RECK_CHICK
ID RECK_CHICK Reviewed; 963 AA.
AC A0A1D5PUP4; A0A1D5PTW4;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Reversion-inducing cysteine-rich protein with Kazal motifs {ECO:0000303|PubMed:23329048};
DE Flags: Precursor;
GN Name=RECK {ECO:0000303|PubMed:23329048};
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].
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 SUBCELLULAR LOCATION, AND GPI-ANCHOR.
RX PubMed=23329048; DOI=10.1126/science.1231921;
RA Park S., Lee C., Sabharwal P., Zhang M., Meyers C.L., Sockanathan S.;
RT "GDE2 promotes neurogenesis by glycosylphosphatidylinositol-anchor cleavage
RT of RECK.";
RL Science 339:324-328(2013).
CC -!- FUNCTION: Functions together with ADGRA2 to enable brain endothelial
CC cells to selectively respond to Wnt7 signals (WNT7A or WNT7B) (By
CC similarity). Plays a key role in Wnt7-specific responses: required for
CC central nervous system (CNS) angiogenesis and blood-brain barrier
CC regulation (By similarity). Acts as a Wnt7-specific coactivator of
CC canonical Wnt signaling by decoding Wnt ligands: acts by interacting
CC specifically with the disordered linker region of Wnt7, thereby
CC conferring ligand selectivity for Wnt7. ADGRA2 is then required to
CC deliver RECK-bound Wnt7 to frizzled by assembling a higher-order RECK-
CC ADGRA2-Fzd-LRP5-LRP6 complex. Also acts as a serine protease inhibitor
CC (By similarity). {ECO:0000250|UniProtKB:O95980,
CC ECO:0000250|UniProtKB:Q9Z0J1}.
CC -!- SUBUNIT: Interacts (via knot repeats) with WNT7A (via disordered linker
CC region); the interaction is direct (By similarity). Interacts (via knot
CC repeats) with WNT7B (via disordered linker region); the interaction is
CC direct (By similarity). Interacts with ADGRA2; the interaction is
CC direct (By similarity). {ECO:0000250|UniProtKB:O95980}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23329048};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:23329048}.
CC -!- DOMAIN: The Kazal-like domains mediate the serine protease inhibitor
CC activity. {ECO:0000250|UniProtKB:O95980}.
CC -!- PTM: Localizes to the plasma membrane via its GPI-anchor
CC (PubMed:23329048). Released from the plasma membrane following cleavage
CC of the GPI-anchor by GDPD5/GPE2 (PubMed:23329048).
CC {ECO:0000269|PubMed:23329048}.
CC -!- SIMILARITY: Belongs to the RECK family. {ECO:0000305}.
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DR EMBL; AADN04000072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_418897.4; XM_418897.5.
DR AlphaFoldDB; A0A1D5PUP4; -.
DR SMR; A0A1D5PUP4; -.
DR STRING; 9031.ENSGALP00000020581; -.
DR Ensembl; ENSGALT00000060231; ENSGALP00000056648; ENSGALG00000036829.
DR GeneID; 420804; -.
DR KEGG; gga:420804; -.
DR CTD; 8434; -.
DR VEuPathDB; HostDB:geneid_420804; -.
DR eggNOG; KOG3649; Eukaryota.
DR GeneTree; ENSGT00390000018540; -.
DR OMA; IPCCEYS; -.
DR OrthoDB; 620790at2759; -.
DR Reactome; R-GGA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR PRO; PR:A0A1D5PUP4; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000036829; Expressed in spermatocyte and 13 other tissues.
DR ExpressionAtlas; A0A1D5PUP4; baseline and differential.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IEA:UniProt.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:1990909; C:Wnt signalosome; ISS:UniProtKB.
DR GO; GO:1904928; F:coreceptor activity involved in canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0001955; P:blood vessel maturation; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:1904684; P:negative regulation of metalloendopeptidase activity; ISS:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0045765; P:regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0090210; P:regulation of establishment of blood-brain barrier; ISS:UniProtKB.
DR GO; GO:0002040; P:sprouting angiogenesis; IBA:GO_Central.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR039016; RECK.
DR PANTHER; PTHR13487; PTHR13487; 1.
DR Pfam; PF07648; Kazal_2; 3.
DR SMART; SM00280; KAZAL; 3.
DR SUPFAM; SSF100895; SSF100895; 3.
DR PROSITE; PS00282; KAZAL_1; 1.
DR PROSITE; PS51465; KAZAL_2; 3.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Protease inhibitor; Reference proteome; Repeat;
KW Serine protease inhibitor; Signal; Wnt signaling pathway.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..936
FT /note="Reversion-inducing cysteine-rich protein with Kazal
FT motifs"
FT /evidence="ECO:0000255"
FT /id="PRO_5008927880"
FT PROPEP 937..963
FT /evidence="ECO:0000255"
FT /id="PRO_0000445619"
FT REPEAT 31..78
FT /note="Knot 1"
FT /evidence="ECO:0000250|UniProtKB:O95980"
FT REPEAT 98..135
FT /note="Knot 2"
FT /evidence="ECO:0000250|UniProtKB:O95980"
FT REPEAT 145..191
FT /note="Knot 3"
FT /evidence="ECO:0000250|UniProtKB:O95980"
FT REPEAT 210..257
FT /note="Knot 4"
FT /evidence="ECO:0000250|UniProtKB:O95980"
FT REPEAT 286..332
FT /note="Knot 5"
FT /evidence="ECO:0000250|UniProtKB:O95980"
FT DOMAIN 621..667
FT /note="Kazal-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 692..746
FT /note="Kazal-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 749..783
FT /note="Kazal-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT REGION 31..332
FT /note="5 X Knot repeats"
FT /evidence="ECO:0000250|UniProtKB:O95980"
FT SITE 631..632
FT /note="Reactive bond"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 712..713
FT /note="Reactive bond"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT SITE 749..750
FT /note="Reactive bond"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT LIPID 936
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 627..652
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 629..648
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 637..665
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 710..729
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 718..744
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 755..781
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ SEQUENCE 963 AA; 105701 MW; D8097472E1E1E0DF CRC64;
MAAAVAAWPW ALFCLAAVPP LLSPGAAGLS CCYHAKDNLM CRDVCEQILS SKSDSRLKHL
LQRAPEYCPE SMGEVWGCIN SSLPGVLKKS DGWVGLGCCE LAIAVECRQA CKQASSKNDI
LKVCRKEYEN ALFSCINRNE MGSICCSYAG HHTNCREYCQ AIFRTDSSPG PSQIKAVENY
CASISPQLIH CVNNYTQSYP MRNPTDSLYC CDRAEDYACQ TACKRILMSM KTELEIVDGL
IEGCKTMPLP QDPLWQCFLE SSRSVHPGVT VHPPPSTGLD GAKLHCCSKA NSSTCRELCT
KLYSTSWGSS QSWQEFDRFC EYNAVEVSML TCLADVREPC QLGCRNLSYC TNFNNRPTEL
FRSCNSQSDQ GAMNDMKLWE KGSIKMPFIN IPVLDINKCQ PEMWKAIACS LQIKPCHSKS
RGSIICKSDC VEILKKCGDH NKFPEGHTAE SICELLSPTD DLENCIPLDT YLSPSSLGNI
VEDVTHPCNP NPCAANQLCE VNRKGCQSGE LCLPYLCVPG CKLGEASDFI VRQGTLIQVP
SSAGDVGCYK ICTCGHTGLL ENCVEMHCVD LQKSCIVGGQ KKSHGTSFNI DCNVCSCFAG
NLICSTRQCL TEHSSEDERQ KFTGLPCNCV DQFVPVCGQN GRTYPSACIA RCVGLQDNQF
EFGSCISKDP CNPNPCSKNQ RCIPKKQVCL TSFGKFECSQ HECVPRQLNC DQTQDPVCDT
DSVEYSNVCT LYQKGKNLAY RGPCQPFCKS VEPVCGHNGE TYSSVCAAYS DRVAVDYYGH
CQAVGVLSDY GFHTECAFVK CPQLSATGCK PVIAPGACCP LCAGMLRILY DKDKLDNFAR
VTNKKPITVL DILEKLRLHV SVPQCDVFGY LSIESEIVIL IIPVDQKPKP LQIEACNKEA
EKIESLINSD SPTLASHVPL SALIASQVQV SFSISSPSVK VGPVLHCLFI SFSFTLLKLM
DYI
