SDK1_CHICK
ID SDK1_CHICK Reviewed; 2169 AA.
AC Q8AV58;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Protein sidekick-1 {ECO:0000303|PubMed:12230981};
DE Flags: Precursor;
GN Name=SDK1 {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, SUBCELLULAR LOCATION, SUBUNIT, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Retina;
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 -!- SIMILARITY: Belongs to the sidekick family. {ECO:0000305}.
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DR EMBL; AF537107; AAN15075.1; -; mRNA.
DR AlphaFoldDB; Q8AV58; -.
DR SMR; Q8AV58; -.
DR STRING; 9031.ENSGALP00000007030; -.
DR PaxDb; Q8AV58; -.
DR PRIDE; Q8AV58; -.
DR VEuPathDB; HostDB:geneid_373894; -.
DR eggNOG; KOG3510; Eukaryota.
DR InParanoid; Q8AV58; -.
DR PhylomeDB; Q8AV58; -.
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: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; 3.
DR SMART; SM00060; FN3; 13.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 7.
DR PROSITE; PS50853; FN3; 13.
DR PROSITE; PS50835; IG_LIKE; 5.
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..50
FT /evidence="ECO:0000255"
FT CHAIN 51..2169
FT /note="Protein sidekick-1"
FT /id="PRO_0000226977"
FT TOPO_DOM 51..1961
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1962..1982
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1983..2169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 56..138
FT /note="Ig-like C2-type 1"
FT DOMAIN 143..229
FT /note="Ig-like C2-type 2"
FT DOMAIN 245..333
FT /note="Ig-like C2-type 3"
FT DOMAIN 338..428
FT /note="Ig-like C2-type 4"
FT DOMAIN 432..521
FT /note="Ig-like C2-type 5"
FT DOMAIN 525..615
FT /note="Ig-like C2-type 6"
FT DOMAIN 622..718
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 723..819
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 824..922
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 926..1020
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1024..1123
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1128..1226
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1231..1328
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1332..1426
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1431..1528
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1533..1651
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1656..1752
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1756..1851
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1854..1955
FT /note="Fibronectin type-III 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1423..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2028..2050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2145..2169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2163..2169
FT /note="PDZ-binding"
FT /evidence="ECO:0000250|UniProtKB:Q6V4S5"
FT COMPBIAS 1429..1443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 734
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 773
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 834
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 967
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 977
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1606
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1700
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1719
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1771
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1845
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 267..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 360..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 453..505
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 547..599
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 2169 AA; 239478 MW; 06BFD900AEF19BD7 CRC64;
MVGRKVDREI IARRNSRRDG MMMKLNFCFF FCRRWWAFLL LQLHMLQALA QDDVAPYFKT
EPGLPQIHLE GNRLVLTCLA EGSWPLEFKW LHNDSEITTY SSEYKYIIPA LQRSDAGFYQ
CIVRNRMGAL LQRRSEVQVA YMGNFMDANQ KKTVTEGEAA VLNFMHIFSY PRPQVTWFRD
GHKIIPSSRI AITLENQLVI LATSVADAGG YYAQAVNEKN GENKTSPLIH LSIASATDPS
DPTAPIIVIP PQNKSVVVGT SEVTLECVAS ARPVERLSIM WKRNGIKITS GISSFGRRLT
ITNPTSADVG MYFCEAKLRD STEEPARAKA FISLMVPPYF TAEPEGVILA EVEKDVDILC
QAMGVPIPSL VWYKDSVPLS KLQNPRYKVL LSGGLRIHAL RPQDAGIFQC FASNKAGEIQ
TYTYLDVTNI KPAFIQPPED TTVTEGMTAM LTCEVSGAPK PAISWKKGNQ ILASGSVQIP
RFVLLESGGL QITPVFLQDA GNYTCHAVNS EGALNAFVML TVWNRTFIVH PPENSTVIKG
TTATLRCEAT HDPRISIRYV WKKDSVVINP SSSSRITVEK DGTLLISQTW SGDIGDYTCE
VISFGGNDSR MARLEVIELP HSPQNLLATL NSSYSRSVVL SWVRPFDGNS PVLYYMVELS
ENNSPWKVHL SNLDPKMTSV TVSGLTPART YQFRVCAVNQ VGKGQYSSET SRLMLPEEPP
SAPPKNIVAS GRTNQSIMVQ WQPPPESEHN GVLHGYILRY RLAGLPGEYQ YKNITSAEIN
YCLVTDLIIW TQYEIQVASY NGAGLGAFSR PVTEYTLQGV PTAPPQNVQV EAVNSTTIQF
LWSPPPQQFI NGINQGYKLL AWPVDAPGSV TVVTIAPDFH GVHSGCITNL KKYTTYYTSV
LCFTTPGDGP RSAPQLLRTL EDKPGAVGHL SFTEILDTSL KVSWQEPVEK NGIITGYQLS
WEVYGRNESR LTRTLTNTTL EYKITGLSSL TTYTIEVAAV TAKGSGWVTS STISSGVPPE
LPGAPSNLVI SNISPRSATL QFRPGYDGKT SICKWIVEGQ VGVLGEEEEW VSLHEVDNEP
DAQMLEVPNL TPYTHYRFRM RQVNVVGASP LSQPSRVIQT LQAPPDVAPG SVSVRTASES
SLRMRWVPLP DTQYNGNPES VGYRIKFWRV DLQPSALLKV ISDRLERECT IQDLEEWTEY
ELQIQAFNAI GAGPWNEVVG VRTRESVPSA PPENVSAEAV SSTQILLTWS AVPESEQNGL
ILGYKILYKA KDLDSEPRSQ TVRGNHTQSC LLSGLRKYVL YEIRVLAFTR IGDGVPSSPV
LTERTKDDAP GPPIRLVFPE VRLTSVRIVW QPPEEPNGII LGYQIAYRLA SSSPNKFTTV
EVGSTVRQFT ATDLTPESAY IFRTSAKTRQ GWGEPLEATV ITTEKRERPA PPQQLTTPQS
DVSSRSLQLH WVPGSDGSSP IRYFTVQVRE LPNGDWQTYS SSISHEATSC IIESLNPFTS
YKLRVKATND IGDSDYSAET EAVTTLQDVP DEPPSSVLVT PHTTSSVLVQ WQPPKAESLN
GLLLGYRIYY RELDYDAGSA TESKAVKNPS ALRAELTPQS SFKTVNSSSA LTTYELTQLK
KYKRYEVLMT AYNVIGESPT STPVEVFVGE AAPAMAPQNI QVNSLSASQL ELTWDPPPAD
SQNGNIQGYK IYYWEGDVQN DTEKVKVFSS LRQLSASKNL TSHTRYLVCI SAFNAAGDGP
RSRPSAGRTH QAAPSAPSFL VFSEITSTTL NVSWGEPTAA NGVLQGYRVV YEPLAPVQGV
SKVVTVDIKG NWQRWLKVRD LTKGMTYLFR VQARTIAYGP ELQANVTAGP AEGSPGSPHE
ILVTKSASGL TVQWTEGDSG EKPTTGYIIE ARPSDEGLWD MFVKDIPRSA TSYTVSLDKL
KQGVTYEFRV VAVNEFGYGE PSVPSVAVSA QTEAPFYEEW WFLLVMALSS LILILLVVFA
LVLHGQSKKY KNCSTGKTIS NVEESVTLDN GGFTALELNS RHLNIKSTFS KKNGTRSPPR
PSPGGLHYSD EDICNKYNGA VLTEGLGLNE KPLEMSESEA TDSDYEDELP KHSFVNHYMS
DPTYYNSWKR QQKGVKHPTS YRYEECSASE TEPYFQTVIT TQSSGGVYTP TGQPAPGSRT
PVTGFSSFV
