTVLA PPSFVEWPES LTRPRAGTAR FVCQAEGIPS PKMSWLKNGR
     RIHSNGRIKM YNSKLVINQI IPEDDAIYQC MAENSQGSVL SRARLTVVMS EDRPSAPYNV
     HAETMSSSAI LLAWERPLYN SDKVIAYSVH YMKAEGLNNE EYQVVLGNDT THYIIDDLEP
     DSNYTFYIVA YMPMGASQMS DHVTQNTLED VPLRPPEISL TSRSPTDILI SWLPIPAKYR
     RGQVVLYRLS FRLSTENSIQ VVELPGTVHE YLLEGLEPDS VYLVRITAAT RVGLGESSVW
     TSHRTPKATS VKAPKSPELH LEPLNCTTIS VRWLQDTEDP AAIRGYKLFY KEEGQQEHGP
     IFLDTGDLLY TLSGLDPRRK YHVRLLAYNN LEDGYQADQT VSTPGCVSVR DRMVPPPPPP
     HHLYAKANTS SSIFLHWRRP AFTTAQVINY TIRCNPVGLQ NASLVLYLQT SETHMLVQGL
     EPNTKYEFAV RLHVDQLSSP WSPVVYHTTL PEAPTGPPVG VKVTLIEDDT ALVSWKPPDG
     PETVVTRYTI LYASRKAWIA GEWQVLHREG AITMALLENL VAGNVYIVKI SASNEVGEGP
     FPNSVELAVL PKDASESNQR PKRLDSSDAK VYSGYYHLDQ KSMTGIAVGV GIALTCILIC
     VLILIYRSKA RKSSASKTTQ SGTQPLSRAS ASVAAGSDMG KNLERATENE ESSVPMMPSC
     FIDAKGGTDL IINSYGPIIK NNPKKKWRFF QDTKKIKVEQ TQRRITQTVC FYQPGTTVLI
     SDEDSPSSPG QTTSFPRPFG PTTLDTEHSA NSEGSHETGD SGRFSHESND EIHLSSVISS
     TPPTSNSLTC GDSDGDAAPK KHGDPAQPLP AEQTSAPQPT PAGLRHAAES VPV
 
 
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