ID CSKP_HUMAN STANDARD; PRT; 921 AA. AC O14936; O43215; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE PERIPHERAL PLASMA MEMBRANE PROTEIN CASK. GN CASK. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Liver, Lung, and Brain; RX MEDLINE=98327121; PubMed=9660868; RA Cohen A.R., Woods D.F., Marfatia S.M., Walther Z., Chishti A.H., RA Anderson J.M.; RT "Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to RT the basolateral membrane of epithelial cells."; RL J. Cell Biol. 142:129-138(1998). RN [2] RP SEQUENCE FROM N.A. RA Zha D., Hu G.; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 489-572. RX MEDLINE=98206299; PubMed=9546224; RA Daniels D.L., Cohen A.R., Anderson J.M., Bruenger A.T.; RT "Crystal structure of the hCASK PDZ domain reveals the structural RT basis of class II PDZ domain target recognition."; RL Nat. Struct. Biol. 5:317-325(1998). CC -!- FUNCTION: BIND TO CELL-SURFACE PROTEINS, INCLUDING AMYLOID CC PRECURSOR PROTEIN, NEUREXINS, AND SYNDECANS. MAY MEDIATE A LINK CC BETWEEN THE EXTRACELLULAR MATRIX AND THE ACTIN CYTOSKELETON VIA CC ITS INTERACTION WITH SYNDECAN AND WITH THE ACTIN/SPECTRIN-BINDING CC PROTEIN 4.1. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (POTENTIAL). CC -!- SIMILARITY: CONTAINS 1 PDZ/DHR DOMAIN. CC -!- SIMILARITY: CONTAINS 1 SH3 DOMAIN. CC -!- SIMILARITY: CONTAINS A GUANYLATE KINASE-LIKE DOMAIN. CC -!- SIMILARITY: BELONGS TO THE MAGUK FAMILY OF CELL JUNCTION PROTEINS. CC LIN-27/CASK SUBFAMILY. 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; AF032119; AAB88125.1; -. DR EMBL; AF035582; AAB88198.1; -. DR PDB; 1KWA; 27-MAY-98. DR MIM; 300172; -. DR InterPro; IPR000619; -. DR InterPro; IPR000719; -. DR InterPro; IPR001452; -. DR InterPro; IPR001478; -. DR Pfam; PF00625; Guanylate_kin; 1. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF00018; SH3; 1. DR Pfam; PF00069; pkinase; 1. DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS50002; SH3; 1. KW SH3 domain; Membrane; Calmodulin-binding; 3D-structure. FT DOMAIN 12 276 PROTEIN KINASE. FT DOMAIN 305 315 CALMODULIN-BINDING. FT DOMAIN 489 564 PDZ. FT DOMAIN 615 682 SH3. FT DOMAIN 734 921 GUANYLATE KINASE. FT CONFLICT 340 345 MISSING (IN REF. 2). FT CONFLICT 401 401 P -> L (IN REF. 2). FT CONFLICT 479 479 G -> D (IN REF. 2). FT CONFLICT 580 602 MISSING (IN REF. 2). FT CONFLICT 675 675 S -> P (IN REF. 2). FT CONFLICT 718 718 A -> AVFDQL (IN REF. 2). FT CONFLICT 775 775 R -> K (IN REF. 2). SQ SEQUENCE 921 AA; 104479 MW; 3A74F7D06B956892 CRC64; MADDDVLFED VYELCEVIGK GPFSVVRRCI NRETGQQFAV KIVDVAKFTS SPGLSTEDLK REASICHMLK HPHIVELLET YSSDGMLYMV FEFMDGADLC FEIVKRADAG FVYSEAVASH YMRQILEALR YCHDNNIIHR DVKPHCVLLA SKENSAPVKL GGFGVAIQLG ESGLVAGGRV GTPHFMAPEV VKREPYGKPV DVWGCGVILF ILLSGCLPFY GTKERLFEGI IKGKYKMNPR QWSHISESAK DLVRRMLMLD PAERITVYEA LNHPWLKERD RYAYKIHLPE TVEQLRKFNA RRKLKGAVLA AVSSHKFNSF YGDPPEELPD FSEDPTSSGL LAAERAVSQV LDSLEEIHAL TDCSEKDLDF LHSVFQDQHL HTLLDLYDKI NTKSSPQIRN PPSDAVQRAK EVLEEISCYP ENNDAKELKR ILTQPHFMAL LQTHDVVAHE VYSDEALRVT PPPTSPYLNG DSPESANGGM DMENVTRVRL VQFQKNTDEP MGITLKMNEL NHCIVARIMH GGMIHRQGTL HVGDEIREIN GISVANQTVE QLQKMLREMR GSITFKIVPS YRTQSSSCER DSPSTSRQSP ANGHSSTNNS VSDLPSTTQP KGRQIYVRAQ FEYDPAKDDL IPCKEAGIRF RVGDIIQIIS KDDHNWWQGK LENSKNGTAG LIPSSELQEW RVACIAMEKT KQEQQASCTW FGKKKKQYKD KYLAKHNADL VTYEEVVKLP AFKRKTLVLL GAHGVGRRHI KNTLITKHPD RFAYPIPHTT RPPKRDEENG KNYYFVSHDQ MMQDISNNEY LEYGSHEDAM YGTKLETIRK IHEQGLIAIL DVEPQALKVL RTAEFAPFVV FIAAPTITPG LNEDESLQRL QKESDILQRT YAHYFDLTII NNEIDETIRH LEEAVELVCT APQWVPVSWV Y //