PTN_CHICK
ID PTN_CHICK Reviewed; 165 AA.
AC P32760; A0A1D5PB28;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Pleiotrophin {ECO:0000250|UniProtKB:P21246};
DE Short=PTN {ECO:0000250|UniProtKB:P21246};
DE AltName: Full=Heparin-binding brain mitogen {ECO:0000303|PubMed:2388713};
DE Short=HBBM {ECO:0000303|PubMed:2388713};
DE AltName: Full=Heparin-binding growth factor 8 {ECO:0000250|UniProtKB:P21782};
DE Short=HBGF-8 {ECO:0000250|UniProtKB:P21782};
DE AltName: Full=Heparin-binding growth-associated molecule {ECO:0000303|PubMed:1550956};
DE Short=HB-GAM {ECO:0000303|PubMed:1550956};
DE AltName: Full=Heparin-binding neutrophic factor {ECO:0000250|UniProtKB:P21246};
DE Short=HBNF {ECO:0000250|UniProtKB:P21246};
DE AltName: Full=Osteoblast-specific factor 1 {ECO:0000250|UniProtKB:P21246};
DE Short=OSF-1 {ECO:0000250|UniProtKB:P21246};
DE Flags: Precursor;
GN Name=PTN {ECO:0000250|UniProtKB:P21246};
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP PROTEIN SEQUENCE OF 31-165.
RX PubMed=1550956; DOI=10.1091/mbc.3.1.85;
RA Hampton B.S., Marshak D.R., Burgess W.H.;
RT "Structural and functional characterization of full-length heparin-binding
RT growth associated molecule.";
RL Mol. Biol. Cell 3:85-93(1992).
RN [3]
RP PROTEIN SEQUENCE OF 31-49.
RC TISSUE=Brain;
RX PubMed=2388713; DOI=10.1007/bf00969930;
RA Huber D., Gautschi-Sova P., Bohlen P.;
RT "Amino-terminal sequences of a novel heparin-binding protein from human,
RT bovine, rat, and chick brain: high interspecies homology.";
RL Neurochem. Res. 15:435-439(1990).
CC -!- FUNCTION: Secreted growth factor that mediates its signal through cell-
CC surface proteoglycan and non-proteoglycan receptors (By similarity).
CC Binds cell-surface proteoglycan receptor via their chondroitin sulfate
CC (CS) groups (By similarity). Thereby regulates many processes like cell
CC proliferation, cell survival, cell growth, cell differentiation and
CC cell migration (By similarity). {ECO:0000250|UniProtKB:P21246}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P21246}.
CC -!- SIMILARITY: Belongs to the pleiotrophin family. {ECO:0000305}.
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DR EMBL; AADN04000025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B60042; B60042.
DR RefSeq; NP_001263291.1; NM_001276362.1.
DR RefSeq; XP_015141094.1; XM_015285608.1.
DR RefSeq; XP_015141102.1; XM_015285616.1.
DR AlphaFoldDB; P32760; -.
DR SMR; P32760; -.
DR STRING; 9031.ENSGALP00000043473; -.
DR PaxDb; P32760; -.
DR PRIDE; P32760; -.
DR Ensembl; ENSGALT00000049974; ENSGALP00000049947; ENSGALG00000040493.
DR Ensembl; ENSGALT00000091282; ENSGALP00000066086; ENSGALG00000040493.
DR Ensembl; ENSGALT00000103339; ENSGALP00000065865; ENSGALG00000040493.
DR GeneID; 418125; -.
DR KEGG; gga:418125; -.
DR CTD; 5764; -.
DR VEuPathDB; HostDB:geneid_418125; -.
DR eggNOG; ENOG502RXV7; Eukaryota.
DR GeneTree; ENSGT00390000007640; -.
DR InParanoid; P32760; -.
DR OMA; PKWRERR; -.
DR OrthoDB; 1489280at2759; -.
DR PhylomeDB; P32760; -.
DR PRO; PR:P32760; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000040493; Expressed in cerebellum and 11 other tissues.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0035374; F:chondroitin sulfate binding; ISS:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; IDA:AgBase.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0030282; P:bone mineralization; ISA:AgBase.
DR GO; GO:0007420; P:brain development; IEP:AgBase.
DR GO; GO:0051216; P:cartilage development; IEP:AgBase.
DR GO; GO:0061054; P:dermatome development; IEP:AgBase.
DR GO; GO:0007507; P:heart development; IEP:AgBase.
DR GO; GO:0007612; P:learning; ISA:AgBase.
DR GO; GO:0060173; P:limb development; IEP:AgBase.
DR GO; GO:0021915; P:neural tube development; IEP:AgBase.
DR GO; GO:0001503; P:ossification; ISA:AgBase.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0010594; P:regulation of endothelial cell migration; IDA:UniProtKB.
DR GO; GO:0061056; P:sclerotome development; IEP:AgBase.
DR GO; GO:0043588; P:skin development; IEP:AgBase.
DR GO; GO:0001756; P:somitogenesis; IEP:AgBase.
DR GO; GO:0035989; P:tendon development; IEP:AgBase.
DR Gene3D; 2.20.60.10; -; 1.
DR Gene3D; 2.30.90.10; -; 1.
DR InterPro; IPR000762; Midkine_heparin-bd_GF.
DR InterPro; IPR020090; PTN/MK_C_dom.
DR InterPro; IPR038130; PTN/MK_C_dom_sf.
DR InterPro; IPR020091; PTN/MK_diS_sf.
DR InterPro; IPR020089; PTN/MK_N_dom.
DR InterPro; IPR037122; PTN/MK_N_dom_sf.
DR InterPro; IPR020092; PTN_MK_heparin-bd_GF_CS.
DR PANTHER; PTHR13850; PTHR13850; 1.
DR Pfam; PF01091; PTN_MK_C; 1.
DR Pfam; PF05196; PTN_MK_N; 1.
DR PRINTS; PR00269; PTNMIDKINE.
DR SMART; SM00193; PTN; 1.
DR SUPFAM; SSF57288; SSF57288; 2.
DR PROSITE; PS00619; PTN_MK_1; 1.
DR PROSITE; PS00620; PTN_MK_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Growth factor; Heparin-binding;
KW Mitogen; Reference proteome; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:1550956,
FT ECO:0000269|PubMed:2388713"
FT CHAIN 31..165
FT /note="Pleiotrophin"
FT /evidence="ECO:0000269|PubMed:1550956"
FT /id="PRO_0000164434"
FT REGION 90..97
FT /note="Chondroitin sulfate binding"
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT REGION 121..129
FT /note="Chondroitin sulfate binding"
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT REGION 137..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..165
FT /note="Chondroitin sulfate A binding"
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT COMPBIAS 144..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 45..74
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT DISULFID 53..83
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT DISULFID 60..87
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT DISULFID 97..129
FT /evidence="ECO:0000250|UniProtKB:P21246"
FT DISULFID 107..139
FT /evidence="ECO:0000250|UniProtKB:P21246"
SQ SEQUENCE 165 AA; 18513 MW; 19F6518E0DE6F1CE CRC64;
MPQQQQQRRM FTAALLALVF ILAAVSTTEA GKKEKPEKKA KKSDCGEWQW SVCVPTNGDC
GLGTREGTRT GAECKQTTKT QKCKIPCNWK KQFGAECKYQ FQAWGECDLN TALKTRTGNL
KRALHNADCQ KTVTISKPCG KLTKPKPQES KKKKKEGKKQ EKMLD