SDK2_CHICK
ID SDK2_CHICK Reviewed; 2177 AA.
AC Q8AV57;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Protein sidekick-2 {ECO:0000303|PubMed:12230981};
DE Flags: Precursor;
GN Name=SDK2 {ECO:0000303|PubMed:12230981};
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 [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=12230981; DOI=10.1016/s0092-8674(02)00910-8;
RA Yamagata M., Weiner J.A., Sanes J.R.;
RT "Sidekicks: synaptic adhesion molecules that promote lamina-specific
RT connectivity in the retina.";
RL Cell 110:649-660(2002).
RN [2]
RP FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=18216854; DOI=10.1038/nature06469;
RA Yamagata M., Sanes J.R.;
RT "Dscam and Sidekick proteins direct lamina-specific synaptic connections in
RT vertebrate retina.";
RL Nature 451:465-469(2008).
CC -!- FUNCTION: Adhesion molecule that promotes lamina-specific synaptic
CC connections in the retina (PubMed:12230981, PubMed:18216854). Expressed
CC in specific subsets of interneurons and retinal ganglion cells (RGCs)
CC and promotes synaptic connectivity via homophilic interactions
CC (PubMed:12230981, PubMed:18216854). {ECO:0000269|PubMed:12230981,
CC ECO:0000269|PubMed:18216854}.
CC -!- SUBUNIT: Homodimer; mediates homophilic interactions to promote cell
CC adhesion. {ECO:0000269|PubMed:12230981}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Synapse {ECO:0000269|PubMed:12230981}.
CC -!- TISSUE SPECIFICITY: Expressed by non-overlapping subsets of retinal
CC neurons (PubMed:12230981). SDK1, SDK2, DSCAM and DSCAML1 are expressed
CC in non-overlapping subsets of interneurons and retinal ganglion cells
CC (RGCs) that form synapses in distinct inner plexiform layer (IPL)
CC sublaminae (PubMed:18216854). {ECO:0000269|PubMed:12230981,
CC ECO:0000269|PubMed:18216854}.
CC -!- DOMAIN: the PDZ-binding motif mediates interaction with PDZ domain-
CC containing proteins and is required for is required for synaptic
CC localization in photoreceptors. {ECO:0000250|UniProtKB:Q6V4S5}.
CC -!- SIMILARITY: Belongs to the sidekick family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN15076.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF537108; AAN15076.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q8AV57; -.
DR SMR; Q8AV57; -.
DR STRING; 9031.ENSGALP00000007092; -.
DR PaxDb; Q8AV57; -.
DR PRIDE; Q8AV57; -.
DR VEuPathDB; HostDB:geneid_395215; -.
DR eggNOG; KOG3510; Eukaryota.
DR InParanoid; Q8AV57; -.
DR PhylomeDB; Q8AV57; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0060219; P:camera-type eye photoreceptor cell differentiation; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:UniProtKB.
DR GO; GO:0010842; P:retina layer formation; IDA:UniProtKB.
DR GO; GO:0007416; P:synapse assembly; IDA:UniProtKB.
DR CDD; cd00063; FN3; 13.
DR Gene3D; 2.60.40.10; -; 19.
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; 13.
DR Pfam; PF07679; I-set; 4.
DR SMART; SM00060; FN3; 13.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF49265; SSF49265; 7.
DR PROSITE; PS50853; FN3; 13.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..2177
FT /note="Protein sidekick-2"
FT /id="PRO_0000226980"
FT TOPO_DOM 27..1937
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1938..1958
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1959..2177
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..113
FT /note="Ig-like C2-type 1"
FT DOMAIN 118..205
FT /note="Ig-like C2-type 2"
FT DOMAIN 220..299
FT /note="Ig-like C2-type 3"
FT DOMAIN 313..401
FT /note="Ig-like C2-type 4"
FT DOMAIN 407..496
FT /note="Ig-like C2-type 5"
FT DOMAIN 501..590
FT /note="Ig-like C2-type 6"
FT DOMAIN 597..693
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 698..794
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 799..898
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 902..996
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1000..1099
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1104..1202
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1207..1304
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1305..1402
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1407..1504
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1509..1626
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1631..1727
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1731..1826
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1829..1928
FT /note="Fibronectin type-III 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 2044..2071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2103..2177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2171..2177
FT /note="PDZ-binding"
FT /evidence="ECO:0000250|UniProtKB:Q6V4S5"
FT COMPBIAS 2044..2064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2103..2134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2141..2155
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 709
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 748
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 809
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 941
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 953
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1675
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1694
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1746
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1820
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 242..289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 335..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 428..480
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 522..574
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 2177 AA; 239152 MW; A425D87BA8500893 CRC64;
MKGLGVPAAA LLWGGLSALL PPSLPADDVS PYFKTEPVRS QVHLEGNRLV LTCMAEGSWP
LEFKWLHNSR ELTKFSLEYR YMITSLDRTH AGFYRCIVRN RMGALLQRQT EVQVAYMGSF
EDSETQQSVS HGEAAVIRAP RIASFPQPQV TWFRDGRKIS PSSRIAITLE NTLVILSTVA
PDAGRYYVQA VNDKNGDNKT SQPITLTVAN VGGPADPIAP TIIVPPRNTS VVAGTSEVTM
ECVANARPLI KLHIIWKKDG VPISSGISDY SRRLTILNPT LGDSGYYECE AVLRSSSVPA
VAEGAYLSVL EPPQFVKEPE RHITAEMEKV VAIPCQAKGV PPPDMAWYKD ASLIHPEQLS
RFQLLADGSL QISGLLPDDT GMFQCFARNA AGEVQTTTYL AVTSIAPNIT RGPQDSTVID
GMSVILNCET SGAPRPAITW QKGERILASG SVQLPRFTLL ESGSLLVSPA HLTDAGTYTC
LATNSRGVDE ASADLVVWAR TRITDPPQDQ SVIKGTKASM SCGVTHDPSV DVRYIWEKDG
APLGTESGPR LRLDETGTLH ISQTWSGDIG TYTCKVLSAG GNDSRSAHLR VRQLPHAPES
PVAVLSPLEK RAINLTWAKP FDGNSPLLRY LVEISENNAP WTVLLASVDP ELTWVVVRGL
VPARSYQFRL CAVNDVGRSQ FSKDTERVSL PEEPPFAPPQ NVIASGRTNQ SIMIQWQPPP
ESHQNGVLKG YIIRYCLAGL PVGYQFKNIT NADVNNLLLE DLIIWTNYEI EVAAYNSAGL
GVYSMKVTEW TLQGVPTVPP GNVQTEATNS TTIRFTWNPP SPQFINGINQ GYKLIAWEPE
HEEEATVVTV RPNFQDSVHV GYVVGLKKFT EYLTSVLCFT TPGDGPRSPP QLVRTHEDVP
GPVGHLSFSE ILDTSLKVSW QEPLEKNGIL TGYRISWEEY NRTNTRVTHY LPNVTLEYRV
TGLTALTTYT IEVAAMTSKG QGQVSSSTIS SGVPPELPGA PTNLGISNIG PRSVTLQFRP
GYDGKTSISR WQVEAQVGQN GEAEEWGLVH QLANEPDARS LEVPNLNPYT YYSFRMRQVN
IVGTSPPSLP SRRIQTLQAP PDVAPANVTL RTASETSLWL RWMPLLEQEY NGNPDSVGYR
IRYLRSDGQG RAVVHVIHDR VEREYTIEDL EEWTEYRVQV QAFNAIGSGP WSHLVLGRTR
ESVPSSGPSN VSAQATSSSN MLVRWSDIPE ADCNGLILGY KVMFKEKDSE ARAQFWLAEG
NTSRSAQLTG LGKFMLYEIR VLAFTRIGDG VPSRPPILER TLDDVPGPPV GMLFPEVRTT
SVRLIWQPPT APNGIILAYQ LTHRLNTTTA NAAVSEVLGP STRQYTATGL QPEATYLFSI
TAQTRKGWGE AAEALVVTTE KRDRPQPPSK PLVRQEDVRA RSVLLSWEPG SDGLSPVRFY
TVQTRELPSG EWALHPASIS HNATAFVVDR LKPFTSYKFR VKATNDIGDS EYSEESESLT
TLQAAPEEAP TILSVTPHTT TSVLIRWQPP SEDKINGILL GFRLRYRELL YDSLRGFTLH
GIGNPGATWA ELTPVYAVHN LSEVSLTQYE LDNLSKHRRY EIRMSVYNAV GEGPPSPPQE
VFVGEAMPTG APQNVAVKAA TATQLDVTWE PPPTESQNGD IQGYKIHFWE AQRQNESARV
KTLFLPETGV KLKNLTGYTS YWVSIAAFNA AGDGPRSTPV TARTQQAAPS APGSIRFSEL
TTTSVNVSWE PPPLPNGILE GYRLVYEPCM PVDGVSKIVT VDVKGNSPLW MKVKDLAEGI
TYRFRIRAKT FAYGPDVEAN ITTGPGEGAP GPPGEPFISR YGSAITIHWT SGDPGQGPIT
RYVIEARPSD EGLWDILIKD IPKEVTSYTF SMDILKQGVS YDFRVIAVND YGYGTPSTPS
PSVSAQKANP FYEEWWFLVV IALVGLIFIL LLVFVLIIRG QSKKYAKKSD SGNGSKANAL
THGEMVSLDE SSFPALELNN RRLSVKNSFC RKNGIYTRSP PRPSPGSLHY SDEDVTKYND
LIPAESSSLT EKPSEVSDSQ GSDSEYEVDP AHQKAHSFVN HYISDPTYYN SWRRQQKGIS
RAQAYSYTES DSGEPDHTPL SNSTSTQQGS LFRPKASRIP TPQTPGNPPS QPGTLYRPPS
SLAPGSRAPI GGFSSFV
